PATENT ATTORNEY DOCKET: 51494-028WO2 COMPOSITIONS AND METHODS FOR THE SYNTHESIS OF BIO-BASED POLYMERS Background of the Invention Finding sustainable biomass sources that may be used for the development of new biomaterials without the need for petroleum-derived materials is an important component in developing a circular and sustainable economy. However, most of these sources are of plant origin and, therefore, compete with food production, requiring cropland, water, and harvesting. It has been recently shown that by-products of synthetic biology, particularly those recovered by distillation, may be able to play a role in developing new biomaterials, as they contain polyols compatible with biopolymer manufacture. However, such by-products are not presently suitable for use, as they are mixed with other degradation by-products, making their use impractical. Accordingly, the valorization of secondary materials from fermentation processes represents an opportunity to access valuable starting materials for the development of novel, bio-based polymers with useful properties. These bio-based polymers can be applied in many fields, such as packaging, automotive coatings and/or adhesives, biomedical devices, and household products, among others. However, to access these resources, there remains a need for physical and chemical processes that are capable of converting secondary materials, such as those from a fermentation mixture, to precursors suitable for downstream synthesis of bio-based polymers. Summary of the Invention The present disclosure provides compositions and methods for synthesizing bio-based polymers (e.g., polyurethanes and polyesters), particularly from a residue (e.g., distillate residue) produced as a by-product of host cells (e.g., yeast cells) capable of producing a fermentation product. The compositions and methods described herein advance the field of synthetic biology in an important way, providing processes that utilize by-products of fermentation for the sustainable synthesis of new materials. This ability is particularly advantageous, as by-products of fermentation are ordinarily discarded as waste. Using the compositions and methods of the disclosure, these by-products can be utilized in a manner that produces bio-based polymers. The present disclosure is based, in part, on the discovery of a series of physical and chemical processes capable of harnessing by-products of fermentation and utilizing these materials for the synthesis of bio-based polymers. The sections that follow provide a description of these physical and chemical processes, the intermediates resulting therefrom, and the bio-based polymers that can be obtained using this methodology. In a first aspect, the disclosure provides a method of synthesizing a polymer from a fermentation composition that has been produced by culturing a population of host cells capable of producing a fermentation product in a culture medium and under conditions suitable for the host cells to produce the fermentation product. In some embodiments, the method comprises an epoxide synthesis step in which a residue from a fermentation composition is reacted with an epoxidation agent, thereby producing an epoxide. In some embodiments, the method further comprises a ring- opening step in which the epoxide is reacted with a ring-opening agent, thereby producing a monomer PATENT ATTORNEY DOCKET: 51494-028WO2 product. In some embodiments, the epoxide synthesis step comprises a pretreatment of the distillate residue from the fermentation composition prior to reacting the residue with the epoxidation agent. PRETREATMENT In some embodiments, the pretreatment step comprises a winterization step and/or a filtration step. In some embodiments, the winterization step comprises dissolving the residue from the fermentation composition in ethanol, thereby forming an ethanol solution. In some embodiments the ethanol is added to a concentration of 4;1 (wt.) of residue from the fermentation composition to ethanol. In some embodiments, the ethanol solution is mixed for between about 1 minute and about 1 hour (e.g., between about 1 minute and 45 minutes, about 1 minute and 30 minutes, 1 minute and 15 minutes, 15 minutes and 1 hour, 30 minutes and 1 hour, or 45 minutes and 1 hour). In some embodiments, the ethanol solution is mixed for between about 1 minute and about 20 minutes (e.g., about 1 minute, 2 minutes, 3 minutes, 4 minutes, 5 minutes, 6 minutes, 7 minutes, 8 minutes, 9 minutes, 10 minutes, 11 minutes, 12 minutes, 13 minutes, 14 minutes, 15 minutes, 16 minutes, 17 minutes, 18 minutes, 19 minutes, or 20 minutes). In some embodiments, the ethanol solution is mixed for about 5 minutes. In some embodiments, the ethanol solution is let stand for between about 10 minutes and about 6 hours (e.g., between about 10 minutes and 5 hours, 10 minutes and 4 hours, 10 minutes and 3 hours, 10 minutes and 2 hours, 10 minutes and 1 hour, 10 minutes and 30 minutes, 30 minutes and 6 hours, 1 hour and 6 hours, 2 hours and 6 hours, 3 hours and 6 hours, 4 hours and 6 hours, or 5 hours and 6 hours). In some embodiments, the ethanol solution is let stand for between about 1 hour and about 3 hours (e.g., between about 1 hour and 2 hours, 1 hour and 1.5 hours, 1.5 hours and 3 hours, 2 hours and 3 hours, or 2.5 hours and 3 hours). In some embodiments, the ethanol solution is let stand for about 2 hours. In some embodiments, the ethanol solution is let stand at about room temperature. In some embodiments, the ethanol solution is chilled for between about 1 hour and about 24 hours (e.g., between about 1 hour and about 18 hours, about 1 hour and 12 hours, 1 hour and 6 hours, 6 hours and 24 hours, 12 hours and 24 hours, or 18 hours and 24 hours). In some embodiments, the ethanol solution is chilled for between about 8 hours and about 16 hours (e.g., about 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 13 hours, 14 hours, 15 hours, or 16 hours). In some embodiments, the ethanol solution is chilled at a temperature of between about -50 ^o C and about 0 ^o C (e.g., between about -50 ^o C and -10 ^o C, -50 ^o C and -20 ^o C, -50 ^o C and -30 ^o C, -50 ^o C and -40 ^o C, -40 ^o C and 0 ^o C, -30 ^o C and 0 ^o C, -20 ^o C and 0 ^o C, or -10 ^o C and 0 ^o C). In some embodiments, the ethanol solution is chilled at a temperature of between about-40 ^o C and about -20 ^o C (e.g., about -40 ^o C, -39 ^o C, -38 ^o C, -37 ^o C, -36 ^o C, -35 ^o C, -34 ^o C, -33 ^o C, -32 ^o C, -31 ^o C, -30 ^o C, - 29 ^o C, -28 ^o C, -27 ^o C, -26 ^o C, -25 ^o C, -24 ^o C, -23 ^o C, -22 ^o C, -21 ^o C, or -20 ^o C). In some embodiments, the ethanol solution is chilled to a temperature of about -30 ^o C. In some embodiments, the winterization step further comprises centrifugation of the ethanol solution. In some embodiments, the ethanol solution is centrifuged at a speed of between about 500 g to about 2000 g (e.g., between about 750 g and 2000 g, 1000 g and 2000 g, 1250 g and 2000 g, 1500 g and 2000 g, 1750 g and 2000 g, 500 g and 1750 g, 500 g and 1500 g, 500 g and 1250 g, 500 PATENT ATTORNEY DOCKET: 51494-028WO2 g and 1000 g, or 500 g and 750 g). In some embodiments, the ethanol solution is centrifuged at a speed of between about 1000 g to about 1500 g (e.g., between about 1100 g and 1500 g, 1200 g and 1500 g, 1300 g and 1500 g, 1400 g and 1500 g, 1000 g and 1400 g, 1000 g and 1300 g, 1000 g and 1200 g, or 1000 g and 1100 g). In some embodiments, the ethanol solution is centrifuged at a speed of about 1250 g. In some embodiments, the ethanol solution is centrifuged for between about 1 minute and about 30 minutes (e.g., between about 1 minute and 25 minutes, 1 minute and 20 minutes, 1 minute and 15 minutes, 1 minute and 10 minutes, 1 minute and 5 minutes, 5 minutes and 30 minutes, 10 minutes and 30 minutes, 15 minutes and 30 minutes, 20 minutes and 30 minutes, or 25 minutes and 30 minutes). In some embodiments, the ethanol solution is centrifuged at about room temperature. In some embodiments, the filtration comprises at least 2 filtration steps. In some embodiments, the method includes between 2 and 5 filtration steps (e.g., 2 filtration steps, 3 filtration steps, 4 filtration steps, or 5 filtration steps). In some embodiments, the method includes a first filtration step, a second filtration step, and a third filtration step. In some embodiments, the first filtration step comprises filtering the residue from a fermentation composition through a nonwoven (TNT) filter. In some embodiments, the second filtration step comprises filtering through a filter having a membrane that is between 5 µm and 15 µm in pore size (e.g., 5 µm, 6 µm, 7 µm, 8 µm, 9 µm, 10 µm, 11 µm, 12 µm, 13 µm, 14 µm, or 15 µm in pore size). In some embodiments, the membrane is about 11 µm in pore size. In some embodiments, the third filtration step comprises filtering through a filter having a membrane that is between 5 µm and 15 µm in pore size (e.g., 5 µm, 6 µm, 7 µm, 8 µm, 9 µm, 10 µm, 11 µm, 12 µm, 13 µm, 14 µm, or 15 µm in pore size). In some embodiments, the membrane is about 8 µm in pore size. In some embodiments, the filtration may be performed under pressure. EPOXIDATION: OXIRANE-RING FORMATION In some embodiments, the epoxidation agent comprises performic acid or hydrogen peroxide, optionally mixed with ethyl acetate and/or formic acid. In some embodiments, the ethyl acetate has a final concentration of between about 10% (w/w) and about 60% (w/w) (e.g., between about 10% (w/w) and 50% (w/w), 10% (w/w) and 40% (w/w), 10% (w/w) and 30% (w/w), 10% (w/w) and 20% (w/w), 20% (w/w) and 60% (w/w), 30% (w/w) and 60% (w/w), 40% (w/w) and 60% (w/w), or 50% (w/w) and 60% (w/w)). In some embodiments, the ethyl acetate has a final concentration of between about 20% (w/w) and about 40% (w/w). In some embodiments, the ethyl acetate has a final concentration of about 32% (w/w). In some embodiments, the performic acid has a final concentration of between about 1% (w/w) and about 10% (w/w) (e.g., about 1% (w/w), 2% (w/w), 3% (w/w), 4% (w/w), 5% (w/w), 6% (w/w), 7% (w/w), 8% (w/w), 9% (w/w), or 10% (w/w)). In some embodiments, the performic acid has a final concentration of between about 2% (w/w) and about 5% (w/w) (e.g., about 2% (w/w), 3% (w/w), 4% (w/w), or 5% (w/w)). In some embodiments, the performic acid has a final concentration of between about 3% (w/w) and about 4% (w/w). In some embodiments, the formic acid has a final concentration of between about 2% (w/w) and about 5% (w/w) (e.g., about 2% (w/w), PATENT ATTORNEY DOCKET: 51494-028WO2 3% (w/w), 4% (w/w), or 5% (w/w)). In some embodiments, the formic acid has a final concentration of between about 3% (w/w) and about 4% (w/w). In some embodiments, the epoxide synthesis step further comprises contacting the residue from a fermentation composition, ethyl acetate, and formic acid with hydrogen peroxide. In some embodiments, the hydrogen peroxide is refrigerated hydrogen peroxide. In some embodiments, the hydrogen peroxide has a final concentration of between about 25% (w/w) and about 75% (w/w) (e.g., between about 35% (w/w) and about 75% (w/w), 45% (w/w) and 75% (w/w), 55% (w/w) and 75% (w/w), 65% (w/w) and 75% (w/w), 25% (w/w) and 65% (w/w), 25% (w/w) and 55% (w/w), 25% (w/w) and 45% (w/w), or 25% (w/w) and 35% (w/w)). In some embodiments, the hydrogen peroxide has a final concentration of between about 40% (w/w) and about 60% (w/w) (e.g., between about 40% (w/w) and 55% (w/w), 40% (w/w) and 50% (w/w), 40% (w/w) and 45% (w/w), 45% (w/w) and 60% (w/w), 50% (w/w) and 60% (w/w), or 55% (w/w) and 60% (w/w)). In some embodiments, the hydrogen peroxide has a final concentration of about 50% (w/w). In some embodiments, the epoxide synthesis step is performed at between about 50 ^o C and about 125 ^o C (e.g., between about 50 ^o C and 100 ^o C, about 50 ^o C and 75 ^o C, about 75 ^o C and 125 ^o C, or about 100 ^o C and 125 ^o C). In some embodiments, the epoxide synthesis step is performed at between about 70 ^o C and about 100 ^o C (e.g., between about 70 ^o C and 90 ^o C, about 70 ^o C and 80 ^o C, about 80 ^o C and 100 ^o C, or about 90 ^o C and 100 ^o C). In some embodiments, the epoxide synthesis step is performed at about 85 ^o C. In some embodiments, the epoxide synthesis step is run for between about 30 minutes and about 6 hours (e.g., between about 30 minutes and about 5 hours, about 30 minutes and about 4 hours, about 30 minutes and about 3 hours, about 30 minutes and 2 hours, about 30 minutes and 1 hour, about 1 hour and about 6 hours, about 2 hours and about 6 hours, about 3 hours and about 6 hours, about 4 hours and about 6 hours, or about 5 hours and about 6 hours). In some embodiments, the epoxide synthesis step is run for between about 1 hour and about 4 hours (e.g., between about 1 hour and 3 hours, about 1 hour and 2 hours, about 2 hours and 4 hours, or about 3 hours and 4 hours). In some embodiments, the epoxide synthesis step is run for between about 2 hours and about 4 hours (e.g., about 2 hours, about 3 hours, or about 4 hours. In some embodiments, the epoxide synthesis step is run for about 3 hours. OPENING RING-STEP: HYDROXYLATION In some embodiments, the ring-opening step comprises contacting the epoxide product with the ring-opening agent. In some embodiments, the ring-opening agent comprises castor oil. In some embodiments, the castor oil has a final concentration of between about 10% (w/w) and about 50% (w/w) (e.g., between about 10% (w/w) and about 40% (w/w), about 10% (w/w) and 30% (w/w), about 10% (w/w) and 20% (w/w), about 20% (w/w) and about 50% (w/w), about 30% (w/w) and about 50% (w/w), or about 40% (w/w) and about 50% (w/w)). In some embodiments, the castor oil has a final concentration of between about 20% (w/w) and about 35% (w/w) (e.g., about 20% (w/w), 21% (w/w), 22% (w/w), 23% (w/w), 24% (w/w), 25% (w/w), 26% (w/w), 27% (w/w), 28% (w/w), 29% (w/w), 30% (w/w), 31% (w/w), 32% (w/w), 33% (w/w), 34% (w/w), or 35% (w/w)). In some embodiments, the castor oil has a final concentration of about 25% (w/w). PATENT ATTORNEY DOCKET: 51494-028WO2 In some embodiments, the ring-opening step is performed at a temperature of between about 100 ^o C and about 225 ^o C (e.g., between about 100 ^o C and about 200 ^o C, about 100 ^o C and about 175 ^o C, about 100 ^o C and about 150 ^o C, about 100 ^o C and about 125 ^o C, about 125 ^o C and about 225 ^o C, about 150 ^o C and about 225 ^o C, about 175 ^o C and about 225 ^o C, or about 200 ^o C and about 225 ^o C). In some embodiments, the ring-opening step is performed at a temperature of between about 140 ^o C and about 180 ^o C (e.g., between about 140 ^o C and about 170 ^o C, about 140 ^o C and about 160 ^o C, about 140 ^o C and about 150 ^o C, about 150 ^o C and about 180 ^o C, about 160 ^o C and about 180 ^o C, or about 170 ^o C and about 180 ^o C). In some embodiments, the ring-opening step is performed at a temperature of about 160 ^o C. In some embodiments, the ring-opening step is performed for between about 2 hours and about 12 hours (e.g., between about 2 hours and about 10 hours, about 2 hours and about 8 hours, about 2 hours and about 6 hours, about 2 hours and about 4 hours, about 4 hours and about 12 hours, about 6 hours and about 12 hours, about 8 hours and about 12 hours, or about 10 hours and about 12 hours). In some embodiments, the ring-opening step is performed for between about 5 hours and about 10 hours (e.g., between about 5 hours and about 8 hours, between about 5 hours and about 6 hours, about 6 hours and about 10 hours, or about 8 hours and about 10 hours). In some embodiments, the ring-opening step is performed between about 6 hours and about 7 hours. In some embodiments, the ring-opening step is performed under a nitrogen purge. In some embodiments, the ring-opening agent comprise phosphoric acid. In some embodiments, the phosphoric acid has a final concentration of between about 5% (w/w) and about 20% (w/w) (e.g., between about 5% (w/w) and about 15% (w/w), about 5% (w/w) and about 10% (w/w), about 10% (w/w) and about 20% (w/w), or about 15% (w/w) and about 20% (w/w)). In some embodiments, the phosphoric has a final concentration of about 9% (w/w). In some embodiments, the ring-opening step is performed at a temperature of between about 60 ^o C and about 100 ^o C (e.g., between about 60 ^o C and about 90 ^o C, about 60 ^o C and about 80 ^o C, about 60 ^o C and about 70 ^o C, about 70 ^o C and about 100 ^o C, about 80 ^o C and about 100 ^o C, or about 90 ^o C and about 100 ^o C). In some embodiments, the ring-opening step is performed at a temperature of between about 75 ^o C and about 90 ^o C (e.g., between about 75 ^o C and about 85 ^o C, about 75 ^o C and about 80 ^o C, about 80 ^o C and about 90 ^o C, or about 85 ^o C and about 90 ^o C). In some embodiments, the ring-opening step is performed at a temperature of about 85 ^o C. In some embodiments, the ring-opening step comprises stirring the epoxide and the ring- opening agent for between about 10 minutes and about 4 hours (e.g., between about 10 minutes and 3 hours, about 10 minutes and 2 hours, about 10 minutes and 1 hour, about 1 hour and about 4 hours, about 2 hours and about 4 hours, or about 3 hours and about 4 hours). In some embodiments, the ring-opening step comprises stirring the epoxide and the ring-opening agent for between about 30 minutes and about 2 hours (e.g., between about 30 minutes and about 1.5 hours, about 30 minute and about 1 hour, about 1 hour and about 2 hours, or about 1.5 hours and about 2 hours). In some embodiments, the ring-opening step comprises stirring the epoxide and the ring-opening agent for about 1 hour. In some embodiments, the monomer product is washed with carbonate. In some embodiments, the carbonate is calcium or sodium carbonate. In some embodiments, the carbonate PATENT ATTORNEY DOCKET: 51494-028WO2 has a concentration of between about 1% (w/w) and about 20 % (w/w) (e.g., between about 1% (w/w) and about 15% (w/w), about 1% (w/w) and about 10% (w/w), about 1% (w/w) and about 5% (w/w), about 5% (w/w) and about 20% (w/w), about 10% (w/w) and about 20% (w/w), or about 15% (w/w) and about 20% (w/w)). In some embodiments, the carbonate has a concentration of between about 5% (w/w) and about 15% (w/w) (e.g., between about 5% (w/w) and about 12% (w/w), about 5% (w/w) and about 7% (w/w), about 7% (w/w) and about 15% (w/w), or about 12% (w/w) and about 15% (w/w)). In some embodiments, the carbonate has a concentration of about 10% (w/w). In some embodiments, after the monomer product is washed with carbonate, the monomer product is washed with distilled water. In some embodiments, after the monomer product is washed with carbonate, the monomer product is washed at least twice with distilled water. In some embodiments, the ring-opening agent comprises a polyol, optionally wherein the polyol is glycerol. In some embodiments, the glycerol has a final concentration of between about 5% (w/w) and about 40% (w/w) (e.g., between about 5% (w/w) and about 30 % (w/w), about 5% (w/w) and about 20% (w/w), about 5% (w/w) and about 10% (w/w), about 10% (w/w) and about 40 % (w/w), about 20% (w/w) and about 40% (w/w), or about 30% (w/w) and about 40% (w/w)). In some embodiments, the glycerol has a final concentration of between about 15% (w/w) and about 30% (w/w) (e.g., about 15% (w/w), 16% (w/w), 17% (w/w), 18% (w/w), 19% (w/w), 20% (w/w), 21% (w/w), 22% (w/w), 23% (w/w), 24% (w/w), 25% (w/w), 26% (w/w), 27% (w/w), 28% (w/w), 29% (w/w), or 30% (w/w)). In some embodiments, the glycerol has a final concentration of about 20% (w/w). In some embodiments, the ring-opening step further comprises tetrafluoroboric acid. In some embodiments, the tetrafluoroboric acid has a final concentration of between about 0.01% (w/w) and about 0.1% (w/w) (e.g., about 0.01% (w/w), 0.02% (w/w), 0.03% (w/w), 0.04% (w/w), 0.05% (w/w), 0.06% (w/w), 0.07% (w/w), 0.08% (w/w), 0.09% (w/w), or 0.1% (w/w)). In some embodiments, the tetrafluoroboric acid has a final concentration of about 0.05% (w/w). In some embodiments, the ring-opening step is performed for between about 2 hours and about 10 hours (e.g., between about 2 hours and about 8 hours, about 2 hours and about 6 hours, about 2 hours and about 4 hours, about 4 hours and about 10 hours, about 6 hours and about 10 hours, or about 8 hours and about 10 hours). In some embodiments, the ring-opening step is performed for between about 4 hours and about 8 hours (e.g., between about 4 hours and about 7 hours, about 4 hours and about 6 hours, about 4 hours and about 5 hours, about 5 hours and about 8 hours, about 6 hours and about 8 hours, or about 7 hours and about 8 hours). In some embodiments, the ring-opening step is performed for about 6 hours. In some embodiments, the ring-opening step is performed at a temperature of between about 40 ^o C and about 80 ^o C (e.g., between about 40 ^o C and about 70 ^o C, about 40 ^o C and about 60 ^o C, about 40 ^o C and about 50 ^o C, about 50 ^o C and about 80 ^o C, about 60 ^o C and about 80 ^o C, or about 70 ^o C and about 80 ^o C). In some embodiments, the ring-opening step is performed at a temperature of between about 30 ^o C and about 70 ^o C (e.g., between about 30 ^o C and about 60 ^o C, about 30 ^o C and about 50 ^o C, about 30 ^o C and about 40 ^o C, about 40 ^o C and about 70 ^o C, about 50 ^o C and about 70 ^o C, or about 60 ^o C and about 70 ^o C). In some embodiments, the ring-opening step is performed at a PATENT ATTORNEY DOCKET: 51494-028WO2 temperature of about 60 ^o C. In some embodiments, the ring-opening step is performed with constant stirring. In some embodiments, the monomer product is hydroxylated. In some embodiments, the monomer product is a polyol. POLYESTER-POLYHYDROXYURETHANE (PHU) POLYMERS In some embodiments, the method further comprises a polyester-polyhydroxyurethane synthesis reaction comprising (i.e., a reaction that produces a polyester product or a polyhydroxyurethane product): (i) a transcarbonation reaction step, (ii) an aminolysis reaction step, optionally wherein the aminolysis reaction step produces an aminolysis reaction step product, and (iii) an esterification step. In some embodiments, the transcarbonation reaction step comprises contacting the monomer product with dimethyl carbonate and sodium carbonate. In some embodiments, the dimethyl carbonate has a final concentration of between about 10% (w/w) and about 50% (w/w) (e.g., between about 10% (w/w) and about 40 % (w/w), about 10% (w/w) and about 30% (w/w), about 10% (w/w) and about 20% (w/w), about 20% (w/w) and about 50% (w/w), about 30% (w/w) and about 50% (w/w), or about 40% (w/w) and about 50% (w/w)). In some embodiments, the dimethyl carbonate has a final concentration of between about 35% (w/w) and about 45% (w/w) (e.g., about 35% (w/w), 36% (w/w), 37% (w/w), 38% (w/w), 39% (w/w), 40% (w/w), 41% (w/w), 42 % (w/w), 43% (w/w), 44% (w/w), or 45% (w/w)). In some embodiments, the sodium carbonate has a final concentration of between about 0.01% (w/w) and about 0.1% (w/w) (e.g., about 0.01% (w/w), 0.02% (w/w), 0.03% (w/w), 0.04% (w/w), 0.05% (w/w), 0.06% (w/w), 0.07% (w/w), 0.08% (w/w), 0.09% (w/w), or 0.1% (w/w)). In some embodiments, the sodium carbonate has a final concentration of about 0.05% (w/w). In some embodiments, the transcarbonation reaction is performed in a reactor coupled with a condenser. In some embodiments, the transcarbonation reaction is performed under reflux conditions for between about 30 minutes and about 4 hours (e.g., between about 30 minutes and about 3 hours, about 30 minutes and about 2 hours, about 30 minutes and about 1 hour, about 1 hour and about 4 hours, about 2 hours and about 4 hours, or about 3 hours and about 4 hours). In some embodiments, the transcarbonation reaction is performed under reflux conditions for between about 1 hour and about 3 hours. (e.g., between about 1 hour and about 3 hours, about 1 hour and about 2 hours, or about 2 hours and about 3 hours). In some embodiments, the transcarbonation reaction is performed under reflux conditions for about 2 hours. In some embodiments, the transcarbonation reaction is refluxed at a temperature of between about 50 ^o C and about 100 ^o C (e.g., about 50 ^o C and about 90 ^o C, about 50 ^o C and about 80 ^o C, about 50 ^o C and about 70 ^o C, about 50 ^o C and about 60 ^o C, about 60 ^o C and about 100 ^o C, about 70 ^o C and about 100 ^o C, about 80 ^o C and about 100 ^o C, or about 90 ^o C and about 100 ^o C). In some embodiments, the transcarbonation reaction is performed under reflux conditions at a temperature of about 75 ^o C. In some embodiments, after the transcarbonation reaction, the transcarbonation reaction is cooled to about room temperature. In some embodiments, after the transcarbonation reaction is cooled, the transcarbonation reaction suspension is centrifuged to isolate a lighter organic phase as a transcarbonation reaction PATENT ATTORNEY DOCKET: 51494-028WO2 product. In some embodiments, the polyhydroxyurethane synthesis reaction comprises contacting the transcarbonation reaction product, a cyclic carbonate, and a cycloaliphatic amine to produce a polyhydroxyurethane synthesis product. In some embodiments, the cyclic carbonate comprises polyalkyl glycidate carbonate. In some embodiments, the cycloaliphatic amine comprises isophorone. In some embodiments, the polyhydroxyurethane synthesis reaction comprises mixing the transcarbonation reaction product, a cyclic carbonate, and a cycloaliphatic amine for between about 1 hour and about 4 hours (e.g., between about 1 hour and about 3 hours, about 1 hour and about 2 hours, about 2 hours and about 4 hours, or about 3 hours and about 4 hours). In some embodiments, the polyhydroxyurethane synthesis reaction comprises mixing the transcarbonation reaction product, a cyclic carbonate, and a cycloaliphatic amine for about 2 hours. In some embodiments, the polyhydroxyurethane synthesis reaction comprises mixing the transcarbonation reaction product, a cyclic carbonate, and a cycloaliphatic amine at a temperature of between about 30 ^o C and about 70 ^o C (e.g., between about 30 ^o C and about 60 ^o C, about 30 ^o C and about 50 ^o C, about 30 ^o C and about 40 ^o C, about 40 ^o C and about 70 ^o C, about 50 ^o C and about 70 ^o C, or about 60 ^o C and about 70 ^o C). In some embodiments, the polyhydroxyurethane synthesis reaction comprises mixing the transcarbonation reaction product, a cyclic carbonate and a cycloaliphatic amine at a temperature of 50 ^o C. In some embodiments, the polyester-polyhydroxyurethane synthesis reaction comprises contacting the aminolysis step reaction product with phthalic acid, citric acid, and 1,4 – butanediol, thereby producing a polyhydroxyurethane product. In some embodiments, the polyhydroxyurethane synthesis product, phthalic acid, citric acid, and butanediol are present in a ratio of 3:4.5:0.5:0.5. In some embodiments, the polyester-polyhydroxyurethane synthesis reaction comprises contacting the aminolysis step reaction product with phthalic acid, citric acid, and 1,4 - butanediol for between about 1 hour and about 4 hours (e.g., between about 1 hour and about 3 hours, about 1 hour and about 2 hours, about 2 hours and about 4 hours, or about 3 hours and about 4 hours). In some embodiments, the polyester-polyhydroxyurethane synthesis reaction comprises contacting the aminolysis step reaction product with phthalic acid, citric acid, and 1,4 - butanediol for about 2 hours. In some embodiments, the polyester-polyhydroxyurethane synthesis reaction comprises contacting the aminolysis step reaction product with phthalic acid, citric acid, and butanediol at a temperature of between about 120 ^o and about 200 ^o C (e.g., between about 120 ^o C and about 180 ^o C, about 120 ^o C and about 160 ^o C, about 120 ^o C and about 140 ^o C, about 140 ^o C and about 200 ^o C, about 160 ^o C and about 200 ^o C, or about 180 ^o C and about 200 ^o C). In some embodiments, the polyester-polyhydroxyurethane synthesis reaction comprises contacting the aminolysis step reaction product with phthalic acid, citric acid, and butanediol at a temperature of about 160 ^o C. In some embodiments, the polyester-polyhydroxyurethane synthesis reaction is performed under nitrogen. SYNTHESIS OF POLYURETHANE FOAMS In some embodiments, the method further comprises a polyurethane synthesis reaction, by a two-step reaction comprising (a) a prepolymer synthesis step, wherein the monomer product is PATENT ATTORNEY DOCKET: 51494-028WO2 contacted with a dicarboxylic acid, a cross-linker, chain extender, an emulsifier, a catalyst, a blowing agent, and optionally sugarcane bagasse ash, thereby producing a prepolymer reaction product and (b) a second-step reaction comprising contacting the prepolymer reaction product with an isocyanate, thereby producing a polyurethane synthesis product. In some embodiments, the prepolymer synthesis step is performed by mixing together and melting the monomer product, the blowing agent, the chain-extender, the catalyst, and the emulsifier. In some embodiments, the prepolymer synthesis step is performed by mixing together the monomer product, the blowing agent, the chain-extender, the catalyst, and the emulsifier, together for between about 5 seconds and about 20 seconds (e.g., between about 5 seconds and 15 seconds, 5 seconds and 10 seconds, 10 seconds and 20 seconds, or 15 seconds and 20 seconds). In some embodiments, the isocyanate is added after mixing together the monomer product, the blowing agent, the chain-extender, the catalyst, and the emulsifier to produce the prepolymer product. In some embodiments, the polyurethane synthesis product is dried at about room temperature. In some embodiments, the chain extender comprises glycerol. In some embodiments, the glycerol has a final concentration of between about 10% (w/w) and about 30% (w/w) (e.g., between about 10% (w/w) and about 25% (w/w), about 10% (w/w) and about 20% (w/w), about 10% (w/w) and about 15% (w/w), about 15% (w/w) and about 30% (w/w), about 20% (w/w) and about 30% (w/w), or about 25% (w/w) and about 30% (w/w)). In some embodiments, the glycerol has a final concentration of between about 15% (w/w) and about 20% (w/w) (e.g., about 15% (w/w), 16% (w/w), 17% (w/w), 18% (w/w), 19% (w/w), or 20% (w/w)). In some embodiments, the glycerol has a final concentration of between about 18% (w/w) and about 19% (w/w). In some embodiments, the catalyst comprises dibutyltin dilaurate. In some embodiments, the dibutyltin dilaurate has a final concentration of between about 1% (w/w) and about 5% (w/w) (e.g., between about 1% (w/w) and about 4% (w/w), about 1% (w/w) and about 3% (w/w), about 1% (w/w) and about 2% (w/w), about 2% (w/w) and about 5% (w/w), about 3% (w/w) and about 5% (w/w), or about 4% (w/w) and about 5% (w/w)). In some embodiments, the dibutyltin dilaurate has a final concentration of between about 2% (w/w) and about 3% (w/w), optionally wherein the dibutyltin dilaurate has a final concentration of about 2.72% (w/w). In some embodiments, the emulsifier comprises polydimethylsiloxane. In some embodiments, the polydimethylsiloxane has a final concentration of between about 0.1% (w/w) and about 5% (w/w) (e.g., between about 0.1% (w/w) and about 4% (w/w), about 0.1% (w/w) and about 3% (w/w), about 0.1% (w/w) and about 2% (w/w), about 0.1% (w/w) and about 1% (w/w), about 1% (w/w) and about 5% (w/w), about 2% (w/w) and about 5% (w/w), about 3% (w/w) and about 5% (w/w), or about 4% (w/w) and about 5% (w/w). In some embodiments, the polydimethylsiloxane has a final concentration of between about 0.5% (w/w) and about 3% (w/w). In some embodiments, wherein the sugarcane bagasse ash was previously heated to a temperature of between about 400 ^o C and about 800 ^o C (e.g., between about 400 ^o C and 700 ^o C, about 400 ^o C and 600 ^o C, about 400 ^o C and 500 ^o C, about 500 ^o C and 800 ^o C, about 600 ^o C and 800 ^o C, or about 700 ^o C and 800 ^o C). In some embodiments, the sugarcane bagasse ash was previously PATENT ATTORNEY DOCKET: 51494-028WO2 heated to a temperature of about 600 ^o C. In some embodiments, the sugarcane bagasse ash was previously heated at a rate of between about 5 ^o C/min and about 20 ^o C/min (e.g., between about 5 ^o C/min and 15 ^o C/min, about 5 ^o C/min and about 10 ^o C/min, about 10 ^o C/min and 20 ^o C/min, or about 15 ^o C/min and 20 ^o C/min). In some embodiments, the sugarcane bagasse ash was previously heated at a rate of about 10 ^o C/min. In some embodiments, the sugarcane bagasse ash was previously heated for between about 1 hour and about 10 hours (e.g., about 1 hour and about 8 hours, about 1 hour and about 6 hours, about 1 hour and about 4 hours, about 1 hour and about 2 hours, about 2 hours and about 10 hours, about 4 hours and about 10 hours, about 6 hours and about 10 hours, or about 8 hours and about 10 hours). In some embodiments, the sugarcane bagasse ash was previously heated for about 5 hours. In some embodiments, the sugarcane bagasse ash is cooled to room temperature. In some embodiments, after the sugarcane bagasse ash is cooled to room temperature, the sugarcane bagasse ash is contacted with a few drops of hydrogen peroxide. In some embodiments, after the sugarcane bagasse ash is contacted with a few drops of hydrogen peroxide, it is heated to about 600 ^o C. In some embodiments, the sugarcane bagasse ash and hydrogen peroxide are heated to about 600 ^o C for about 5 hours, and then cooled to room temperature. In some embodiments, the polyurethane synthesis step has a final concentration of sugarcane bagasse ash of between about 2% (w/w) and about 10% (w/w) (e.g., between about 2% (w/w) and about 8% (w/w), about 2% (w/w) and about 6% (w/w), about 2% (w/w) and about 4% (w/w), about 4% (w/w) and about 10% (w/w), about 6% (w/w) and about 10% (w/w), or about 8% (w/w) and about 10% (w/w). In some embodiments, the polyurethane synthesis step has a final concentration of sugarcane bagasse ash of about 4.5% (w/w). In some embodiments, the isocyanate comprises one or more of toluene diisocyanate (TDI), methylenediphenyl diisocyanate (MDI), hexamethylene diisocyanate (HDI), or isophorone diisocyanate (IPDI). In some embodiments, the isocyanate comprises MDI. In some embodiments, the MDI comprises 4,4’-MDI. In some embodiments, the isocyanate has a final concentration of between about 25% (w/w) and about 75% (w/w) (e.g., between about 35% (w/w) and 75% (w/w), 45% (w/w) and 75% (w/w), 55% (w/w) and 75% (w/w), 65% (w/w) and 75% (w/w), 25% (w/w) and 65% (w/w), 25% (w/w) and 55% (w/w), 25% (w/w) and 45% (w/w), or 25% (w/w) and 35% (w/w)). In some embodiments, the isocyanate has a final concentration of between about 50% (w/w) and about 60% (w/w) (e.g., about 50% (w/w), 51% (w/w), 52% (w/w), 53% (w/w), 54% (w/w), 55% (w/w), 56% (w/w), 57% (w/w), 58% (w/w), 59% (w/w), or 60% (w/w)). In some embodiments, the blowing agent is water. In some embodiments, the water has a final concentration of between about 0.5% (w/w) and about 5% (w/w) (e.g., between about 1% (w/w) and 5% (w/w), 2% (w/w) and 5% (w/w), 3% (w/w) and 5% (w/w), 4% (w/w) and 5% (w/w), 0.5% (w/w) and 4% (w/w), 0.5% (w/w) and 3% (w/w), 0.5% (w/w) and 2% (w/w), or 0.5% (w/w) and 1% (w/w)). In some embodiments, the water has a final concentration of between about 1% (w/w) and about 3% (w/w) (e.g., about 1% (w/w), 2% (w/w), or 3% (w/w)). POLYESTER SYNTHESIS PATENT ATTORNEY DOCKET: 51494-028WO2 The method described herein may further include a polyester synthesis step. The polyester synthesis step may include reacting the monomer product with a dicarboxylic acid, a cross-linker, and a chain extender. The polyester synthesis step may be performed by melting the monomer product with the dicarboxylic acid, cross-linker, chain extender, and mechanical enhancer using heat. For example, in the polyester synthesis step, the monomer product may be reacted with a dicarboxylic acid, a cross-linker, chain extender, thereby producing a polyester product. The monomer product and the dicarboxylic acid may be present at a ratio of between about 2:1 (w/w) and about 1:2 (w/w) (e.g., between about 2:1 (w/w) and 1:1 (w/w) or between 1:1 and about 1:2 (w/w)). In some embodiments, the monomer product and the dicarboxylic acid are present at a ratio of about 3:2 (w/w). The monomer product and the cross-linker may be present at a ratio of between about 4:1 (w/w) and about 1:2 (w/w) (e.g., about 4:1 (w/w) and about 1:1 (w/w), about 4:1 (w/w) and about 2:1 (w/w), about 4:1 (w/w) and about 3:1 (w/w), about 3:1 (w/w) and about 1:2 (w/w), about 2:1 (w/w) and about 1:2 (w/w), or about 1:1 (w/w) and about 1:2 (w/w)). In some embodiments, the monomer product and the cross-linker are present at a ratio of about 2:1 (w/w). The monomer product and the chain extender may be present at a ratio of between about 4:1 (w/w) and about 1:1 (w/w) (e.g., between about 4:1 (w/w) and about 2:1 (w/w), about 4:1 (w/w) and about 3:1 (w/w), about 3:1 (w/w) and about 1:1 (w/w), or about 2:1 (w/w) and about 1:1 (w/w)). For example, the monomer product and the chain extender may be present at a ratio of about 3:1 (w/w). The dicarboxylic acid may be, for example, azelaic acid or phthalic acid. In some embodiments, the dicarboxylic acid is phthalic acid. The cross-linker may be citric acid. The chain extender may be 1,4-butanediol, sorbitol, or glycerol. In some embodiments, the chain extender is 1,4-butanediol and sorbitol. In some embodiments, the dicarboxylic acid, cross-linker, and chain extender are mixed for between 10 minutes and 2 hours (e.g., between 10 minutes and 90 minutes, 10 minutes and 60 minutes, 10 minutes and 30 minutes, 30 minutes and 2 hours, 1 hour and 2 hours, 90 minutes and 2 hours, or 30 minutes and 90 minutes). In some embodiments, the dicarboxylic acid, cross-linker, and chain extender are mixed for about 1 hour. In some embodiments, the dicarboxylic acid, cross-linker, and chain extender are mixed under nitrogen. In some embodiments, the monomer product and the dicarboxylic acid are present at a ratio of between about 2:1 (w/w) and about 1:2 (w/w) (e.g., between about 2:1 (w/w) and 1:1 (w/w) or between 1:1 and about 1:2 (w/w)). In some embodiments, the monomer product and the Dicarboxylic acid are present at a ratio of about 3:2 (w/w). In some embodiments, the Monomer product and the cross-linker are present at a ratio of between about 4:1 (w/w) and about 1:2 (w/w) (e.g., about 4:1 (w/w) and about 1:1 (w/w), about 4:1 (w/w) and about 2:1 (w/w), about 4:1 (w/w) and about 3:1 (w/w), about 3:1 (w/w) and about 1:2 (w/w), about 2:1 (w/w) and about 1:2 (w/w), or about 1:1 (w/w) and about 1:2 (w/w)). In some embodiments, the monomer product and the cross-linker are present at a ratio of about 2:1 (w/w). In some embodiments, the monomer product and the chain extender are present at a ratio of between about 4:1 (w/w) and about 1:1 (w/w) (e.g., between about 4:1 (w/w) and about 2:1 (w/w), PATENT ATTORNEY DOCKET: 51494-028WO2 about 4:1 (w/w) and about 3:1 (w/w), about 3:1 (w/w) and about 1:1 (w/w), or about 2:1 (w/w) and about 1:1 (w/w)). In some embodiments, the monomer synthesis product and the chain extender are present at a ratio of about 3:1 (w/w). In some embodiments, the dicarboxylic acid comprises azelaic acid. In some embodiments, the dicarboxylic acid comprises phthalic acid. In some embodiments, the cross-linker comprises citric acid. In some embodiments, the chain extender and mechanical enhancer comprise 1,4-butanediol and sorbitol. In some embodiments, the 1,4-butanediol and sorbitol are present at a ratio of about 1:1 (w/w). In some embodiments, the polyester synthesis product is dried for between about 24 hours and about 72 hours (e.g., between about 24 hours and 60 hours, about 24 hours and 48 hours, about 24 hours and 36 hours, 36 hours and 72 hours, 48 hours and 72 hours, or 60 hours and 72 hours). In some embodiments, the polyester synthesis product is dried for about 48 hours. In some embodiments, the polyester synthesis step is performed at a temperature of between about 120 ^o C and about 200 ^o C (e.g., between about 150 ^o C and 200 ^o C, 175 ^o C and 200 ^o C, 120 ^o C and 175 ^o C, or 120 ^o C and 150 ^o C). In some embodiments, the polyester synthesis step is performed at a temperature of between about 140 ^o C and about 180 ^o C (e.g., between about 140 ^o C and 170 ^o C, 140 ^o C and 160 ^o C, 140 ^o C and 150 ^o C, 150 ^o C and 180 ^o C, 160 ^o C and 180 ^o C, or 170 ^o C and 180 ^o C). In some embodiments, the polyester synthesis step is performed at a temperature of about 160 ^o C. In some embodiments, the polyester synthesis step is performed for between about 30 minutes and about 4 hours (e.g., between about 1 hour and 4 hours, 2 hours and 4 hours, 3 hours and 4 hours, 30 minutes and 3 hours, 30 minutes and 2 hours, or 30 minutes and 1 hour). In some embodiments, the polyester synthesis step is performed for between about 1 hour and about 3 hours (e.g., between 1 hour and 2 hours, between 2 hours and 3 hours). In some embodiments, the polyester synthesis step is performed for about 2 hours. In some embodiments, the polyester synthesis product is dried for between about 1 day and about 5 days (e.g., between about 1 day and about 4 days, about 1 day and 3 days, about 1 day and 2 days, about 2 days and 5 days, about 3 days and 5 days, or about 4 days and 5 days). In some embodiments, the polyester synthesis product is dried for between about 2 days and about 4 days (e.g., about 2 days, about 3 days, and about 4 days). In some embodiments, the polyester synthesis product is dried for about 3 days. In some embodiments, the polyester synthesis product is dried for about 2 days. In some embodiments, the polyester synthesis product is dried at a temperature of between about 100 ^o C and about 180 ^o C (e.g., between about 100 ^o C and about 160 ^o C, about 100 ^o C and about 140 ^o C, about 100 ^o C and about 120 ^o C, about 120 ^o C and about 180 ^o C, about 140 ^o C and about 180 ^o C, or about 160 ^o C and about 180 ^o C). In some embodiments, the polyester synthesis product was dried at a temperature of between about 120 ^o C and about 160 ^o C (e.g., between about 120 ^o C and about 150 ^o C, about 120 ^o C and about 140 ^o C, about 120 ^o C and about 130 ^o C, about 130 ^o C and about 160 ^o C, about 140 ^o C and about 160 ^o C, or about 150 ^o C and about 160 ^o C). In some embodiments, the polyester synthesis product was dried at a temperature of about 140 ^o C. In some embodiments, the polyester synthesis is dried at a temperature of about 150 ^o C. In some embodiments, the polyester synthesis product is a linear polyester. In some embodiments, the polyester synthesis product is an unsaturated, aliphatic polyester. In some PATENT ATTORNEY DOCKET: 51494-028WO2 embodiments, the polyester synthesis product has a surface wettability of between about 40 ^o and 85 ^o (e.g., between about 40 ^o and about 60 ^o , about 40 ^o and about 50 ^o , about 50 ^o and about 85 ^o , about 60 ^o and about 85 ^o , or about 70 ^o and about 85 ^o ) when tested with water. In some embodiments, the polyester synthesis product has a surface wettability of between about 50 ^o and 75 ^o (e.g., between about 50 ^o and about 70 ^o , about 50 ^o and about 65 ^o , about 50 ^o and about 60 ^o , about 60 ^o and about 75 ^o , or about 65 ^o and about 70 ^o ) when tested with water. In some embodiments, the polyester synthesis product has a surface wettability of between about 5 ^o and 40 ^o (e.g., between about 5 ^o and about 30 ^o , about 5 ^o and about 20 ^o , about 5 ^o and about 20 ^o , about 5 ^o and about 10 ^o , about 10 ^o and about 40 ^o , about 10 ^o and about 40 ^o , or about 30 ^o and about 40 ^o ) when tested with squalane. In some embodiments, the polyester synthesis product has a surface wettability of between about 8 ^o and 35 ^o (e.g., about 10 ^o and about 30 ^o , about 10 ^o and about 20 ^o , about 20 ^o and about 35 ^o , or about 25 ^o and about 35 ^o ) when tested with squalane. In some embodiments of any of the above aspects or embodiments of the disclosure, the fermentation product is an isoprene. In some embodiments, the fermentation product is an isoprenoid. In some embodiments, the fermentation product is β-farnesene. In some embodiments, the fermentation product is a steviol glycoside. In some embodiments, the fermentation product is a human milk oligosaccharide. In some embodiments, the fermentation product is a cannabinoid. In some embodiments, the host cell is a yeast cell. In some embodiments, the yeast cell is S. cerevisiae. In another aspect, the disclosure provides a composition comprising a polymer, wherein the polymer is produced by any one of the methods described herein. In some embodiments, the polymer is a linear polyester. In some embodiments, the polymer is an unsaturated, aliphatic polyester. In some embodiments, the polymer has a surface wettability of between about 40 ^o and about 85 ^o (e.g., between about 40 ^o and about 60 ^o , about 40 ^o and about 50 ^o , about 50 ^o and about 85 ^o , about 60 ^o and about 85 ^o , or about 70 ^o and about 85 ^o ) when tested with water. In some embodiments, the polymer has a surface wettability of between about 50 ^o and about 75 ^o (e.g., between about 50 ^o and about 70 ^o , about 50 ^o and about 65 ^o , about 50 ^o and about 60 ^o , about 60 ^o and about 75 ^o , or about 65 ^o and about 70 ^o ) when tested with water. In some embodiments, the polymer has a surface wettability of between about 5 ^o and about 40 ^o (e.g., between about 5 ^o and about 30 ^o , about 5 ^o and about 20 ^o , about 5 ^o and about 20 ^o , about 5 ^o and about 10 ^o , about 10 ^o and about 40 ^o , about 10 ^o and about 40 ^o , or about 30 ^o and about 40 ^o ) when tested with squalane. In some embodiments, the polymer has a surface wettability of between about 8 ^o and about 35 ^o (e.g., about 10 ^o and about 30 ^o , about 10 ^o and about 20 ^o , about 20 ^o and about 35 ^o , or about 25 ^o and about 35 ^o ) when tested with squalane. In another aspect, the disclosure provides a composition comprising an epoxide produced by any one of the methods described herein. In some embodiments, the composition comprises a viscosity of about 1350±5 mPa. In some embodiments, the composition comprises an acid value of about 5.5±1 mg KOH/g. In some embodiments, the composition comprises a hydroxyl value of about 104.2±22.5 mg KOH/g. In some embodiments, the composition comprises a density of about 0.989 g/cm ³ . In some embodiments, the composition comprises a polydispersity index of about 0.99. PATENT ATTORNEY DOCKET: 51494-028WO2 In another aspect, the disclosure provides a composition comprising a monomer product produced by any one of the methods described herein. In some embodiments, the composition comprises a viscosity of about 13256 mPa. In some embodiments, the composition comprises, an acid value of about 3.3 mg KOH/g. In some embodiments, the composition comprises a hydroxyl value of about 82.3 mg KOH/g. In some embodiments, the composition comprises a density of about 0.994 g/cm ³ . In some embodiments, the composition comprises a polydispersity index of about 1.24. In another aspect, the disclosure provides a composition comprising a monomer product produced by any one of the methods described herein. In some embodiments, the composition comprises has a viscosity of about 2650 mPa. In some embodiments, the composition comprises an acid value of about 2.9±2 mg KOH/g. In some embodiments, the composition comprises, a hydroxyl value of about 265±12 mg KOH/g. In some embodiments, the composition comprises a density of about 0.998 g/cm ³ . In some embodiments, the composition comprises a polydispersity index of about 1.80. In another aspect, the disclosure provides a composition comprising squalane and any one of the compositions described herein. In another aspect, the disclosure provides any one of the compositions described herein which is formulated for topical application to a subject. In another aspect, the disclosure provides a composition comprising a viscosity of about 1600±50 mPa, an acid value of about 10.7±2 mg KOH/g, a hydroxyl value of about 63.5±2 mg KOH/g, or a density of about 1.04 g/cm ³ . In another aspect, the disclosure provides an epoxide comprising a viscosity of about 2650 mPa, an acid value of about 2.9±2 mg KOH/g, a hydroxyl value of about 265±12 mg KOH/g, a density of about 0.998 g/cm ³ , or a polydispersity index of about 1.80. In another aspect, the disclosure provides a polyol comprising a viscosity of about 13256 mPa, an acid value of about 3.3 mg KOH/g, a hydroxyl value of about 82.3 mg KOH/g, a density of about 0.994 g/cm ³ , or a polydispersity index of about 1.24. In another aspect, the disclosure provides a polyol comprising a viscosity of about 1350±5 mPa, an acid value of about 5.5±1 mg KOH/g, a hydroxyl value of about 104.2±22.5 mg KOH/g, a density of about 0.989 g/cm ³ , or a polydispersity index of about 0.99. In another aspect, the disclosure provides a polymer comprising a density of about 0.210 g/cm ³ , a melting temperature of about 242.4 ^o C, or a glass transition temperature of about 91.4 ^o C. In another aspect, the disclosure provides a polymer comprising a viscosity of a polydispersity index of about 1833.7 or a glass transition temperature of between about 51.1 ^o C and about 60.7 ^o C. In another aspect, the disclosure provides a polymer comprising a viscosity of a melting temperature of between about 167.8 ^o C and about 172.6 ^o C or a glass transition temperature of about -50.4 ^o C. In another aspect, the disclosure provides a polymer comprising a viscosity of a polydispersity index of about 1.03, or a glass transition temperature of between about -12.3 ^o C, or a melting temperature of about - 165.8 ^o C. PATENT ATTORNEY DOCKET: 51494-028WO2 Definitions As used in this specification and the appended claims, the singular forms “a,” “an,” and “the” include plural reference unless the context clearly dictates otherwise. The term “about” when modifying a numerical value or range herein includes normal variation encountered in the field, and includes plus or minus 1-10% (e.g., 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9% or 10%) of the numerical value or end points of the numerical range. Thus, a value of 10 includes all numerical values from 9 to 11. All numerical ranges described herein include the endpoints of the range unless otherwise noted, and all numerical values in-between the end points, to the first significant digit. As used herein, the term “cannabinoid” refers to a chemical substance that binds or interacts with a cannabinoid receptor (for example, a human cannabinoid receptor) and includes, without limitation, chemical compounds such endocannabinoids, phytocannabinoids, and synthetic cannabinoids. Synthetic compounds are chemicals made to mimic phytocannabinoids which are naturally found in the cannabis plant (e.g., Cannabis sativa), including but not limited to cannabigerols (CBG), cannabichromens (CBC), cannabidiol (CBD), tetrahydrocannabinol (THC), cannabinol (CBN), cannabinodiol (CBDL), cannabicyclol (CBL), cannabielsoin (CBE), and cannabitriol (CBT). As used herein, the term “capable of producing” refers to a host cell which includes the enzymes necessary for the production of a given compound in accordance with a biochemical pathway that produces the compound. For example, a cell (e.g., a yeast cell) that is “capable of producing” squalene is one that contains the enzymes necessary for production of the squalene according to the squalene biosynthetic pathway. As used herein, the term “distillation” describes a process by which at least a portion of a liquid undergoes a state change to have a gaseous state. For example, distillation may be used to separate two liquids from one another or to remove one liquid from a mixture containing one or more additional liquids. In some embodiments, evaporation includes the process of distillation, in which a liquid not only changes phase to a gaseous state but is subsequently condensed back to a liquid form. In some embodiments of the disclosure, a distillation is performed by heating a mixture of liquids such that a lower-boiling point substance begins to evaporate, changing phase from a liquid to a gaseous state, while leaving the remaining liquid(s) in the mixture in a liquid phase. The lower- boiling point substance may then be condensed, e.g., upon exposure to reduced temperature, thereby: (1) returning the lower-boiling point substance to a liquid phase, and (2) separating the lower- boiling point substance from the remaining liquid(s) in the mixture. The distillation may be, for example, a “simple distillation,” which refers to a process in which a mixture of liquids having substantially different boiling points (e.g., boiling points that differ from one another by about 25 C ^o or more) is separated by heating the mixture until substantially all of the lower- boiling point substance evaporates and substantially all of the higher-boiling point substance remains in the liquid phase. The vapor of the lower-boiling point substance, in turn, is condensed so as to return the lower-boiling point substance to the liquid phase. In some embodiments, the distillation may be a “fractional distillation,” a process that is used, e.g., for separating highly miscible liquids and/or those having boiling points that differ by less than about 25 C ^o . A fractional distillation process PATENT ATTORNEY DOCKET: 51494-028WO2 involves heating a mixture containing the liquids such that the resulting vapor enters a fractionating column. The fractionating column is a column (e.g., a vertical, inclined, or horizontal column) configured so as to have a temperature gradient: the bottom of the fractionating column (i.e., the point at which the vapor enters the column) is the warmest, and the top of the fractionating column is the coolest. As the vapor proceeds upward through the column, the vapor is enriched for the lower- boiling point substance as a result of the temperature gradient. Once enriched for the lower-boiling point substance, the vapor exits the fractionating column and is exposed to a reduced temperature, thereby condensing the lower-boiling point substance and resolving the liquid mixture into its components. As used herein, the term “distillate residue” refers to material remaining after a composition (e.g., a fermentation composition including a population of host cells capable of producing a fermentation product and a culture medium) has undergone a distillation process. The term “distillate residue” includes residue that is left behind in a first vessel after a fermentation composition has undergone distillation, and the distillation product is now found in a second vessel. In some embodiments, the distillate residue may include a hydroxylated product or may include polyols. As used herein, the term “endogenous” describes a molecule (e.g., a polypeptide, nucleic acid, or cofactor) that is found naturally in a particular organism (e.g., a human) or in a particular location within an organism (e.g., an organ, a tissue, or a cell, such as a human cell). As used herein, the term “exogenous” describes a molecule (e.g., a polypeptide, nucleic acid, or cofactor) that is not found naturally in a particular organism (e.g., a human) or in a particular location within an organism (e.g., an organ, a tissue, or a cell, such as a human cell). Exogenous materials include those that are provided from an external source to an organism or to cultured matter extracted therefrom. As used herein in the context of a gene, the term “express” refers to any one or more of the following events: (1) production of an RNA template from a DNA sequence (e.g., by transcription); (2) processing of an RNA transcript (e.g., by splicing, editing, 5’ cap formation, and/or 3’ end processing); (3) translation of an RNA into a polypeptide or protein; and (4) post-translational modification of a polypeptide or protein. Expression of a gene of interest in a cell, tissue sample, or subject can manifest, for example, as: an increase in the quantity or concentration of mRNA encoding a corresponding protein (as assessed, e.g., using RNA detection procedures described herein or known in the art, such as quantitative polymerase chain reaction (qPCR) and RNA seq techniques), an increase in the quantity or concentration of a corresponding protein (as assessed, e.g., using protein detection methods described herein or known in the art, such as enzyme-linked immunosorbent assays (ELISA), among others), and/or an increase in the activity of a corresponding protein (e.g., in the case of an enzyme, as assessed using an enzymatic activity assay described herein or known in the art). As used herein, the term “fermentation composition” refers to a composition which contains host cells and products, or metabolites produced by the genetically modified host cells. An example of a fermentation composition is a whole cell broth, which may be the entire contents of a vessel, including cells, aqueous phase, and compounds produced from the host cells. PATENT ATTORNEY DOCKET: 51494-028WO2 As used herein, the term “fermentation product” refers to a compound that is produced by a host cell (e.g., yeast cell), which is cultured in a medium and under conditions suitable for the host cells to produce the fermentation product. The fermentation product may be naturally produced by the host cells or may be produced by host cells that have been genetically modified to produce the fermentation product. As used herein, the term “gene” refers to the segment of DNA involved in producing or encoding a polypeptide chain. It may include regions preceding and following the coding region (leader and trailer) as well as intervening sequences (introns) between individual coding segments (exons). Alternatively, the term “gene” can refer to the segment of DNA involved in producing or encoding a non-translated RNA, such as an rRNA, tRNA, gRNA, or micro-RNA. A “genetic pathway” or “biosynthetic pathway” as used herein refers to a set of at least two different coding sequences, where the coding sequences encode enzymes that catalyze different parts of a synthetic pathway to form a desired product. In a genetic pathway, a first encoded enzyme uses a substrate to make a first product which in turn is used as a substrate for a second encoded enzyme to make a second product. In some embodiments, the genetic pathway includes 3 or more members (e.g., 3, 4, 5, 6, 7, 8, 9, etc.), wherein the product of one encoded enzyme is the substrate for the next enzyme in the synthetic pathway. As used herein, the term “genetically modified” denotes a host cell that contains a heterologous nucleotide sequence. The genetically modified host cells described herein typically do not exist in nature. As used herein, the term “heterologous” refers to what is not normally found in nature. The term “heterologous nucleic acid” refers to a nucleic acid not normally found in a given cell in nature. A heterologous nucleic acid can be: (a) foreign to its host cell, i.e., exogenous to the host cell such that a host cell does not naturally contain the nucleic acid; (b) naturally found in the host cell, i.e., endogenous or native to the host cell, but present at an unnatural quantity in the cell (i.e., greater or lesser quantity than naturally found in the host cell); (c) be naturally found in the host cell but positioned outside of its natural locus. A “heterologous” polypeptide refers to a polypeptide that is encoded by a “heterologous nucleic acid”. Thus, for example, a “heterologous” polypeptide may be naturally produced by a host cell but is encoded by a heterologous nucleic acid that has been introduced into the host cell by genetic engineering. For example, a “heterologous” polypeptide can include embodiments in which an endogenous polypeptide is produced by an expression construct and is overexpressed in the host cell compared to native levels of the polypeptide produced by the host cell. A “heterologous genetic pathway” or a “heterologous biosynthetic pathway” as used herein refer to a genetic pathway that does not normally or naturally exist in an organism or cell. The term “host cell” as used in the context of this disclosure refers to a microorganism, such as yeast, and includes an individual cell or cell culture including a heterologous vector or heterologous polynucleotide as described herein. Host cells include progeny of a single host cell, and the progeny may not necessarily be completely identical (in morphology or in total DNA complement) to the original parent cell due to natural, accidental, or deliberate mutation and/or change. A host cell PATENT ATTORNEY DOCKET: 51494-028WO2 includes cells into which a recombinant vector or a heterologous polynucleotide of the invention has been introduced, including by transformation, transfection, and the like. The terms “human milk oligosaccharide” and “HMO” are used interchangeably herein to refer to a group of nearly 200 identified sugar molecules that are found as the third most abundant component in human breast milk. HMOs in human breast milk are a complex mixture of free, indigestible carbohydrates with many different biological roles, including promoting the development of a functional infant immune system. HMOs include, without limitation, lacto-N-neotetraose (LNnT), 2’-fucosyllactose (2’-FL), 3-fucosyllactose (3-FL), difucosyllactose (DFL), lacto-N-tetraose (LNT), lacto-N-fucopentaose (LNFP) I, LNFP II, LNFP III, LNFP V, LNFP VI, lacto-N-difucohexaose (LNDFH) I, LNDFH II, lacto-N-hexaose (LNH), lacto-N-neohexaose (LNnH), fucosyllacto-N-hexaose (F-LNH) I, F-LNH II, difucosyllacto-N-hexaose (DFLNH) I, DFLNH II, difucosyllacto-N-neohexaose (DFLNnH), difucosyl-para-lacto-N-hexaose (DF-para-LNH), difucosyl-para-lacto-N-neohexaose (DF-para-LNnH), trifucosyllacto-N-hexaose (TF-LNH), 3’-siallylactose (3’-SL), 6’-siallylactose (6’-SL), sialyllacto-N- tetraose (LST) a, LST b, LST c, disialyllacto-N-tetraose (DS-LNT), fucosyl-sialyllacto-N-tetraose (F- LST) a, F-LST b, fucosyl-sialyllacto-N-hexaose (FS-LNH), fucosyl-sialyllacto-N-neohexaose (FS- LNnH) I, and fucosyl-disialyllacto-N-hexaose (FDS-LNH II), among others. As used herein, the term “medium” refers to culture medium and/or fermentation medium. The terms “modified,” “recombinant” and “engineered,” when used to modify a host cell described herein, refer to host cells or organisms that do not exist in nature, or express compounds, nucleic acids or proteins at levels that are not expressed by naturally occurring cells or organisms. As used herein, the phrase “operably linked” refers to a functional linkage between nucleic acid sequences such that the linked promoter and/or regulatory region functionally controls expression of the coding sequence. As used herein, the term “polyurethane” refers to a polymer which includes a chain including two or more monomer units which are joined together by carbamate linkages. As used herein, the term “production” generally refers to an amount of compound produced by a host cell provided herein. In some embodiments, production is expressed as a yield of the compound by the host cell. In other embodiments, production is expressed as a productivity of the host cell in producing the compound. As used herein, the term “steviol glycoside” refers to a glycoside of steviol including but not limited to 19-glycoside, steviolmonoside, steviolbioside, rubusoside, dulcoside B, dulcoside A, rebaudioside A (RebA), rebaudioside B (RebB), rebaudioside C (RebC), rebaudioside D (RebD), rebaudioside E (RebE), rebaudioside F (RebF), rebaudioside G (RebG), rebaudioside H (RebH), rebaudioside I (RebI), rebaudioside J (RebJ), rebaudioside K (RebK), rebaudioside L (RebL), rebaudioside M (RebM), rebaudioside N (RebN), rebaudioside O (RebO), rebaudioside D2, and rebaudioside M2. As used herein, the term “subject” refers to an individual that is in need of therapeutic intervention wherein the individual may be an animal or a human. As used herein, the term “therapeutic” refers to a composition that is administered to a subject to treat or prevent the symptoms of a disease or condition. PATENT ATTORNEY DOCKET: 51494-028WO2 Brief Description of the Drawings FIG.1 is a graph showing the Fourier Transform spectra of the epoxide, the polyol, and the polyester. ` FIG.2 is a graph showing the wettability study of the polymer film using water or squalane. FIG.3 is a graph showing the amount of mass lost due to degradation of the polymer film over time. FIG.4 is a graph showing the cell viability of HaCaT cells that were exposed to media conditioned with polymer discs as a way of measuring the cytotoxicity of the polymer. FIG.5 is a graph showing the result of a differential scanning calorimetry experiment which shows the glass transition, melting temperature, and temperature of decomposition for a polyurethane film. FIG.6 is a graph showing the representative stress versus strain curves of a polyurethane film. FIG.7 is a schematic drawing showing the steps of producing a polyurethane film. FIG.8A and FIG.8B are a set of representative SEM micrographs of the polyurethane film resulting from salt leaching for generating 2D (FIG.8A) and 3D (FIG.8B) films. FIG.9 is a chart showing the results of the characterization of the various polymer films that were produced FIG.10A and FIG.10B are comparative structural analysis (FT-IR) of the reaction progression starting with the oil residue (FDR) (FIG.10A), the respective epoxide and subsequent polyol; bio-based and benchmark PUR foams (FIG.10B). FIG.11 is a graph showing the comparative thermograms (DSC) of the bio-based and benchmark PUR foams. FIG.12 is a series of photographs showing the representative polyurethane foams synthesized with the bio-based polyol, without ash (PF) and with ash (PAF). FIGS.13A-13D are a series of representative SEM micrographs (magnification 50 x) of polyurethane foams of SF (FIG.13A), SFRH (FIG.13B), PF (FIG.13C), and PAF (FIG.13D) foams. FIG.14 is a representative photograph of the universal testing machine used to measure tensile strength, residual strain, and stress-relaxation. FIG.15 is a representative photograph of the type geometry of the polyester coupons used in the tensile, residual strain, and stress-relaxation tests. FIG.16 is graph showing the structural analysis (ATR-FTIR) of the polyester synthesis encompassing the feedstock and the intermediates produced. FIG.17 is a series of graphs showing the interaction curves of time-strain factors in the residual strain response after 1 minute of load removal. FIG.18 is a series of graphs showing the stress-relaxation curves of the flexible polymer at different load levels. FIG.19 is a differential scanning calorimetry thermogram showing the second heating of two different thermal program cycles. FIG.20 is a graph showing the dynamic mechanical analysis (DMA) of the polyester. PATENT ATTORNEY DOCKET: 51494-028WO2 FIG.21 is a chart showing the physical and chemical properties of the fermentation distillate residue (FDR) as well the intermediate compounds prior to synthesis of the polymer. Detailed Description The present disclosure provides compositions and methods for synthesizing bio-based polymers (e.g., polyurethanes and polyesters) from a fermentation composition. The polyurethane is synthesized by culturing a population of host cells capable of producing the fermentation product in a culture medium and under conditions suitable for the host cells to produce the fermentation product. Given the interest in producing new biomaterials from the by-products of fermentation, the challenge of treating the polyols from these by-products such that they are suitable for polymerization has been significant. However, while the polyols are known to be present in a fermentation composition, they are also known to be present among sludge and wax which prevent them from being used in generating new materials. It has presently been discovered that a distillate residue from a fermentation composition may treated to isolate and purify polyols capable of polymerization, thus producing a polymer. By reacting the distillate residue from a fermentation composition with an epoxidation agent to produce an epoxide and subsequently reacting the epoxide in a polyester synthesis step, a polymer may be successfully produced from the by-product of the fermentation composition. The sections that follow provide a description of exemplary compositions and methods that may be used to synthesize a polyurethane including extraction, distillation, and reaction steps of the disclosure. Methods of Synthesizing Bio-Based Polymers Provided herein are methods of synthesizing a polymer from a fermentation composition that has been produced by culturing a population of host cells capable of producing a fermentation product in a culture medium and under conditions suitable for the host cells to produce the fermentation product. The disclosure provides methods of synthesizing a polymer by using an epoxide synthesis step in which a residue from a fermentation composition is reacted with an epoxidation agent, thereby producing an epoxide. The method may further include a ring-opening step. The ring-opening step may include reacting the epoxide is reacted with a ring-opening agent to produce a monomer product. The epoxide synthesis step may include a pretreatment of a distillate residue from the fermentation composition and an epoxidation reaction to produce an epoxidation product. In some embodiments, the pretreatment step includes a winterization step. The winterization step may include dissolving the residue from the fermentation composition in ethanol to form an ethanol solution. In some embodiments, the ethanol is added to a concentration of 4:1 (wt) of residue from the fermentation composition to ethanol. The ethanol solution may then be mixed for between about 1 minute and about 1 hour (e.g., between about 1 minute and 45 minutes, about 1 minute and 30 minutes, 1 minute and 15 minutes, 15 minutes and 1 hour, 30 minutes and 1 hour, or 45 minutes and 1 hour). For example, the ethanol solution may be mixed for between about 1 minute and about 20 minutes (e.g., about 1 minute, 2 minutes, 3 minutes, 4 minutes, 5 minutes, 6 minutes, 7 minutes, 8 minutes, 9 minutes, 10 minutes, 11 minutes, 12 minutes, 13 minutes, 14 minutes, 15 minutes, 16 PATENT ATTORNEY DOCKET: 51494-028WO2 minutes, 17 minutes, 18 minutes, 19 minutes, or 20 minutes). In some embodiments, the ethanol solution is mixed for about 5 minutes. After mixing the ethanol solution, it may be left to stand for between about 10 minutes and about 6 hours (e.g., between about 10 minutes and 5 hours, 10 minutes and 4 hours, 10 minutes and 3 hours, 10 minutes and 2 hours, 10 minutes and 1 hour, 10 minutes and 30 minutes, 30 minutes and 6 hours, 1 hour and 6 hours, 2 hours and 6 hours, 3 hours and 6 hours, 4 hours and 6 hours, or 5 hours and 6 hours). For example, the ethanol solution may be left to stand for between about 1 hour and about 3 hours (e.g., between about 1 hour and 2 hours, 1 hour and 1.5 hours, 1.5 hours and 3 hours, 2 hours and 3 hours, or 2.5 hours and 3 hours). In some embodiments, the ethanol solution is let stand for about 2 hours. The ethanol solution may be left to stand at about room temperature. The ethanol solution may then be chilled for between about 1 hour and about 24 hours (e.g., between about 1 hour and about 18 hours, about 1 hour and 12 hours, 1 hour and 6 hours, 6 hours and 24 hours, 12 hours and 24 hours, or 18 hours and 24 hours). For example, the ethanol solution is chilled for between about 8 hours and about 16 hours (e.g., about 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 13 hours, 14 hours, 15 hours, or 16 hours). The ethanol solution may be chilled to a temperature of between about -50 ^o C and about 0 ^o C (e.g., between about -50 ^o C and -10 ^o C, -50 ^o C and -20 ^o C, -50 ^o C and -30 ^o C, -50 ^o C and -40 ^o C, -40 ^o C and 0 ^o C, -30 ^o C and 0 ^o C, -20 ^o C and 0 ^o C, or -10 ^o C and 0 ^o C). In some embodiments, the ethanol solution is chilled at a temperature of between about-40 ^o C and about -20 ^o C (e.g., about -40 ^o C, -39 ^o C, -38 ^o C, -37 ^o C, -36 ^o C, -35 ^o C, -34 ^o C, -33 ^o C, -32 ^o C, -31 ^o C, -30 ^o C, -29 ^o C, -28 ^o C, -27 ^o C, -26 ^o C, -25 ^o C, -24 ^o C, -23 ^o C, -22 ^o C, -21 ^o C, or -20 ^o C); for example, the ethanol solution may be chilled to a temperature of about -30 ^o C. The winterization step may further comprise centrifugation of the ethanol solution. The ethanol solution may be centrifuged at a speed which allows for the separation of the oil phase. For example, it may be centrifuged at a speed of between about 500 g to about 2000 g (e.g., between about 750 g and 2000 g, 1000 g and 2000 g, 1250 g and 2000 g, 1500 g and 2000 g, 1750 g and 2000 g, 500 g and 1750 g, 500 g and 1500 g, 500 g and 1250 g, 500 g and 1000 g, or 500 g and 750 g). In some embodiments, the ethanol solution is centrifuged at a speed of about 1250 g. The centrifugation may last for between about 1 minute and about 30 minutes (e.g., between about 1 minute and 25 minutes, 1 minute and 20 minutes, 1 minute and 15 minutes, 1 minute and 10 minutes, 1 minute and 5 minutes, 5 minutes and 30 minutes, 10 minutes and 30 minutes, 15 minutes and 30 minutes, 20 minutes and 30 minutes, or 25 minutes and 30 minutes). Furthermore, the centrifugation may occur at room temperature The pretreatment step may include a filtration step. The filtration step may include comprises at least 2 filtration steps, such as between 2 and 5 filtration steps (e.g., 2 filtration steps, 3 filtration steps, 4 filtration steps, or 5 filtration steps). In some embodiments, the method includes a first filtration step, a second filtration step, and a third filtration step. The first filtration step may comprise filtering the residue from a fermentation composition through a nonwoven (TNT) filter. The second filtration step may comprise filtering through a filter having a membrane that is between 5 µm and 15 µm in pore size (e.g., 5 µm, 6 µm, 7 µm, 8 µm, 9 µm, 10 µm, 11 µm, 12 µm, 13 µm, 14 µm, or 15 µm in pore size); for example, the membrane may have pores which are about 11 µm. The third filtration PATENT ATTORNEY DOCKET: 51494-028WO2 step may include filtering through a filter having a membrane that is between 5 µm and 15 µm in pore size (e.g., 5 µm, 6 µm, 7 µm, 8 µm, 9 µm, 10 µm, 11 µm, 12 µm, 13 µm, 14 µm, or 15 µm in pore size). In some embodiments, the membrane is about 8 µm in pore size. EPOXIDATION: OXIRANE-RING FORMATION The epoxide synthesis step may comprise contacting the distillate residue from a fermentation composition with the epoxidation agent to form an epoxidation product. The epoxidation agent may include performic acid or hydrogen peroxide, optionally mixed with ethyl acetate and/or formic acid. The ethyl acetate may have a final concentration of between about 10% (w/w) and about 60% (w/w) (e.g., between about 10% (w/w) and 50% (w/w), 10% (w/w) and 40% (w/w), 10% (w/w) and 30% (w/w), 10% (w/w) and 20% (w/w), 20% (w/w) and 60% (w/w), 30% (w/w) and 60% (w/w), 40% (w/w) and 60% (w/w), or 50% (w/w) and 60% (w/w)). For example, the ethyl acetate may have a final concentration of between about 20% (w/w) and about 40% (w/w). In some embodiments, the ethyl acetate has a final concentration about 32% (w/w). The performic acid may have a final concentration of between about 1% (w/w) and about 10% (w/w) (e.g., about 1% (w/w), 2% (w/w), 3% (w/w), 4% (w/w), 5% (w/w), 6% (w/w), 7% (w/w), 8% (w/w), 9% (w/w), or 10% (w/w)). For example, the performic acid may have a final concentration of between about 2% (w/w) and about 5% (w/w) (e.g., about 2% (w/w), 3% (w/w), 4% (w/w), or 5% (w/w)). In some embodiments, the performic acid has a final concentration of between about 3% (w/w) and about 4% (w/w). The epoxide synthesis step may further include contacting the distillate residue from a fermentation composition, ethyl acetate, and formic acid with hydrogen peroxide, which may be refrigerated hydrogen peroxide. The hydrogen peroxide may be refrigerated such as to reduce foaming upon contact with the distillate residue from a fermentation composition. The hydrogen peroxide may have a final concentration of between about 25% (w/w) and about 75% (w/w) (e.g., between about 35% (w/w) and 75% (w/w), 45% (w/w) and 75% (w/w), 55% (w/w) and 75% (w/w), 65% (w/w) and 75% (w/w), 25% (w/w) and 65% (w/w), 25% (w/w) and 55% (w/w), 25% (w/w) and 45% (w/w), or 25% (w/w) and 35% (w/w)). In some embodiments, the hydrogen peroxide has a final concentration of about 50% (w/w). The epoxide synthesis step may be performed at a temperature that is between about 50 ^o C and about 125 ^o C (e.g., between about 50 ^o C and 100 ^o C, about 50 ^o C and 75 ^o C, about 75 ^o C and 125 ^o C, or about 100 ^o C and 125 ^o C) such between about 70 ^o C and about 100 ^o C (e.g., between about 70 ^o C and 90 ^o C, about 70 ^o C and 80 ^o C, about 80 ^o C and 100 ^o C, or about 90 ^o C and 100 ^o C). In some embodiments, the epoxide synthesis step is performed at about 85 ^o C. The epoxide synthesis step may be run for between about 30 minutes and about 6 hours (e.g., between about 30 minutes and about 5 hours, about 30 minutes and about 4 hours, about 30 minutes and about 3 hours, about 30 minutes and 2 hours, about 30 minutes and 1 hour, about 1 hour and about 6 hours, about 2 hours and about 6 hours, about 3 hours and about 6 hours, about 4 hours and about 6 hours, or about 5 hours and about 6 hours); for example, the epoxide synthesis step may be reacted for between about 1 hour and about 4 hours (e.g., between about 1 hour and 3 hours, about 1 hour and 2 PATENT ATTORNEY DOCKET: 51494-028WO2 hours, about 2 hours and 4 hours, or about 3 hours and 4 hours). In some embodiments, the epoxide synthesis step is run for between about 3 hours. OPENING RING-STEP: HYDROXYLATION The ring-opening step may include contacting the epoxide product with the ring-opening agent. In some embodiments, the ring-opening agent comprises castor oil. The castor oil may have a final concentration of between about 10% (w/w) and about 50% (w/w) (e.g., between about 10% (w/w) and about 40% (w/w), about 10% (w/w) and 30% (w/w), about 10% (w/w) and 20% (w/w), about 20% (w/w) and about 50% (w/w), about 30% (w/w) and about 50% (w/w), or about 40% (w/w) and about 50% (w/w)). For example, the castor oil may have a final concentration of between about 20% (w/w) and about 35% (w/w) (e.g., about 20% (w/w), 21% (w/w), 22% (w/w), 23% (w/w), 24% (w/w), 25% (w/w), 26% (w/w), 27% (w/w), 28% (w/w), 29% (w/w), 30% (w/w), 31% (w/w), 32% (w/w), 33% (w/w), 34% (w/w), or 35% (w/w)). In some embodiments, the castor oil has a final concentration of about 25% (w/w). The ring-opening step may be performed at a temperature of between about 100 ^o C and about 225 ^o C (e.g., between about 100 ^o C and about 200 ^o C, about 100 ^o C and about 175 ^o C, about 100 ^o C and about 150 ^o C, about 100 ^o C and about 125 ^o C, about 125 ^o C and about 225 ^o C, about 150 ^o C and about 225 ^o C, about 175 ^o C and about 225 ^o C, or about 200 ^o C and about 225 ^o C), such as a temperature of between about 140 ^o C and about 180 ^o C (e.g., between about 140 ^o C and about 170 ^o C, about 140 ^o C and about 160 ^o C, about 140 ^o C and about 150 ^o C, about 150 ^o C and about 180 ^o C, about 160 ^o C and about 180 ^o C, or about 170 ^o C and about 180 ^o C). For example, the ring-opening step may be performed at a temperature of about 160 ^o C. The ring-opening step may be performed for a period of time of between about 2 hours and about 12 hours (e.g., between about 2 hours and about 10 hours, about 2 hours and about 8 hours, about 2 hours and about 6 hours, about 2 hours and about 4 hours, about 4 hours and about 12 hours, about 6 hours and about 12 hours, about 8 hours and about 12 hours, or about 10 hours and about 12 hours). During this time, the component of the ring-opening action may be mixed continuously. In some embodiments, the ring-opening step is performed between about 6 hours and about 7 hours. This reaction may be performed under a nitrogen purge in order to reduce exposure to oxygen. The ring-opening agent may be phosphoric acid, and the phosphoric acid may have a final concentration in the ring-opening step of between about 5% (w/w) and about 20% (w/w) (e.g., between about 5% (w/w) and about 15% (w/w), about 5% (w/w) and about 10% (w/w), about 10% (w/w) and about 20% (w/w), or about 15% (w/w) and about 20% (w/w)), optionally, the phosphoric may have a final concentration of about 9% (w/w). The ring-opening step may be performed at any suitable temperature such that the reaction may proceed. In some embodiments, the ring-opening step is performed at a temperature of between about 60 ^o C and about 100 ^o C (e.g., between about 60 ^o C and about 90 ^o C, about 60 ^o C and about 80 ^o C, about 60 ^o C and about 70 ^o C, about 70 ^o C and about 100 ^o C, about 80 ^o C and about 100 ^o C, or about 90 ^o C and about 100 ^o C); for example, the ring- opening step may be performed at a temperature of between about 75 ^o C and about 90 ^o C (e.g., between about 75 ^o C and about 85 ^o C, about 75 ^o C and about 80 ^o C, about 80 ^o C and about 90 ^o C, or PATENT ATTORNEY DOCKET: 51494-028WO2 about 85 ^o C and about 90 ^o C). In some embodiments, the ring-opening step is performed at a temperature of about 85 ^o C. The ring-opening step may be stirred for between about 10 minutes and about 4 hours (e.g., between about 10 minutes and 3 hours, about 10 minutes and 2 hours, about 10 minutes and 1 hour, about 1 hour and about 4 hours, about 2 hours and about 4 hours, or about 3 hours and about 4 hours). In some embodiments, the ring-opening step comprises stirring the epoxide and the ring- opening agent for between about 30 minutes and about 2 hours (e.g., between about 30 minutes and about 1.5 hours, about 30 minute and about 1 hour, about 1 hour and about 2 hours, or about 1.5 hours and about 2 hours). For example, the ring-opening step comprises stirring the epoxide and the ring-opening agent for about 1 hour. The monomer product may be washed with carbonate. In some embodiments, the carbonate is calcium carbonate. In some embodiments, the carbonate is sodium carbonate. The carbonate used to wash the monomer product may have a concentration of between about 1% (w/w) and about 20 % (w/w) (e.g., between about 1% (w/w) and about 15% (w/w), about 1% (w/w) and about 10% (w/w), about 1% (w/w) and about 5% (w/w), about 5% (w/w) and about 20% (w/w), about 10% (w/w) and about 20% (w/w), or about 15% (w/w) and about 20% (w/w)). For example, the carbonate may have a concentration of between about 5% (w/w) and about 15% (w/w) (e.g., between about 5% (w/w) and about 12% (w/w), about 5% (w/w) and about 7% (w/w), about 7% (w/w) and about 15% (w/w), or about 12% (w/w) and about 15% (w/w)). In some embodiments, the carbonate has a concentration of about 10% (w/w). After the monomer product is washed with carbonate, the monomer product may be further washed with distilled water. For example, after the monomer product is washed with carbonate, the monomer product may be washed at least twice with distilled water. In some embodiments, the ring-opening agent may be glycerol. The glycerol may have a final concentration of between about 5% (w/w) and about 40% (w/w) (e.g., between about 5% (w/w) and about 30 % (w/w), about 5% (w/w) and about 20% (w/w), about 5% (w/w) and about 10% (w/w), about 10% (w/w) and about 40 % (w/w), about 20% (w/w) and about 40% (w/w), or about 30% (w/w) and about 40% (w/w)), such as between about 15% (w/w) and about 30% (w/w) (e.g., about 15% (w/w), 16% (w/w), 17% (w/w), 18% (w/w), 19% (w/w), 20% (w/w), 21% (w/w), 22% (w/w), 23% (w/w), 24% (w/w), 25% (w/w), 26% (w/w), 27% (w/w), 28% (w/w), 29% (w/w), or 30% (w/w)). In some embodiments, the glycerol has a final concentration of about 20% (w/w). The ring-opening step may further comprise tetrafluoroboric acid. The tetrafluoroboric acid may be used to reduce the humidity present during the reaction. The tetrafluoroboric acid may have a final concentration of between about 0.01% (w/w) and about 0.1% (w/w) (e.g., about 0.01% (w/w), 0.02% (w/w), 0.03% (w/w), 0.04% (w/w), 0.05% (w/w), 0.06% (w/w), 0.07% (w/w), 0.08% (w/w), 0.09% (w/w), or 0.1% (w/w)). In some embodiments, the tetrafluoroboric acid has a final concentration of about 0.05% (w/w). The components of the ring-opening step may be allowed to react over a period of between about 2 hours and about 10 hours (e.g., between about 2 hours and about 8 hours, about 2 hours and about 6 hours, about 2 hours and about 4 hours, about 4 hours and about 10 hours, about 6 hours PATENT ATTORNEY DOCKET: 51494-028WO2 and about 10 hours, or about 8 hours and about 10 hours). In some embodiments, the ring-opening step is performed for about 6 hours. The ring-opening step may be performed at a temperature of between about 40 ^o C and about 80 ^o C (e.g., between about 40 ^o C and about 70 ^o C, about 40 ^o C and about 60 ^o C, about 40 ^o C and about 50 ^o C, about 50 ^o C and about 80 ^o C, about 60 ^o C and about 80 ^o C, or about 70 ^o C and about 80 ^o C). For example, the ring-opening step may be performed at a temperature of between about 30 ^o C and about 70 ^o C (e.g., between about 30 ^o C and about 60 ^o C, about 30 ^o C and about 50 ^o C, about 30 ^o C and about 40 ^o C, about 40 ^o C and about 70 ^o C, about 50 ^o C and about 70 ^o C, or about 60 ^o C and about 70 ^o C). In some embodiments, the ring-opening step is performed at a temperature of about 60 ^o C. The ring-opening step may be constantly stirred over the course of the reaction. The monomer product may be any hydroxylated, monomer product. The resulting monomer product may be a polyol. THE POLYESTER-POLYHYDROXYURETHANE (PHU) POLYMER The method may further include a polyester-polyhydroxyurethane synthesis reaction. The polyester-polyhydroxyurethane synthesis reaction may include a transcarbonation reaction step, an aminolysis reaction step, wherein the aminolysis reaction step produces an aminolysis reaction step product, and an esterification step. The transcarbonation reaction step may include contacting the monomer product with dimethyl carbonate and sodium carbonate. In some embodiments, the dimethyl carbonate has a final concentration of between about 10% (w/w) and about 50% (w/w) (e.g., between about 10% (w/w) and about 40 % (w/w), about 10% (w/w) and about 30% (w/w), about 10% (w/w) and about 20% (w/w), about 20% (w/w) and about 50% (w/w), about 30% (w/w) and about 50% (w/w), or about 40% (w/w) and about 50% (w/w)). For example, the dimethyl carbonate may have a final concentration of between about 35% (w/w) and about 45% (w/w) (e.g., about 35% (w/w), 36% (w/w), 37% (w/w), 38% (w/w), 39% (w/w), 40% (w/w), 41% (w/w), 42 % (w/w), 43% (w/w), 44% (w/w), or 45% (w/w)). The sodium carbonate may have a final concentration of between about 0.01% (w/w) and about 0.1% (w/w) (e.g., about 0.01% (w/w), 0.02% (w/w), 0.03% (w/w), 0.04% (w/w), 0.05% (w/w), 0.06% (w/w), 0.07% (w/w), 0.08% (w/w), 0.09% (w/w), or 0.1% (w/w)). In some embodiments, the sodium carbonate has a final concentration of about 0.05% (w/w). The transcarbonation reaction may be performed in a reactor coupled with a condenser. In some embodiments, the transcarbonation reaction is performed under reflux conditions for between about 30 minutes and about 4 hours (e.g., between about 30 minutes and about 3 hours, about 30 minutes and about 2 hours, about 30 minutes and about 1 hour, about 1 hour and about 4 hours, about 2 hours and about 4 hours, or about 3 hours and about 4 hours). For example, the transcarbonation reaction may be performed under reflux conditions for between about 1 hour and about 3 hours. (e.g., between about 1 hour and about 3 hours, about 1 hour and about 2 hours, or about 2 hours and about 3 hours). In some embodiments, the transcarbonation reaction is performed under reflux conditions for about 2 hours. The transcarbonation reaction may be refluxed at a temperature of between about 50 ^o C and about 100 ^o C (e.g., about 50 ^o C and about 90 ^o C, about 50 ^o C and about 80 ^o C, about 50 ^o C and about 70 ^o C, about 50 ^o C and about 60 ^o C, about 60 ^o C and PATENT ATTORNEY DOCKET: 51494-028WO2 about 100 ^o C, about 70 ^o C and about 100 ^o C, about 80 ^o C and about 100 ^o C, or about 90 ^o C and about 100 ^o C), such as a temperature of about 75 ^o C. After refluxing, the transcarbonation reaction may be cooled to about room temperature. After the transcarbonation reaction is cooled, the transcarbonation reaction suspension may be centrifuged to isolate a lighter organic phase as a transcarbonation reaction product. The polyhydroxyurethane synthesis reaction may include contacting the transcarbonation reaction product, a cyclic carbonate, and a cycloaliphatic amine to produce a polyhydroxyurethane synthesis product. The cyclic carbonate may be a polyalkyl glycidate carbonate. The cycloaliphatic amine may be isophorone. The transcarbonation reaction product, a cyclic carbonate, and a cycloaliphatic amine may be mixed for between about 1 hour and about 4 hours (e.g., between about 1 hour and about 3 hours, about 1 hour and about 2 hours, about 2 hours and about 4 hours, or about 3 hours and about 4 hours), for example, about 2 hours. In some embodiments, the polyhydroxyurethane synthesis reaction includes mixing the transcarbonation reaction product, a cyclic carbonate, and a cycloaliphatic amine at a temperature of between about 30 ^o C and about 70 ^o C (e.g., between about 30 ^o C and about 60 ^o C, about 30 ^o C and about 50 ^o C, about 30 ^o C and about 40 ^o C, about 40 ^o C and about 70 ^o C, about 50 ^o C and about 70 ^o C, or about 60 ^o C and about 70 ^o C). For example, the transcarbonation reaction product, a cyclic carbonate and a cycloaliphatic amine may be mixed at a temperature of 50 ^o C. The polyester-polyhydroxyurethane synthesis reaction may include contacting the aminolysis step reaction product with phthalic acid, citric acid, and 1,4 - butanediol. The polyhydroxyurethane synthesis product, phthalic acid, citric acid, and butanediol may be present in a ratio of 3:4.5:0.5:0.5. The polyester-polyhydroxyurethane synthesis reaction may include contacting the aminolysis step reaction product with phthalic acid, citric acid, and 1,4 - butanediol for between about 1 hour and about 4 hours (e.g., between about 1 hour and about 3 hours, about 1 hour and about 2 hours, about 2 hours and about 4 hours, or about 3 hours and about 4 hours). For example, the aminolysis step reaction product, phthalic acid, citric acid, and 1,4 - butanediol may be mixed for about 2 hours. The polyester-polyhydroxyurethane synthesis reaction may include contacting the aminolysis step reaction product with phthalic acid, citric acid, and butanediol at a temperature of between about 120 ^o and about 200 ^o C (e.g., between about 120 ^o C and about 180 ^o C, about 120 ^o C and about 160 ^o C, about 120 ^o C and about 140 ^o C, about 140 ^o C and about 200 ^o C, about 160 ^o C and about 200 ^o C, or about 180 ^o C and about 200 ^o C). For example, the aminolysis step reaction product may be mixed with phthalic acid, citric acid, and butanediol at a temperature of about 160 ^o C. The polyester- polyhydroxyurethane synthesis reaction may be performed under nitrogen. POLYURETHANE FOAMS SYNTHESIS The method may further include a polyurethane synthesis reaction. The polyurethane synthesis reaction may include a two-step reaction. The first step may include a prepolymer synthesis step, wherein the monomer product is contacted with a dicarboxylic acid, a cross-linker, chain extender, an emulsifier, a catalyst, a blowing agent, and optionally sugarcane bagasse ash, PATENT ATTORNEY DOCKET: 51494-028WO2 thereby producing a prepolymer reaction product. The second step may include contacting the prepolymer reaction product with an isocyanate, thereby producing a polyurethane synthesis product. The prepolymer synthesis step may be performed by mixing together and melting the monomer product, the blowing agent, the chain-extender, the catalyst, and the emulsifier. In some embodiments, the monomer product, the blowing agent, the chain-extender, the catalyst, and the emulsifier, may be mixed together for between about 5 seconds and about 20 seconds (e.g., between about 5 seconds and 15 seconds, 5 seconds and 10 seconds, 10 seconds and 20 seconds, or 15 seconds and 20 seconds). The isocyanate may be added after mixing together the monomer product, the blowing agent, the chain-extender, the catalyst, and the emulsifier to produce the prepolymer product. The polyurethane synthesis product is dried at about room temperature. The chain extender may include glycerol. In some embodiments, the glycerol has a final concentration of between about 10% (w/w) and about 30% (w/w) (e.g., between about 10% (w/w) and about 25% (w/w), about 10% (w/w) and about 20% (w/w), about 10% (w/w) and about 15% (w/w), about 15% (w/w) and about 30% (w/w), about 20% (w/w) and about 30% (w/w), or about 25% (w/w) and about 30% (w/w)). For example, the glycerol may have a final concentration of between about 15% (w/w) and about 20% (w/w) (e.g., about 15% (w/w), 16% (w/w), 17% (w/w), 18% (w/w), 19% (w/w), or 20% (w/w)). In some embodiments, the glycerol has a final concentration of between about 18% (w/w) and about 19% (w/w). The catalyst may include dibutyltin dilaurate. The dibutyltin dilaurate may have a final concentration of between about 1% (w/w) and about 5% (w/w) (e.g., between about 1% (w/w) and about 4% (w/w), about 1% (w/w) and about 3% (w/w), about 1% (w/w) and about 2% (w/w), about 2% (w/w) and about 5% (w/w), about 3% (w/w) and about 5% (w/w), or about 4% (w/w) and about 5% (w/w)). In some embodiments, the dibutyltin dilaurate has a final concentration of between about 2% (w/w) and about 3% (w/w), optionally wherein the dibutyltin dilaurate has a final concentration of about 2.72% (w/w). The emulsifier may include polydimethylsiloxane. The polydimethylsiloxane may have a final concentration of between about 0.1% (w/w) and about 5% (w/w) (e.g., between about 0.1% (w/w) and about 4% (w/w), about 0.1% (w/w) and about 3% (w/w), about 0.1% (w/w) and about 2% (w/w), about 0.1% (w/w) and about 1% (w/w), about 1% (w/w) and about 5% (w/w), about 2% (w/w) and about 5% (w/w), about 3% (w/w) and about 5% (w/w), or about 4% (w/w) and about 5% (w/w), such as between about 0.5% (w/w) and about 3% (w/w). In some embodiments, wherein the sugarcane bagasse ash was previously heated to a temperature of between about 400 ^o C and about 800 ^o C (e.g., between about 400 ^o C and 700 ^o C, about 400 ^o C and 600 ^o C, about 400 ^o C and 500 ^o C, about 500 ^o C and 800 ^o C, about 600 ^o C and 800 ^o C, or about 700 ^o C and 800 ^o C). In some embodiments, the sugarcane bagasse ash was previously heated to a temperature of about 600 ^o C. In some embodiments, the sugarcane bagasse ash was previously heated at a rate of between about 5 ^o C/min and about 20 ^o C/min (e.g., between about 5 ^o C/min and 15 ^o C/min, about 5 ^o C/min and about 10 ^o C/min, about 10 ^o C/min and 20 ^o C/min, or about 15 ^o C/min and 20 ^o C/min). In some embodiments, the sugarcane bagasse ash was previously heated PATENT ATTORNEY DOCKET: 51494-028WO2 at a rate of about 10 ^o C/min. In some embodiments, the sugarcane bagasse ash was previously heated for between about 1 hour and about 10 hours (e.g., about 1 hour and about 8 hours, about 1 hour and about 6 hours, about 1 hour and about 4 hours, about 1 hour and about 2 hours, about 2 hours and about 10 hours, about 4 hours and about 10 hours, about 6 hours and about 10 hours, or about 8 hours and about 10 hours). In some embodiments, the sugarcane bagasse ash was previously heated for about 5 hours. In some embodiments, the sugarcane bagasse ash is cooled to room temperature. In some embodiments, after the sugarcane bagasse ash is cooled to room temperature, the sugarcane bagasse ash is contacted with a few drops of hydrogen peroxide. In some embodiments, after the sugarcane bagasse ash is contacted with a few drops of hydrogen peroxide, it is heated to about 600 ^o C. In some embodiments, the sugarcane bagasse ash and hydrogen peroxide are heated to about 600 ^o C for about 5 hours, and then cooled to room temperature. In some embodiments, the polyurethane synthesis step has a final concentration of sugarcane bagasse ash of between about 2% (w/w) and about 10% (w/w) (e.g., between about 2% (w/w) and about 8% (w/w), about 2% (w/w) and about 6% (w/w), about 2% (w/w) and about 4% (w/w), about 4% (w/w) and about 10% (w/w), about 6% (w/w) and about 10% (w/w), or about 8% (w/w) and about 10% (w/w). In some embodiments, the polyurethane synthesis step has a final concentration of sugarcane bagasse ash of about 4.5% (w/w). In some embodiments, the isocyanate comprises one or more of toluene diisocyanate (TDI), methylenediphenyl diisocyanate (MDI), hexamethylene diisocyanate (HDI), or isophorone diisocyanate (IPDI). In some embodiments, the isocyanate comprises MDI. In some embodiments, the MDI comprises 4,4’-MDI. In some embodiments, the isocyanate has a final concentration of between about 25% (w/w) and about 75% (w/w) (e.g., between about 35% (w/w) and 75% (w/w), 45% (w/w) and 75% (w/w), 55% (w/w) and 75% (w/w), 65% (w/w) and 75% (w/w), 25% (w/w) and 65% (w/w), 25% (w/w) and 55% (w/w), 25% (w/w) and 45% (w/w), or 25% (w/w) and 35% (w/w)). In some embodiments, the isocyanate has a final concentration of between about 50% (w/w) and about 60% (w/w) (e.g., about 50% (w/w), 51% (w/w), 52% (w/w), 53% (w/w), 54% (w/w), 55% (w/w), 56% (w/w), 57% (w/w), 58% (w/w), 59% (w/w), or 60% (w/w)). In some embodiments, the blowing agent is water. In some embodiments, the water has a final concentration of between about 0.5% (w/w) and about 5% (w/w) (e.g., between about 1% (w/w) and 5% (w/w), 2% (w/w) and 5% (w/w), 3% (w/w) and 5% (w/w), 4% (w/w) and 5% (w/w), 0.5% (w/w) and 4% (w/w), 0.5% (w/w) and 3% (w/w), 0.5% (w/w) and 2% (w/w), or 0.5% (w/w) and 1% (w/w)). In some embodiments, the water has a final concentration of between about 1% (w/w) and about 3% (w/w) (e.g., about 1% (w/w), 2% (w/w), or 3% (w/w)). POLYESTER SYNTHESIS The method described herein may further include a polyester synthesis step. The polyester synthesis step may include reacting the monomer product (e.g., the polyol) with a dicarboxylic acid, a cross-linker, and a chain extender. The polyester synthesis step may be performed by melting the PATENT ATTORNEY DOCKET: 51494-028WO2 monomer product with the dicarboxylic acid, cross-linker, chain extender, and mechanical enhancer using heat. For example, in the polyester synthesis step, the monomer product may be reacted with a dicarboxylic acid, a cross-linker, chain extender, thereby producing a polyester product. The monomer product and the dicarboxylic acid may be present at a ratio of between about 2:1 (w/w) and about 1:2 (w/w) (e.g., between about 2:1 (w/w) and 1:1 (w/w) or between 1:1 and about 1:2 (w/w)). In some embodiments, the monomer product and the dicarboxylic acid are present at a ratio of about 3:2 (w/w). The monomer product and the cross-linker may be present at a ratio of between about 4:1 (w/w) and about 1:2 (w/w) (e.g., about 4:1 (w/w) and about 1:1 (w/w), about 4:1 (w/w) and about 2:1 (w/w), about 4:1 (w/w) and about 3:1 (w/w), about 3:1 (w/w) and about 1:2 (w/w), about 2:1 (w/w) and about 1:2 (w/w), or about 1:1 (w/w) and about 1:2 (w/w)). In some embodiments, the monomer product and the cross-linker are present at a ratio of about 2:1 (w/w). The monomer product and the chain extender may be present at a ratio of between about 4:1 (w/w) and about 1:1 (w/w) (e.g., between about 4:1 (w/w) and about 2:1 (w/w), about 4:1 (w/w) and about 3:1 (w/w), about 3:1 (w/w) and about 1:1 (w/w), or about 2:1 (w/w) and about 1:1 (w/w)). For example, the monomer product and the chain extender may be present at a ratio of about 3:1 (w/w). The dicarboxylic acid may be, for example, azelaic acid or phthalic acid. The cross-linker may be citric acid. The chain extender may be 1,4-butanediol, sorbitol, or glycerol. In some embodiments, the chain extender is 1,4-butanediol and sorbitol. The dicarboxylic acid, cross-linker, and chain extender may be mixed for between 10 minutes and 2 hours (e.g., between 10 minutes and 90 minutes, 10 minutes and 60 minutes, 10 minutes and 30 minutes, 30 minutes and 2 hours, 1 hour and 2 hours, 90 minutes and 2 hours, or 30 minutes and 90 minutes). For example, the dicarboxylic acid, cross-linker, and chain extender may be mixed for about 1 hour. In some embodiments, the dicarboxylic acid, cross-linker, and chain extender are mixed under nitrogen. In some embodiments, the phthalic acid is mixed with 1,4–butanediol and citric acid for between 10 minutes and 2 hours. In some embodiments, sorbitol is added to the mixture including phthalic acid is mixed with 1,4–butanediol and citric acid. In some embodiments, the mixture including phthalic acid, 1,4-butanediol, citric acid, and sorbitol is mixed for between about 5 minutes and about 1 hour (e.g., between 5 minutes and 50 minutes, 5 minutes and 40 minutes, 5 minutes and 30 minutes, 5 minutes and 20 minutes, 5 minutes and 10 minutes, 10 minutes and 1 hour, 20 minutes and 1 hour, 30 minutes and 1 hour, 40 minutes and 1 hour, 50 minutes and 1 hour, or 20 minutes and 40 minutes). The monomer product and the dicarboxylic acid may be present at a ratio of between about 2:1 (w/w) and about 1:2 (w/w) (e.g., between about 2:1 (w/w) and 1:1 (w/w) or between 1:1 and about 1:2 (w/w)). For example, the monomer product and the dicarboxylic acid may be present at a ratio of about 3:2 (w/w). The monomer product and the cross-linker may be present at a ratio of between about 4:1 (w/w) and about 1:2 (w/w) (e.g., about 4:1 (w/w) and about 1:1 (w/w), about 4:1 (w/w) and about 2:1 (w/w), about 4:1 (w/w) and about 3:1 (w/w), about 3:1 (w/w) and about 1:2 (w/w), about 2:1 (w/w) and PATENT ATTORNEY DOCKET: 51494-028WO2 about 1:2 (w/w), or about 1:1 (w/w) and about 1:2 (w/w)); for example, the monomer product and the cross-linker may be present at a ratio of about 2:1 (w/w). The monomer product and the chain extender may be present at a ratio of between about 4:1 (w/w) and about 1:1 (w/w) (e.g., between about 4:1 (w/w) and about 2:1 (w/w), about 4:1 (w/w) and about 3:1 (w/w), about 3:1 (w/w) and about 1:1 (w/w), or about 2:1 (w/w) and about 1:1 (w/w)). For example, the monomer synthesis product and the chain extender may be present at a ratio of about 3:1 (w/w). The dicarboxylic acid may include azelaic acid or phthalic acid. The cross-linker may include citric acid. The chain extender and mechanical enhancer may include 1,4-butanediol and sorbitol. In some embodiments, the 1,4-butanediol and sorbitol are present at a ratio of about 1:1 (w/w). The polyester synthesis product is dried for between about 24 hours and about 72 hours (e.g., between about 24 hours and 60 hours, about 24 hours and 48 hours, about 24 hours and 36 hours, 36 hours and 72 hours, 48 hours and 72 hours, or 60 hours and 72 hours), such as for about 48 hours. The polyester synthesis step may be performed at a temperature of between about 120 ^o C and about 200 ^o C (e.g., between about 150 ^o C and 200 ^o C, 175 ^o C and 200 ^o C, 120 ^o C and 175 ^o C, or 120 ^o C and 150 ^o C). For example, the polyester synthesis step may be performed at a temperature of between about 140 ^o C and about 180 ^o C (e.g., between about 140 ^o C and 170 ^o C, 140 ^o C and 160 ^o C, 140 ^o C and 150 ^o C, 150 ^o C and 180 ^o C, 160 ^o C and 180 ^o C, or 170 ^o C and 180 ^o C). In some embodiments, the polyester synthesis step is performed at a temperature of about 160 ^o C. The polyester synthesis step may be performed for between about 30 minutes and about 4 hours (e.g., between about 1 hour and 4 hours, 2 hours and 4 hours, 3 hours and 4 hours, 30 minutes and 3 hours, 30 minutes and 2 hours, or 30 minutes and 1 hour). For example, the polyester synthesis step may be performed for between about 1 hour and about 3 hours (e.g., between 1 hour and 2 hours, between 2 hours and 3 hours). In some embodiments, the polyester synthesis step is performed for about 2 hours. The polyester synthesis product may be dried for between about 1 day and about 5 days (e.g., between about 1 day and about 4 days, about 1 day and 3 days, about 1 day and 2 days, about 2 days and 5 days, about 3 days and 5 days, or about 4 days and 5 days); for example, the polyester synthesis product may be dried for between about 2 days and about 4 days (e.g., about 2 days, about 3 days, and about 4 days). In some embodiments, the polyester synthesis product is dried for about 3 days. In some embodiments, the polyester synthesis product is dried for about 2 days. The polyester synthesis product may be dried at a temperature of between about 100 ^o C and about 180 ^o C (e.g., between about 100 ^o C and about 160 ^o C, about 100 ^o C and about 140 ^o C, about 100 ^o C and about 120 ^o C, about 120 ^o C and about 180 ^o C, about 140 ^o C and about 180 ^o C, or about 160 ^o C and about 180 ^o C), such a temperature of between about 120 ^o C and about 160 ^o C (e.g., between about 120 ^o C and about 150 ^o C, about 120 ^o C and about 140 ^o C, about 120 ^o C and about 130 ^o C, about 130 ^o C and about 160 ^o C, about 140 ^o C and about 160 ^o C, or about 150 ^o C and about 160 ^o C). In some embodiments, the polyester synthesis product was dried at a temperature of about 140 ^o C. In some embodiments, the polyester synthesis product was dried at a temperature of about 150 ^o C. PATENT ATTORNEY DOCKET: 51494-028WO2 The resulting polyester product may be unsaturated aliphatic polyesters. The polyester product may be characterized in terms of surface wettability. For example, the polyester product may have a surface wettability of between about 40 ^o and about 85 ^o (e.g., between about 40 ^o and about 60 ^o , about 40 ^o and about 50 ^o , about 50 ^o and about 85 ^o , about 60 ^o and about 85 ^o , or about 70 ^o and about 85 ^o ) when tested with water. In some embodiments, the polyester product may have a surface wettability of between about 5 ^o and about 40 ^o (e.g., between about 5 ^o and about 30 ^o , about 5 ^o and about 20 ^o , about 5 ^o and about 20 ^o , about 5 ^o and about 10 ^o , about 10 ^o and about 40 ^o , about 10 ^o and about 40 ^o , or about 30 ^o and about 40 ^o ) when tested with squalane. For example, the polyester product may have surface wettability of between about 8 ^o and about 35 ^o (e.g., about 10 ^o and about 30 ^o , about 10 ^o and about 20 ^o , about 20 ^o and about 35 ^o , or about 25 ^o and about 35 ^o ) when tested with squalane. Enzymes of Exemplary Biosynthetic Pathways The host cells (and/or the previously fermented cells) described herein may express one or more enzymes of a biosynthetic pathway capable of producing a fermentation product of interest. In some embodiments, for example, host cells and/or previously fermented cells of the disclosure (e.g., yeast cells) may naturally express some of the enzymes of the biosynthetic pathway for a given fermentation product. Such cells may be modified to express the remaining or heterologous enzymes of the biosynthetic pathway. In some embodiments, for instance, a cell (e.g., a yeast cell) may naturally express many of the enzymes of the biosynthetic pathway of a desired fermentation product, and the cells may be modified so as to express the remaining enzymes of the biosynthetic pathway for the desired fermentation product by providing the cells with one or more heterologous nucleic acid molecules that, together, encode the remaining enzymes of the biosynthetic pathway. In some embodiments, the cells may be genetically modified to produce a fermentation product. The cells may produce a fermentation product such as, for example, an isoprene, an isoprenoid, a human milk oligosaccharide (HMO), a steviol glycoside, or a cannabinoid. Isoprenoid Biosynthetic Pathway The cells described herein may be modified to express one or more enzymes of the mevalonate-dependent (MEV) biosynthetic pathway. Cells which are modified with one or more enzymes of the MEV biosynthetic pathway may be capable of an increased production of one or more isoprenoid compounds as compared to cell which is not modified with one or enzymes of the MEV biosynthetic pathway. In some embodiments, the isoprenoid producing cell comprises a heterologous nucleotide sequence encoding an enzyme that can condense two molecules of acetyl-coenzyme A to form acetoacetyl-CoA, e.g., an acetyl-CoA thiolase. Illustrative examples of nucleotide sequences encoding such an enzyme include but are not limited to: (NC_000913 REGION: 2324131.2325315; Escherichia coli), (D49362; Paracoccus denitrifzcans), and (L20428; Saccharomyces cerevisiae). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme that can condense acetoacetyl-CoA with another molecule of acetyl-CoA to form 3-hydroxy- PATENT ATTORNEY DOCKET: 51494-028WO2 3-methylglutaryl-CoA (HMG-CoA), e.g., a HMGCoA synthase. Illustrative examples of nucleotide sequences encoding such an enzyme include but are not limited to: (NC_00l 145. Complement 19061.20536; Saccharomyces cerevisiae), (X96617; Saccharomyces cerevisiae), (X83882; Arabidopsis thaliana), (AB037907; Kitasatospora griseola), (BT007302; Homo sapiens), and (NC_002758, Locus tag SAV2546, GeneID 1122571; Staphylococcus aureus). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme that can convert HMG-CoA into mevalonate, e.g., an HMG-CoA reductase. Illustrative examples of nucleotide sequences encoding such an enzyme include, but are not limited to: (NM_206548; Drosophila melanogaster), (NC_002758, Locus tag SAV2545, GeneID 1122570; Staphylococcus aureus), (NM_204485; Gallus gallus), (AB015627; Streptomyces sp. KO 3988), (AF542543; Nicotiana attenuata), (AB037907; Kitasatospora griseola), (AX128213, providing the sequence encoding a truncated HMGR; Saccharomyces cerevisiae), and (NC_001145: complement (115734.118898; Saccharomyces cerevisiae). In some embodiments, the cells include a heterologous nucleotide sequence encoding an enzyme that can convert mevalonate into mevalonate 5-phosphate, e.g., a mevalonate kinase. Illustrative examples of nucleotide sequences encoding such an enzyme include but are not limited to: (L77688; Arabidopsis thaliana), and (X55875; Saccharomyces cerevisiae). In some embodiments, the cells include a heterologous nucleotide sequence encoding an enzyme that can convert mevalonate 5-phosphate into mevalonate 5-pyrophosphate, e.g., a phosphomevalonate kinase. Illustrative examples of nucleotide sequences encoding such an enzyme include but are not limited to: (Af 429385; Hevea brasiliensis), (NM_006556; Homo sapiens), and (NC_00l 145. Complement 712315.713670; Saccharomyces cerevisiae). In some embodiments, the cells include a heterologous nucleotide sequence encoding an enzyme that can convert mevalonate 5-pyrophosphate into isopentenyl diphosphate (IPP), e.g., a mevalonate pyrophosphate decarboxylase. Illustrative examples of nucleotide sequences encoding such an enzyme include but are not limited to: (X97557; Saccharomyces cerevisiae), (AF290095; Enterococcus faecium), and (U49260; Homo sapiens). In some embodiments, the cells include one or more heterologous nucleotide sequences encoding more than one enzyme of the MEV pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding two enzymes of the MEV pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding an enzyme that can convert HMG-CoA into mevalonate and an enzyme that can convert mevalonate into mevalonate 5-phosphate. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding three enzymes of the MEV pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding four enzymes of the MEV pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding five enzymes of the MEV pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding six enzymes of the MEV pathway. PATENT ATTORNEY DOCKET: 51494-028WO2 In some embodiments, the cell further includes a heterologous nucleotide sequence encoding an enzyme that can convert IPP generated via the MEV pathway into its isomer, dimethylallyl pyrophosphate (DMAPP). DMAPP can be condensed and modified through the action of various additional enzymes to form simple and more complex isoprenoids. The cells described herein may be modified to express one or more enzymes of the 1-deoxy- D-xylulose 5-diphosphate (DXP) biosynthetic pathway. Cells which are modified with one or more enzymes of the DXP biosynthetic pathway may be capable of an increased production of one or more isoprenoid compounds as compared to cell which is not modified with one or enzymes of the DXP biosynthetic pathway. In some embodiments, the cells include a heterologous nucleotide sequence encoding an enzyme that can condense two molecules of acetyl-coenzyme A to form acetoacetyl-CoA, e.g., an acetyl-CoA thiolase. Illustrative examples of nucleotide sequences encoding such an enzyme include but are not limited to: (NC_000913 REGION: 2324131.2325315; Escherichia coli), (D49362; Paracoccus denitrifzcans), and (L20428; Saccharomyces cerevisiae). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme, e.g., l-deoxy-D-xylulose-5-phosphate synthase, which can condense pyruvate with D- glyceraldehyde 3-phosphate to make l-deoxy-D-xylulose- 5-phosphate. Illustrative examples of nucleotide sequences encoding such an enzyme include but are not limited to: (AF035440; Escherichia coli), (NC_002947, locus tag PP0527; Pseudomonas putida KT2440), (CP000026, locus tag SPA2301; Salmonella enterica Paratyphi, see ATCC 9150), (NC_007493, locus tag RSP _0254; Rhodobacter sphaeroides 2.4.1 ), (NC_ 005296, locus tag RP A0952; Rhodopseudomonas palustris CGA009), (NC_004556, locus tag PD1293; Xylellafastidiosa Temecula]), and (NC_003076, locus tag AT5Gl 1380; Arabidopsis thaliana). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme, e.g., l-deoxy-D-xylulose-5-phosphate reductoisomerase, which can convert l-deoxy-D- xylulose-5-phosphate to 2C-methyl-Derythritol- 4-phosphate. Illustrative examples of nucleotide sequences include but are not limited to: (AB013300; Escherichia coli), (AF148852; Arabidopsis thaliana), (NC_002947, locus tag PP1597; Pseudomonas putida KT2440), (AL939124, locus tag SCO5694; Streptomyces coelicolor A3(2)), (NC_007493, locus tag RSP 2709; Rhodobacter sphaeroides 2.4.1), and (NC_007492, locus tag Pfl_l 107; Pseudomonas jluorescens PfO-1). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme, e.g., 4-diphosphocytidyl-2C-methyl-D-erythritol synthase, which can convert 2C-methyl-D- erythritol-4-phosphate to 4-diphosphocytidyl-2Cmethyl-D-erythritol. Illustrative examples of nucleotide sequences include but are not limited to: (AF230736; Escherichia coli), (NC_007493, locus tag RSP 2835; Rhodobacter sphaeroides 2.4.1), (NC_003071, locus tag AT2G02500; Arabidopsis thaliana), and (NC_002947, locus tag PP1614; Pseudomonas putida KT2440). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme, e.g., 4-diphosphocytidyl-2C-methyl-D-erythritol kinase, which can convert 4- diphosphocytidyl-2C-methyl-D-erythritol to 4-diphosphocytidyl-2C-methyl-D-erythritol-2-phosphate. PATENT ATTORNEY DOCKET: 51494-028WO2 Illustrative examples of nucleotide sequences include but are not limited to: (AF216300; Escherichia coli) and (NC_007493, locus tag RSP 1779; Rhodobacter sphaeroides 2.4.1). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme, 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, which can convert 4- diphosphocytidyl-2C-methyl-D-erythritol-2-phosphate to 2Cmethyl-D-erythritol 2,4-cyclodiphosphate. Illustrative examples of nucleotide sequences include but are not limited to: (AF230738; Escherichia coli), (NC_007493, locus tag RSP _6071; Rhodobacter sphaeroides 2.4.1), and (NC_002947, locus tag PP1618; Pseudomonas putida KT2440). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme, e.g., l-hydroxy-2-methyl-2-(E)-butenyl-4- diphosphate synthase, which can convert 2C- methyl-D-erythritol 2,4-cyclodiphosphate to 1- hydroxy-2-methy 1-2-(E)-butenyl 1-4-di phosphate. Illustrative examples of nucleotide sequences include but are not limited to: (AY033515; Escherichia coli), (NC_002947, locus tag PP0853; Pseudomonas putida KT2440), and (NC_007493, locus tag RSP 2982; Rhodobacter sphaeroides 2.4.1). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme, e.g., isopentyl/dimethylallyl diphosphate synthase, which can convert l-hydroxy-2-methyl-2- (E)-butenyl-4-diphosphate into either IPP or its isomer, DMAPP. Illustrative examples of nucleotide sequences include but are not limited to: (AY062212; Escherichia coli) and (NC_002947, locus tag PP0606; Pseudomonas putida KT2440). In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding more than one enzyme of the DXP pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding two enzymes of the DXP pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding three enzymes of the DXP pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding four enzymes of the DXP pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding five enzymes of the DXP pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding six enzymes of the DXP pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding five enzymes of the DXP pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding seven enzymes of the DXP pathway. In some embodiments, "cross talk" (or interference) between the cell's own metabolic processes and those processes involved with the production of IPP are minimized or eliminated entirely. For example, cross talk is minimized or eliminated entirely when the cell relies exclusively on the DXP pathway for synthesizing IPP, and a MEV pathway is introduced to provide additional IPP. Such a cell would not be equipped to alter the expression of the MEV pathway enzymes or process the intermediates associated with the MEV pathway. Organisms that rely exclusively or predominately on the DXP pathway include, for example, Escherichia coli. In some embodiments, the cell produces IPP via the MEV pathway, either exclusively or in combination with the DXP pathway. In other embodiments, a cell’s DXP pathway is functionally PATENT ATTORNEY DOCKET: 51494-028WO2 disabled so that the cell produces IPP exclusively through a heterologously introduced MEV pathway. The DXP pathway can be functionally disabled by disabling gene expression or inactivating the function of one or more of the DXP pathway enzymes. In some embodiments, the cell further includes a heterologous nucleotide sequence encoding a polyprenyl synthase that can condense IPP and/or DMAPP molecules to form polyprenyl compounds containing more than five carbons. In some embodiments, the isoprenoid producing cell further comprises a heterologous nucleotide sequence encoding an enzyme that can convert IPP generated via the MEV pathway into DMAPP, e.g., an IPP isomerase. Illustrative examples of nucleotide sequences encoding such an enzyme include but are not limited to: (NC_000913, 3031087.3031635; Escherichia coli), and (AF082326; Haematococcus pluvialis). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme that can condense one molecule of IPP with one molecule of DMAPP to form one molecule of geranyl pyrophosphate (GPP), e.g., a GPP synthase. Illustrative examples of nucleotide sequences encoding such an enzyme include, but are not limited to: (AF513lll;Abies grandis), (AF513112;Abies grandis), (AF513113;Abies grandis), (AY534686; Antirrhinum majus), (AY534687; Antirrhinum majus), (Yl 7376; Arabidopsis thaliana), (AE016877, Locus APl 1092; Bacillus cereus; ATCC 14579), (AJ243739; Citrus sinensis), (AY534745; Clarkia breweri), (AY953508; fps pini), (DQ286930; Lycopersicon esculentum), (AF182828; Mentha x piperita), (AF182827; Mentha x piperita), (MPI249453; Mentha x piperita), (PZE431697, Locus CAD24425; Paracoccus l 862; Vi tis vinifera), and (AF203881, Locus In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme that can condense two molecules of IPP with one molecule of DMAPP or add a molecule of IPP to a molecule of GPP, to form a molecule of farnesyl pyrophosphate (FPP), e.g., a FPP synthase. Illustrative examples of nucleotide sequences that encode such an enzyme include, but are not limited to: (ATU80605; Arabidopsis thaliana), (ATHFPS2R; Arabidopsis thaliana), (AAU36376; Artemisia annua), (AF461050; Bos taurus), (D00694; Escherichia coli K-12), (AE009951, Locus AAL95523; Fusobacterium nucleatum subsp. nucleatum ATCC 25586), (GFFPPSGEN; Gibberella Jujikuroi), (CP000009, Locus AAW60034; Gluconobacter oxydans 621H), (AF019892; Helianthus annuus ), (HUMP APS; Homo sapiens), (KLPFPSQCR; Kluyveromyces lactis ), (LAU15777; Lupinus albus), (LAU20771; Lupinus albus), (AF309508; Mus musculus), (NCFPPSGEN; Neurospora crassa), (PAFPSl; Parthenium argentatum), (PAFPS2; Parthenium argentatum), (RA TF APS; Rattus norvegicus), (YSCFPP; Saccharomyces cerevisiae), (D89104; SchizoSaccharomyces pombe), (CP000003, Locus AAT87386; Streptococcus pyogenes), (CP0000l 7, Locus AAZ51849; Streptococcus pyogenes), (NC_ 008022, Locus YP 598856; Streptococcus pyogenes MGAS 10270), (NC_ 008023, Locus YP 600845; Streptococcus pyogenes MGAS2096), (NC_008024, Locus YP 602832; Streptococcus pyogenes MGAS10750), (MZEFPS; Zea mays), (AE000657, Locus AAC06913; Aquifex aeolicus VF5), (NM_202836; Arabidopsis thaliana), (D84432, Locus BAA12575; Bacillus subtilis), (Ul2678, Locus AAC28894; Bradyrhizobiumjaponicum USDA 110), (BACFDPS; PATENT ATTORNEY DOCKET: 51494-028WO2 Geobacillus stearothermophilus), (NC_002940, Locus NP 873754; Haemophilus ducreyi 35000HP), (L42023, Locus AAC23087; Haemophilus injluenzae Rd KW20), (J05262; Homo sapiens), (YP 395294; Lactobacillus sakei subsp. sakei 23K), (NC_005823, Locus YP 000273; Leptospira interrogans serovar Copenhageni str. Fiocruz Ll-130), (AB003187; Micrococcus luteus), (NC_002946, Locus YP _208768; Neisseria gonorrhoeae FA 1090), (U00090, Locus AAB91752; Rhizobium sp. NGR234), (J05091; Saccharomyces cerevisiae), (CP000031, Locus AAV93568; Silicibacter pomeroyi DSS-3), (AE008481, Locus AAK99890; Streptococcus pneumoniae R6), and (NC_ 004556, Locus NP 779706; Xylella fastidiosa Temecula1). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme that can combine IPP and DMAPP or IPP and FPP to form geranylgeranyl pyrophosphate (GGPP). Illustrative examples of nucleotide sequences that encode such an enzyme include, but are not limited to: (ATHGERPYRS; Arabidopsis thaliana), (BT005328; Arabidopsis thaliana), (NM_l 19845; Arabidopsis thaliana), (NZ_AAJM01000380, Locus ZP 00743052; Bacillus thuringiensis serovar israelensis, ATCC 35646 sql563), (CRGGPPS; Catharanthus roseus), (NZ_AABF02000074, Locus ZP 00144509; Fusobacterium nucleatum subsp. vincentii, ATCC 49256), (GFGGPPSGN; Gibberellafujikuroi), (AY371321; Ginkgo biloba), (AB055496; Hevea brasiliensis), (AB0l 7971; Homo sapiens), (MCI276129; Mucor circinelloides f. lusitanicus), (AB016044; Mus musculus), (AABX01000298, Locus NCU01427; Neurospora crassa), (NCU20940; Neurospora crassa), (NZ_AAKL01000008, Locus ZP 00943566; Ralstonia solanacearum UW551), (ABl 18238; Rattus norvegicus), (SCU31632; Saccharomyces cerevisiae), (AB016095; Synechococcus elongates), (SAGGPS; Sinapis alba), (SSOGDS; Sulfolobus acidocaldarius), (NC_007759, Locus YP 461832; Syntrophus aciditrophicus SB), (NC_006840, Locus YP 204095; Vibrio jischeri ESl 14), (NM_ 112315; Arabidopsis thaliana), (ERWCR TE; Pantoea agglomerans), (D90087, Locus BAA14124; Pantoea ananatis), (X52291, Locus CAA36538; Rhodobacter capsulatus), (AF195122, Locus AAF24294; Rhodobacter sphaeroides), and (NC_004350, Locus NP 721015; Streptococcus mutans UA159). In some embodiments, the cell further includes a heterologous nucleotide sequence encoding an enzyme that can modify a polyprenyl to form a hemiterpene, a monoterpene, a sesquiterpene, a diterpene, a triterpene, a tetraterpene, a polyterpene, a steroid compound, a carotenoid, or a modified isoprenoid compound. In some embodiments, the heterologous nucleotide encodes a carene synthase. Illustrative examples of suitable nucleotide sequences include, but are not limited to: (AF461460, REGION 43.1926; Picea abies) and (AF527416, REGION: 78.1871; Salvia stenophylla). In some embodiments, the heterologous nucleotide encodes a geraniol synthase. Illustrative examples of suitable nucleotide sequences include but are not limited to: (Af 457070; Cinnamomum tenuipilum), (A Y362553; Ocimum basilicum), (DQ234300; Perilla frutescens strain 1864), (DQ234299; Perilla citriodora strain 1861), (DQ234298; Perilla citriodora strain 4935), and (DQ088667; Perilla citriodora). In some embodiments, the heterologous nucleotide encodes a linalool synthase. Illustrative examples of a suitable nucleotide sequence include, but are not limited to: (AF497485; Arabidopsis thaliana), (AC002294, Locus AAB71482; Arabidopsis thaliana), (AY059757; Arabidopsis thaliana), PATENT ATTORNEY DOCKET: 51494-028WO2 (NM_104793; Arabidopsis thaliana), (AF154124; Artemisia annua), (AF067603; Clarkia breweri), (AF067602; Clarkia concinna), (AF067601; Clarkia breweri), (U58314; Clarkia breweri), (AY840091; Lycopersicon esculentum), (DQ263741; Lavandula angustifolia), (AY083653;Mentha citrate), (AY693647; Ocimum basilicum), (XM_ 463918; Oryza sativa), (AP004078, Locus BAD07605; Oryza sativa), (XM_ 463918, Locus XP _ 463918; Oryza sativa), (AY917193; Perilla citriodora), (AF271259; Perillafrutescens), (AY473623; Picea abies), (DQ195274; Picea sitchensis), and (AF444798; Perilla frutescens var. crispa cultivar No.79). In some embodiments, the heterologous nucleotide encodes a limonene synthase. Illustrative examples of suitable nucleotide sequences include but are not limited to:(+) limonene synthases (AF514287, REGION: 47.1867; Citrus limon) and (AY055214, REGION: 48.1889; Agastache rugosa) and (-)-limonene synthases (DQ195275, REGION: 1.1905; Picea sitchensis), (AF006193, REGION: 73.1986;Abies grandis), and (MHC4SLSP, REGION: 29.1828; Mentha spicata). In some embodiments, the heterologous nucleotide encodes a myrcene synthase. Illustrative examples of suitable nucleotide sequences include, but are not limited to: (U87908; Abies grandis), (A Yl 95609; Antirrhinum majus), (A Yl 95608; Antirrhinum majus), (NM_l27982; Arabidopsis thaliana TPSlO), (NM_ll3485; Arabidopsis thaliana ATTPS-CIN), (NM_ 113483; Arabidopsis thaliana ATTPS- CIN), (AF271259; Perilla frutescens), (AY473626; Picea abies), (AF369919; Picea abies), and (AJ304839; Quercus ilex). In some embodiments, the heterologous nucleotide encodes an ocimene synthase. Illustrative examples of suitable nucleotide sequences include, but are not limited to: (AYl 95607; Antirrhinum majus), (A Yl 95609; Antirrhinum majus), (A Yl 95608; Antirrhinum majus), (AK221024; Arabidopsis thaliana), (NM_ 113485; Arabidopsis thaliana ATTPS-CIN), (NM_ll3483; Arabidopsis thaliana ATTPS-CIN), (NM_ll 7775; Arabidopsis thaliana ATTPS03), (NM_001036574; Arabidopsis thaliana ATTPS03), (NM_l27982; Arabidopsis thaliana TPS 10), (AB 110642; Citrus unshiu CitMTSL4), and (AY575970; Lotus corniculatus var. Japonicus ). In some embodiments, the heterologous nucleotide encodes an aα-pinene synthase. Illustrative examples of suitable nucleotide sequences include but are not limited to: (+) α-pinene synthase (AF543530, REGION: 1.1887; Pinus taeda), (-) α-pinene synthase (AF543527, REGION: 32.1921; Pinus taeda), and (+)/ (-)a-pinene synthase (AGU87909, REGION: 6111892;Abies grandis). In some embodiments, the heterologous nucleotide encodes a P-pinene synthase. Illustrative examples of suitable nucleotide sequences include but are not limited to: (-) Ppinene synthases (AF276072, REGION: 1.1749; Artemisia annua) and (AF514288, REGION: 26.1834; Citrus limon). In some embodiments, the heterologous nucleotide encodes a sabinene synthase. An illustrative example of a suitable nucleotide sequence includes but is not limited to AF05 l 901, REGION: 26.1798 from Salvia ofjicinalis. In some embodiments, the heterologous nucleotide encodes a y-terpinene synthase. Illustrative examples of suitable nucleotide sequences include, but are not limited to: (AF514286, REGION: 30.1832 from Citrus limon) and (ABl 10640, REGION 1.1803 from Citrus unshiu). PATENT ATTORNEY DOCKET: 51494-028WO2 In some embodiments, the heterologous nucleotide encodes a terpinolene synthase. Illustrative examples of a suitable nucleotide sequence include but are not limited to: (AY693650 from Ocimum basilicum) and (AY906866, REGION: 10.1887 from Pseudotsuga menziesii). In some embodiments, the heterologous nucleotide encodes an amorphadiene synthase. An illustrative example of a suitable nucleotide sequence is SEQ ID NO.37 of U.S. Patent Publication No.2004/0005678. In some embodiments, the heterologous nucleotide encodes an α-farnesene synthase. Illustrative examples of suitable nucleotide sequences include but are not limited to DQ309034 from Pyrus communis cultivar d'Anjou (pear; gene name AFSl) and AY182241 from Malus domestica (apple; gene AFSl). Pechouus et al., Planta 219(1):84-94 (2004). In some embodiments, the heterologous nucleotide encodes a β-farnesene synthase. Illustrative examples of suitable nucleotide sequences include but are not limited to GenBank accession number AF024615 from Mentha x piperita (peppermint; gene Tspal 1), and A Y835398 from Artemisia annua. Picaud et al., Phytochemistry 66(9): 961-967 (2005). In some embodiments, the heterologous nucleotide encodes a farnesol synthase. Illustrative examples of suitable nucleotide sequences include but are not limited to GenBank accession number AF529266 from Zea mays and YDR481C from Saccharomyces cerevisiae (gene Pho8). Song, L., Applied Biochemistry and Biotechnology 128: 149-158 (2006). In some embodiments, the heterologous nucleotide encodes a nerolidol synthase. An illustrative example of a suitable nucleotide sequence includes but is not limited to AF529266 from Zea mays (maize; gene tpsl). In some embodiments, the heterologous nucleotide encodes a patchoulol synthase. Illustrative examples of suitable nucleotide sequences include but are not limited to AY508730 REGION: 1.1659 from Pogostemon cablin. In some embodiments, the heterologous nucleotide encodes a nootkatone synthase. Illustrative examples of a suitable nucleotide sequence include but are not limited to AF441124 REGION: 1.1647 from Citrus sinensis and AY917195 REGION: 1.1653 from Perilla frutescens. In some embodiments, the heterologous nucleotide encodes an abietadiene synthase. Illustrative examples of suitable nucleotide sequences In some embodiments, one or more heterologous nucleic acids encoding one or more enzymes are integrated into the genome of the cell. In some embodiments, one or more heterologous nucleic acids encoding one or more enzymes are present within one or more plasmids. Cannabinoid Biosynthetic Pathway The cell may include one or more nucleic acids encoding one or more enzymes of a heterologous genetic pathway that produces a cannabinoid or a precursor of a cannabinoid. The cannabinoid biosynthetic pathway may begin with hexanoic acid as the substrate for an acyl activating enzyme (AAE) to produce hexanoyl-CoA, which is used as the substrate of a tetraketide synthase (TKS) to produce tetraketide-CoA, which is used by an olivetolic acid cyclase (OAC) to produce olivetolic acid, which is then used to produce a cannabigerolic acid by a geranyl pyrophosphate (GPP) PATENT ATTORNEY DOCKET: 51494-028WO2 synthase and a cannabigerolic acid synthase (CBGaS). In some embodiments, the cannabinoid precursor that is produced is a substrate in the cannabinoid pathway (e.g., hexanoate or olivetolic acid). In some embodiments, the precursor is a substrate for an AAE, a TKS, an OAC, a CBGaS, or a GPP synthase. In some embodiments, the precursor, substrate, or intermediate in the cannabinoid pathway is hexanoate, olivetol, or olivetolic acid. In some embodiments, the precursor is hexanoate. In some embodiments, the cell does not contain the precursor, substrate or intermediate in an amount sufficient to produce the cannabinoid or a precursor of the cannabinoid. In some embodiments, the cell does not contain hexanoate at a level or in an amount sufficient to produce the cannabinoid in an amount over 10 mg/L. In some embodiments, the heterologous genetic pathway encodes at least one enzyme selected from the group consisting of an AAE, a TKS, an OAC, a CBGaS, or a GPP synthase. In some embodiments, the genetically modified cell includes an AAE, TKS, OAC, CBGaS, and a GPP synthase. The cannabinoid pathway is described in Keasling et al., U.S. Patent No. 10,563,211, the disclosure of which is incorporated herein by reference. The cell may include, in some embodiments, a heterologous AAE such that the cell is capable of producing a cannabinoid. The AAE may be from Cannabis sativa or may be an enzyme from another plant or fungal source which has been shown to have AAE activity in the cannabinoid biosynthetic pathway, resulting in the production of the cannabinoid precursor olivetolic acid In some embodiments, the cell may include a heterologous TKS such that the cell is capable of producing a cannabinoid. A TKS uses the hexanoyl-CoA precursor to generate tetraketide-CoA. The TKS may be from Cannabis sativa or may be an enzyme from another plant or fungal source which has been shown to have TKS activity in the cannabinoid biosynthetic pathway, resulting in the production of the cannabinoid precursor olivetolic acid. Some embodiments concern a cell that includes a heterologous CBGaS such that the cell is capable of producing a cannabinoid. A CBGaS uses the olivetolic acid precursor and GPP precursor to generate cannabigerolic acid. The CBGaS may be from Cannabis sativa or may be an enzyme from another plant or fungal source which has been shown to have CBGaS activity in the cannabinoid biosynthetic pathway, resulting in the production of the cannabinoid cannabigerolic acid. Some embodiments concern a cell that includes a heterologous GPP synthase such that the cell is capable of producing a cannabinoid. A GPP synthase uses the product of the isoprenoid biosynthesis pathway precursor to generate cannabigerolic acid together with a prenyltransferase enzyme. The GPP synthase may be from Cannabis sativa or may be an enzyme from another plant or bacterial source which has been shown to have GPP synthase activity in the cannabinoid biosynthetic pathway, resulting in the production of the cannabinoid cannabigerolic acid. The population of cells may further express other heterologous enzymes in addition to the AAE, TKS, CBGaS, and/or GPP synthase. For example, in some embodiments, the cell may include a heterologous nucleic acid that encodes at least one enzyme from the mevalonate biosynthetic pathway. Enzymes which make up the mevalonate biosynthetic pathway may include but are not limited to an acetyl-CoA thiolase, an HMG-CoA synthase, an HMG-CoA reductase, a mevalonate kinase, a phosphomevalonate kinase, a mevalonate pyrophosphate decarboxylase, and an IPP: DMAPP isomerase. In some embodiments, the cell includes a heterologous nucleic acid that PATENT ATTORNEY DOCKET: 51494-028WO2 encodes the acetyl-CoA thiolase, the HMG-CoA synthase, the HMG-CoA reductase, the mevalonate kinase, the phosphomevalonate kinase, the mevalonate pyrophosphate decarboxylase, and the IPP: DMAPP isomerase of the mevalonate biosynthesis pathway. In some embodiments, the cell may include an olivetolic acid cyclase (OAC) as part of the cannabinoid biosynthetic pathway. In some embodiments, the cell further includes one or more heterologous nucleic acids that each, independently, encode an acetyl-CoA synthase, and/or an aldehyde dehydrogenase, and/or a pyruvate decarboxylase. In some embodiments, the cell contains a heterologous nucleic acid encoding an aceto-CoA carboxylase (ACC). In some embodiments, the cell contains a heterologous nucleic acid encoding an ACC and an acetoacetyl-CoA synthase (AACS) instead of a heterologous nucleic acid encoding an acetyl-CoA thiolase. Human Milk Oligosaccharide Biosynthetic Pathway In addition to being modified so as to be deficient in expression and/or activity of one or more endogenous oxidoreductases (e.g., one or more endogenous aldose reductases described herein), cells of the disclosure may also be modified so as to express the enzymes of the biosynthetic pathway of a target HMO. In some embodiments, for example, cells of the disclosure (e.g., yeast cells) may naturally express some of the enzymes of the biosynthetic pathway for a given HMO. Such cells may be modified to express the remaining enzymes of the biosynthetic pathway. In some embodiments, for instance, a cell (e.g., a yeast cell) may naturally express many of the enzymes of the biosynthetic pathway of a desired HMO, and the cells may be modified so as to express the remaining enzymes of the biosynthetic pathway for the desired HMO by providing the cells with one or more heterologous nucleic acid molecules that, together, encode the remaining enzymes of the biosynthetic pathway. In some embodiments, cells of the disclosure are provided with heterologous nucleic acid molecules that encode one or more enzymes of a pathway for synthesizing LNnT, including a β-1,3- N-acetylglucosaminyltransferase (LgtA), a β-1,4-galactosyltransferase (LgtB), and a UDP-N- acetylglucosamine diphosphorylase. Exemplary LgtA and LgtB enzymes useful in conjunction with the compositions and methods of the disclosure are described in the sections that follow. In some embodiments, cells of the disclosure are provided with heterologous nucleic acid molecules that encode one or more enzymes of a pathway for synthesizing 2’-FL, including a lactose permease, a GDP-mannose 4,6-dehydratase, a GDP-L-fucose synthase, an α-1,2-fucosyltransferase, and a fucosidase. Exemplary enzymes useful in conjunction with the compositions and methods of the disclosure are described in the sections that follow. In some embodiments, cells of the disclosure are provided with heterologous nucleic acid molecules that encode one or more enzymes of a pathway for synthesizing 3-fucosyllactose, including a GDP-mannose 4,6-dehydratase, a GDP-L-fucose synthase, an α-1,3-fucosyltransferase, and a PATENT ATTORNEY DOCKET: 51494-028WO2 fucosidase. Exemplary enzymes useful in conjunction with the compositions and methods of the disclosure are described in the sections that follow. In some embodiments, cells of the disclosure are provided with heterologous nucleic acid molecules that encode one or more enzymes of a pathway for synthesizing lacto-N-tetraose, including a β-1,3-N-acetylglucosaminyltransferase, a β-1,3-galactosyltransferase, and a UDP-N- acetylglucosamine diphosphorylase. Exemplary enzymes useful in conjunction with the compositions and methods of the disclosure are described in the sections that follow. In some embodiments, cells of the disclosure are provided with heterologous nucleic acid molecules that encode one or more enzymes of a pathway for synthesizing 3’-sialyllactose, including a CMP-Neu5Ac synthetase, a sialic acid synthase, a UDP-N-acetylglucosamine 2-epimerase, a UDP- N-acetylglucosamine diphosphorylase, and a CMP-N-acetylneuraminate-β-galactosamide-α-2,3- sialyltransferase. Exemplary enzymes useful in conjunction with the compositions and methods of the disclosure are described in the sections that follow. In some embodiments, cells of the disclosure are provided with heterologous nucleic acid molecules that encode one or more enzymes of a pathway for synthesizing 6’-sialyllactose, including a CMP-Neu5Ac synthetase, a sialic acid synthase, a UDP-N-acetylglucosamine 2-epimerase, a UDP- N-acetylglucosamine diphosphorylase, and a β-galactoside-α-2,6-sialyltransferase. Exemplary enzymes useful in conjunction with the compositions and methods of the disclosure are described in the sections that follow. In some embodiments, cells of the disclosure are provided with heterologous nucleic acid molecules that encode one or more enzymes of a pathway for synthesizing difucosyllactose, including a GDP-mannose 4,6-dehydratase, a GDP-L-fucose synthase, an α-1,2-fucosyltransferase, and an α- 1,3-fucosyltransferase. Exemplary enzymes useful in conjunction with the compositions and methods of the disclosure are described in the sections that follow. In some embodiments, the cells of the disclosure express an LgtA polypeptide. The LgtA polypeptides of the disclosure can be used to produce one or more of a variety of HMOs, including, without limitation, LNnT, LNT, LNFP I, LNFP II, LNFP III, LNFP V, LNFP VI, LNDFH I, LNDFH II, LNH, LNnH, F-LNH I, F-LNH II, DFLNH I, DFLNH II, DFLNnH, DF-para-LNH, DF-para-LNnH, TF-LNH, LST a, LST b, LST c, DS-LNT, F-LST a, F-LST b, FS-LNH, FS-LNnH I, and FDS-LNH II. In some embodiments, the cells of the disclosure express a LgtB polypeptide. In some embodiments, the cells of the disclosure express a protein that transports lactose into the cell. In some embodiments, the cells of the disclosure express a GDP-mannose 4,6-dehydratase. In some embodiments, the cells of the disclosure express a GDP-L-fucose synthase. In some embodiments, the cells of the disclosure express an α-1,2-fucosyltransferase polypeptide. Steviol Glycoside Biosynthetic Pathway In some embodiments, the cells are capable of producing one or more steviol glycosides may encode on or more enzymes of the steviol glycoside biosynthesis pathway. In some embodiments, the steviol glycoside biosynthesis pathway is activated in the genetically modified cells by engineering PATENT ATTORNEY DOCKET: 51494-028WO2 the cells to express polynucleotides encoding enzymes capable of catalyzing the biosynthesis of steviol glycosides. In some embodiments, the genetically modified cells contain one or more heterologous polynucleotides encoding a geranylgeranyl diphosphate synthase (GGPPS), a copalyl diphosphate synthase (CDPS), a kaurene synthase (KS), a kaurene oxidase (KO), a kaurene acid hydroxylase (KAH), a cytochrome P450 reductase (CPR), and/or one or more additional UDP- glycosyltransferases, such as UGT74G1, UGT76G1, UGT85C2, UGT91D, EUGT11, and/or UGT40087. In some embodiments, the genetically modified cells contain one or more heterologous polynucleotides encoding a variant GGPPS, CDPS, KS, KO, KAH, CPR, UDP-glycosyltransferase, UGT74G1, UGT76G1, UGT85C2, UGT91D, EUGT11, and/or UGT40087. In certain embodiments, the variant enzyme may have from 1 up to 20 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 1313, 15, 16, 17, 18, 19, or 20) amino acid substitutions relative to a reference enzyme. In certain embodiments, the coding sequence of the polynucleotide is codon optimized for the particular cell. GGPPS (EC 2.5.1.29) catalyzes the conversion of farnesyl pyrophosphate into geranylgeranyl diphosphate. Examples of GGPPS include those of Stevia rebaudiana (accession no. ABD92926), Gibberella fujikuroi (accession no. CAA75568), Mus musculus (accession no. AAH69913), Thalassiosira pseudonana (accession no. XP_002288339), Streptomyces clavuligerus (accession no. ZP-05004570), Sulfulobus acidocaldarius (accession no. BAA43200), Synechococcus sp. (accession no. ABC98596), Arabidopsis thaliana (accession no. MP_195399), and Blakeslea trispora (accession no. AFC92798.1), and those described in U.S. Patent No.9,631,215. CDPS (EC 5.5.1.13) catalyzes the conversion of geranylgeranyl diphosphate into copalyl diphosphate. Examples of copalyl diphosphate synthases include those from Stevia rebaudiana (accession no. AAB87091), Streptomyces clavuligerus (accession no. EDY51667), Bradyrhizobioum japonicum (accession no. AAC28895.1), Zea mays (accession no. AY562490), Arabidopsis thaliana (accession no. NM_116512), and Oryza sativa (accession no. Q5MQ85.1), and those described in U.S. Patent No.9,631,215. In some embodiments, the cell includes a heterologous nucleic acid encoding a CDPS. KS (EC 4.2.3.19) catalyzes the conversion of copalyl diphosphate into kaurene and diphosphate. Examples of enzymes include those of Bradyrhizobium japonicum (accession no. AAC28895.1), Arabidopsis thaliana (accession no. Q9SAK2), and Picea glauca (accession no. ADB55711.1), and those described in U.S. Patent No.9,631,215. In some embodiments, the cell includes a heterologous nucleic acid encoding a KS. CDPS-KS bifunctional enzymes (EC 5.5.1.13 and EC 4.2.3.19) may also be used in the cells of the invention. Examples include those of Phomopsis amygdali (accession no. BAG30962), Phaeosphaeria sp. (accession no. O13284), Physcomitrella patens (accession no. BAF61135), and Gibberella fujikuroi (accession no. Q9UVY5.1), and those described in U.S. Patent Application Publication Nos.2014/032928 A1, 2014/0357588 A1, 2015/0159188, and WO 2016/038095. KO (EC 1.14.13.88) catalyzes the conversion of kaurene into kaurenoic acid. Illustrative examples of enzymes include those of Oryza sativa (accession no. Q5Z5R4), Gibberella fujikuroi (accession no. O94142), Arabidopsis thaliana (accession no. Q93ZB2), Stevia rebaudiana (accession PATENT ATTORNEY DOCKET: 51494-028WO2 no. AAQ63464.1), and Pisum sativum (Uniprot no. Q6XAF4), and those described in U.S. Patent Application Publication Nos.2014/0329281 A1, 2014/0357588 A1, 2015/0159188, and WO 2016/038095. In some embodiments, the cell includes a heterologous nucleic acid encoding a KO. KAH (EC 1.14.13) also referred to as steviol synthases catalyze the conversion of kaurenoic acid into steviol. Examples of enzymes include those of Stevia rebaudiana (accession no. ACD93722), Arabidopsis thaliana (accession no. NP_197872), Vitis vinifera (accession no. XP_002282091), and Medicago trunculata (accession no. ABC59076), and those described in U.S. Patent Application Publication Nos.2014/0329281, 2014/0357588, 2015/0159188, and WO 2016/038095. In some embodiments, the cell includes a heterologous nucleic acid encoding a KAH. A CPR (EC 1.6.2.4) is necessary for the activity of KO and/or KAH above. Examples of enzymes include those of Stevia rebaudiana (accession no. ABB88839), Arabidopsis thaliana (accession no. NP_194183), Gibberella fujikuroi (accession no. CAE09055), and Artemisia annua (accession no. ABC47946.1), and those described in U.S. Patent Application Publication Nos. 2014/0329281, 2014/0357588, 2015/0159188, and WO 2016/038095. In some embodiments, the cell includes a heterologous nucleic acid encoding a CPR. UGT74G1 is capable of functioning as a uridine 5’-diphospho glucosyl: steviol 19-COOH transferase and as a uridine 5’-diphospho glucosyl: steviol-13-O-glucoside 19-COOH transferase. Accordingly, UGT74G1 is capable of converting steviol to 19-glycoside; converting steviol to 19- glycoside, steviolmonoside to rubusoside; and steviolbioside to stevioside. UGT74G1 has been described in Richman et al., 2005, Plant J., vol.41, pp.56-67; U.S. Patent Application Publication No. 2014/0329281; WO 2016/038095; and accession no. AAR06920.1. In some embodiments, the cell includes a heterologous nucleic acid encoding a UGT74G1. UGT76G1 is capable of transferring a glucose moiety to the C-3’ position of an acceptor molecule a steviol glycoside (where glycoside = Glcb(1 ^2)Glc). This chemistry can occur at either the C-13-O-linked glucose of the acceptor molecule, or the C-19-O-linked glucose acceptor molecule. Accordingly, UGT76G1 is capable of functioning as a uridine 5’-diphospho glucosyltransferase to the: (1) C-3’ position of the 13-O-linked glucose on steviolbioside in a beta linkage forming RebB, (2) C-3’ position of the 19-O-linked glucose on stevioside in a beta linkage forming RebA, and (3) C-3’ position of the 19-O-linked glucose on RebD in a beta linkage forming RebM. UGT76G1 has been described in Richman et al., 2005, Plant J., vol.41, pp.56-67; US2014/0329281; WO2016/038095; and accession no. AAR06912.1. UGT85C2 is capable of functioning as a uridine 5’-diphospho glucosyl: steviol 13-OH transferase, and a uridine 5’-diphospho glucosyl: steviol-19-O-glucoside 13-OH transferase. UGT85C2 is capable of converting steviol to steviolmonoside and is also capable of converting 19- glycoside to rubusoside. Examples of UGT85C2 enzymes include those of Stevia rebaudiana: see e.g., Richman et al., (2005), Plant J., vol.41, pp.56-67; U.S. Patent Application Publication No. 2014/0329281; WO 2016/038095; and accession no. AAR06916.1. In some embodiments, the cell includes a heterologous nucleic acid encoding a UGT85C2. UGT40087 is capable of transferring a glucose moiety to the C-2’ position of the 19-O- glucose of RebA to produce RebD. UGT40087 is also capable of transferring a glucose moiety to the PATENT ATTORNEY DOCKET: 51494-028WO2 C-2’ position of the 19-O-glucose of stevioside to produce RebE. Examples of UGT40087 include those of accession no. XP_004982059.1 and WO 2018/031955. In some embodiments, the cell includes a heterologous nucleic acid encoding a UGT40087. Introduction of Heterologous Nucleic Acids into a Host Cell In some embodiments, a heterologous nucleic acid of the disclosure is introduced into a host cell (e.g., yeast cell) by way of a gap repair molecular biology technique. The host cell may be host cell capable of producing a fermentation product or a previously fermented cell. In these methods, if the host cell has non-homologous end joining (NHEJ) activity, as is the case for Kluyveromyces marxianus, then the NHEJ activity in the host cell can be first disrupted in any of a number of ways. Further details related to genetic modification of host cells (e.g., yeast cells) through gap repair can be found in U.S. Patent No.9,476,065, the disclosure of which is incorporated herein by reference in its entirety. In some embodiments, a heterologous nucleic acid of the disclosure is introduced into the host cell by way of one or more site-specific nucleases capable of causing breaks at designated regions within selected nucleic acid target sites. Examples of such nucleases include, but are not limited to, endonucleases, site-specific recombinases, transposases, topoisomerases, zinc finger nucleases, TAL-effector DNA binding domain-nuclease fusion proteins (TALENs), CRISPR/Cas- associated RNA-guided endonucleases, and meganucleases. Further details related to genetic modification of host cells through site specific nuclease activity can be found in U.S. Patent No. 9,476,065, the disclosure of which is incorporated herein by reference in its entirety. Nucleic Acid and Amino Acid Sequence Optimization Described herein are specific genes and proteins useful in the methods, compositions, and organisms of the disclosure; however, it will be recognized that absolute identity to such genes is not necessary. For example, changes in a particular gene or polynucleotide including a sequence encoding a polypeptide or enzyme can be performed and screened for activity. Typically, such changes include conservative mutations and silent mutations. Such modified or mutated polynucleotides and polypeptides can be screened for expression of a functional enzyme using methods known in the art. Due to the inherent degeneracy of the genetic code, other polynucleotides which encode substantially the same or functionally equivalent polypeptides can also be used to clone and express the polynucleotides encoding such enzymes. As will be understood by those of skill in the art, it can be advantageous to modify a coding sequence to enhance its expression in a particular host. The genetic code is redundant with 64 possible codons, but most organisms typically use a subset of these codons. The codons that are utilized most often in a species are called optimal codons, and those not utilized very often are classified as rare or low-usage codons. Codons can be substituted to reflect the preferred codon usage of the host, in a process sometimes called "codon optimization" or "controlling for species codon bias." PATENT ATTORNEY DOCKET: 51494-028WO2 Optimized coding sequences containing codons preferred by a particular prokaryotic or eukaryotic host (Murray et al., 1989, Nucl Acids Res.17: 477-508) can be prepared, for example, to increase the rate of translation or to produce recombinant RNA transcripts having desirable properties, such as a longer half-life, as compared with transcripts produced from a non-optimized sequence. Translation stop codons can also be modified to reflect host preference. For example, typical stop codons for S. cerevisiae and mammals are UAA and UGA, respectively. The typical stop codon for monocotyledonous plants is UGA, whereas insects and E. coli commonly use UAA as the stop codon (Dalphin et al., 1996, Nucl Acids Res.24: 216-8). Those of skill in the art will recognize that, due to the degenerate nature of the genetic code, a variety of DNA molecules differing in their nucleotide sequences can be used to encode a given heterologous polypeptide of the disclosure. A native DNA sequence encoding the biosynthetic enzymes described above is referenced herein merely to illustrate an embodiment of the disclosure, and the disclosure includes DNA molecules of any sequence that encode the amino acid sequences of the polypeptides and proteins of the enzymes utilized in the methods of the disclosure. In similar fashion, a polypeptide can typically tolerate one or more amino acid substitutions, deletions, and insertions in its amino acid sequence without loss or significant loss of a desired activity. The disclosure includes such polypeptides with different amino acid sequences than the specific proteins described herein so long as the modified or variant polypeptides have the enzymatic anabolic or catabolic activity of the reference polypeptide. Furthermore, the amino acid sequences encoded by the DNA sequences shown herein merely illustrate embodiments of the disclosure. When "homologous" is used in reference to proteins or peptides, it is recognized that residue positions that are not identical often differ by conservative amino acid substitutions. A "conservative amino acid substitution" is one in which an amino acid residue is substituted by another amino acid residue having a side chain (R group) with similar chemical properties, e.g., charge or hydrophobicity. In general, a conservative amino acid substitution will not substantially change the functional properties of a protein. In cases where two or more amino acid sequences differ from each other by conservative substitutions, the percent sequence identity or degree of homology may be adjusted upwards to correct for the conservative nature of the substitution. Means for making this adjustment are well known to those of skill in the art (See, e.g., Pearson W. R., 1994, Methods in Mol. Biol.25: 365-89). Furthermore, any of the genes encoding an enzyme described herein (or any of the regulatory elements that control or modulate expression thereof) can be optimized by genetic/protein engineering techniques, such as directed evolution or rational mutagenesis, which are known to those of ordinary skill in the art. Such action allows those of ordinary skill in the art to optimize the enzymes for expression and activity in yeast. In addition, genes encoding these enzymes can be identified from other fungal and bacterial species and can be expressed for the modulation of this pathway. A variety of organisms could serve as sources for these enzymes, including, but not limited to, Saccharomyces spp., including S. cerevisiae and S. uvarum, Kluyveromyces spp., including K. thermotolerans, K. lactis, and K. marxianus, Pichia spp., Hansenula spp., including H. polymorpha, Candida spp., Trichosporon spp., PATENT ATTORNEY DOCKET: 51494-028WO2 Yamadazyma spp., including Y. spp. stipitis, Torulaspora pretoriensis, Issatchenkia orientalis, Schizosaccharomyces spp., including S. pombe, Cryptococcus spp., Aspergillus spp., Neurospora spp., or Ustilago spp. Sources of genes from anaerobic fungi include, but are not limited to, Piromyces spp., Orpinomyces spp., or Neocallimastix spp. Sources of prokaryotic enzymes that are useful include, but are not limited to, Escherichia. coli, Zymomonas mobilis, Staphylococcus aureus, Bacillus spp., Clostridium spp., Corynebacterium spp., Pseudomonas spp., Lactococcus spp., Enterobacter spp., Salmonella spp., or X. dendrorhous. Techniques known to those skilled in the art may be suitable to identify additional homologous genes and homologous enzymes. Generally, analogous genes and/or analogous enzymes can be identified by functional analysis and will have functional similarities. Techniques known to those skilled in the art can be suitable to identify analogous genes and analogous enzymes. Techniques include, but are not limited to, cloning a gene by PCR using primers based on a published sequence of a gene/enzyme of interest, or by degenerate PCR using degenerate primers designed to amplify a conserved region among a gene of interest. Further, one skilled in the art can use techniques to identify homologous or analogous genes, proteins, or enzymes with functional homology or similarity. Techniques include examining a cell or cell culture for the catalytic activity of an enzyme through in vitro enzyme assays for said activity, e.g., as described herein or in Kiritani, K., Branched-Chain Amino Acids Methods Enzymology, 1970; then isolating the enzyme with said activity through purification; determining the protein sequence of the enzyme through techniques such as Edman degradation; design of PCR primers to the likely nucleic acid sequence; amplification of said DNA sequence through PCR; and cloning of said nucleic acid sequence. To identify homologous or similar genes and/or homologous or similar enzymes, suitable techniques also include comparison of data concerning a candidate gene or enzyme with databases such as BRENDA, KEGG, or MetaCYC. The candidate gene or enzyme can be identified within the above-mentioned databases in accordance with the teachings herein. Culture and Fermentation Methods Materials and methods for the maintenance and growth of microbial cultures are well known to those skilled in the art of microbiology or fermentation science (see, for example, Bailey et al., Biochemical Engineering Fundamentals, second edition, McGraw Hill, New York, 1986). Consideration must be given to appropriate culture medium, pH, temperature, and requirements for aerobic, microaerobic, or anaerobic conditions, depending on the specific requirements of the host cell, the fermentation, and the process. The methods of producing squalene provided herein may be performed in a suitable culture medium in a suitable container, including but not limited to a cell culture plate, a flask, or a fermentor. Further, the methods can be performed at any scale of fermentation known in the art to support industrial production of microbial products. Any suitable fermentor may be used including a stirred tank fermentor, an airlift fermentor, a bubble fermentor, or any combination thereof. In particular embodiments utilizing Saccharomyces cerevisiae as the host cell, strains can be grown in a fermentor as described in detail by Kosaric, et al, in Ullmann's Encyclopedia of Industrial Chemistry, Sixth Edition, Volume 12, pages 398-473, Wiley-VCH Verlag GmbH & Co. KDaA, Weinheim, Germany. PATENT ATTORNEY DOCKET: 51494-028WO2 In some embodiments, the culture medium is any culture medium in which a microorganism capable of producing a heterologous product can subsist, i.e., maintain growth and viability. In some embodiments, the culture medium is an aqueous medium comprising assimilable carbon, nitrogen and phosphate sources. Such a medium can also include appropriate salts, minerals, metals, and other nutrients. In some embodiments, the carbon source and each of the essential cell nutrients are added incrementally or continuously to the fermentation medium, and each required nutrient is maintained at essentially the minimum level needed for efficient assimilation by growing cells, for example, in accordance with a predetermined cell growth curve based on the metabolic or respiratory function of the cells which convert the carbon source to a biomass. Suitable conditions and suitable medium for culturing microorganisms are well known in the art. In some embodiments, the suitable medium is supplemented with one or more additional agents, such as, for example, an inducer (e.g., when one or more nucleotide sequences encoding a gene product are under the control of an inducible promoter), a repressor (e.g., when one or more nucleotide sequences encoding a gene product are under the control of a repressible promoter), or a selection agent (e.g., an antibiotic to select for microorganisms comprising the genetic modifications). Host Cell Strains Any suitable cell may be used in the practice of the present invention as the host cell or previously fermented cell. Illustrative examples of suitable cells include any archae, prokaryotic, or eukaryotic cell. Examples of an archae cell include but are not limited to those belonging to the genera: Aeropyrum, Archaeglobus, Halobacterium, Methanococcus, Methanobacterium, Pyrococcus, Sulfolobus, and Thermoplasma. Illustrative examples of archae strains include but are not limited to: Aeropyrum pernix, Archaeoglobus fulgidus, Methanococcus jannaschii, Methanobacterium thermoautotrophicum, Pyrococcus abyssi, Pyrococcus horikoshii, Thermoplasma acidophilum, Thermoplasma volcanium. Examples of a prokaryotic cell include, but are not limited to those belonging to the genera: Agrobacterium, Alicyclobacillus, Anabaena, Anacystis, Arthrobacter, Azobacter, Bacillus, Brevibacterium, Chromatium, Clostridium, Corynebacterium, Enterobacter, Erwinia, Escherichia, Lactobacillus, Lactococcus, Mesorhizobium, Methylobacterium, Microbacterium, Phormidium, Pseudomonas, Rhodobacter, Rhodopseudomonas, Rhodospirillum, Rhodococcus, Salmonella, Scenedesmun, Serratia, Shigella, Staphlococcus, Strepromyces, Synnecoccus, and Zymomonas. Illustrative examples of prokaryotic bacterial strains include but are not limited to: Bacillus subtilis, Bacillus amyloliquefacines, Brevibacterium ammoniagenes, Brevibacterium immariophilum, Clostridium beigerinckii, Enterobacter sakazakii, Escherichia coli, Lactococcus lactis, Mesorhizobium loti, Pseudomonas aeruginosa, Pseudomonas mevalonii, Pseudomonas pudica, Rhodobacter capsulatus, Rhodobacter sphaeroides, Rhodospirillum rubrum, Salmonella enterica, Salmonella typhi, Salmonella typhimurium, Shigella dysenteriae, Shigella flexneri, Shigella sonnei, Staphylococcus aureus, and the like. In general, if a bacterial host cell is used, a non-pathogenic strain is preferred. Illustrative examples of non-pathogenic strains include but are not limited to: Bacillus subtilis, Escherichia coli, Lactibacillus acidophilus, Lactobacillus helveticus, Pseudomonas aeruginosa, Pseudomonas PATENT ATTORNEY DOCKET: 51494-028WO2 mevalonii, Pseudomonas pudita, Rhodobacter sphaeroides, Rhodobacter capsulatus, Rhodospirillum rubrum, and the like. Examples of eukaryotic cells include but are not limited to fungal cells. Examples of fungal cell include but are not limited to those belonging to the genera: Aspergillus, Candida, Chrysosporium, Cryotococcus, Fusarium, Kluyveromyces, Neotyphodium, Neurospora, Penicillium, Pichia, Saccharomyces, Trichoderma and Xanthophyllomyces (formerly Phaffia). Illustrative examples of eukaryotic strains include but are not limited to: Aspergillus nidulans, Aspergillus niger, Aspergillus oryzae, Candida albicans, Chrysosporium lucknowense, Fusarium graminearum, Fusarium venenatum, Kluyveromyces lactis, Neurospora crassa, Pichia angusta, Pichia finlandica, Pichia kodamae, Pichia membranaefaciens, Pichia methanolica, Pichia opuntiae, Pichia pastoris, Pichia pijperi, Pichia quercuum, Pichia salictaria, Pichia thermotolerans, Pichia trehalophila, Pichia stipitis, Streptomyces ambofaciens, Streptomyces aureofaciens, Streptomyces aureus, Saccaromyces bayanus, Saccaromyces boulardi, Saccharomyces cerevisiae, Streptomyces fungicidicus, Streptomyces griseochromogenes, Streptomyces griseus, Streptomyces lividans, Streptomyces olivogriseus, Streptomyces rameus, Streptomyces tanashiensis, Streptomyces vinaceus, Trichoderma reesei and Xanthophyllomyces dendrorhous (formerly Phaffia rhodozyma). In some embodiments of the present disclosure, the host cell is a yeast cell. In some embodiments, the previously fermented cell is a yeast cell. Yeast cells useful in conjunction with the compositions and methods described herein include yeast that have been deposited with microorganism depositories (e.g. IFO, ATCC, etc.), such as those that belong to the genera Aciculoconidium, Ambrosiozyma, Arthroascus, Arxiozyma, Ashbya, Babjevia, Bensingtonia, Botryoascus, Botryozyma, Brettanomyces, Bullera, Bulleromyces, Candida, Citeromyces, Clavispora, Cryptococcus, Cystofilobasidium, Debaryomyces, Dekkara, Dipodascopsis, Dipodascus, Eeniella, Endomycopsella, Eremascus, Eremothecium, Erythrobasidium, Fellomyces, Filobasidium, Galactomyces, Geotrichum, Guilliermondella, Hanseniaspora, Hansenula, Hasegawaea, Holtermannia, Hormoascus, Hyphopichia, Issatchenkia, Kloeckera, Kloeckeraspora, Kluyveromyces, Kondoa, Kuraishia, Kurtzmanomyces, Leucosporidium, Lipomyces, Lodderomyces, Malassezia, Metschnikowia, Mrakia, Myxozyma, Nadsonia, Nakazawaea, Nematospora, Ogataea, Oosporidium, Pachysolen, Phachytichospora, Phaffia, Pichia, Rhodosporidium, Rhodotorula, Saccharomyces, Saccharomycodes, Saccharomycopsis, Saitoella, Sakaguchia, Saturnospora, Schizoblastosporion, chizosaccharomyces, Schwanniomyces, Sporidiobolus, Sporobolomyces, Sporopachydermia, Stephanoascus, Sterigmatomyces, Sterigmatosporidium, Symbiotaphrina, Sympodiomyces, Sympodiomycopsis, Torulaspora, Trichosporiella, Trichosporon, Trigonopsis, Tsuchiyaea, Udeniomyces, Waltomyces, Wickerhamia, Wickerhamiella, Williopsis, Yamadazyma, Yarrowia, Zygoascus, Zygosaccharomyces, Zygowilliopsis, and Zygozyma, among others. In some embodiments, the strain is Saccharomyces cerevisiae, Pichia pastoris, Schizosaccharomyces pombe, Dekkera bruxellensis, Kluyveromyces lactis (previously called Saccharomyces lactis), Kluveromyces marxianus, Arxula adeninivorans, or Hansenula polymorphs (now known as Pichia angusta). In some embodiments, the host microbe is a strain of the genus PATENT ATTORNEY DOCKET: 51494-028WO2 Candida, such as Candida lipolytica, Candida guilliermondii, Candida krusei, Candida pseudotropicalis, or Candida utilis. In a particular embodiment, the strain is Saccharomyces cerevisiae. In some embodiments, the host is a strain of Saccharomyces cerevisiae selected from the group consisting of Baker's yeast, CEN.PK, CEN.PK2, CBS 7959, CBS 7960, CBS 7961, CBS 7962, CBS 7963, CBS 7964, IZ-1904, TA, BG-1, CR-1, SA-1, M-26, Y-904, PE-2, PE-5, VR-1, BR-1, BR-2, ME-2, VR-2, MA-3, MA-4, CAT- 1, CB-1, NR-1, BT-1, and AL-1. In some embodiments, the strain of Saccharomyces cerevisiae is CEN.PK. In some embodiments, the yeast strain used is Y21900. In some embodiments, the yeast strain used is Y23508. In some embodiments, the strain is a microbe that is suitable for industrial fermentation. In particular embodiments, the microbe is conditioned to subsist under high solvent concentration, high temperature, expanded substrate utilization, nutrient limitation, osmotic stress due to sugar and salts, acidity, sulfite and bacterial contamination, or combinations thereof, which are recognized stress conditions of the industrial fermentation environment. Examples The following examples are put forth so as to provide those of ordinary skill in the art with a description of how the compositions and methods described herein may be used, made, and evaluated, and are intended to be purely exemplary of the invention and are not intended to limit the scope of what the inventors regard as their invention. Example 1. Methods of synthesizing a bio-based polymer from fermentation residue Several distinct methods were used to synthesize a polymer using the fermentation distillate residue (FDR) which resulted as the residual product after a fermentation composition which included host cells capable of producing β-farnesene had undergone distillation. These exemplary methods are described in further detail in the sections below. 1) Making rigid polyurethane foams from FDR Procedure Polyol synthesis was performed according to the method described elsewhere, by a simple two-step mechanism where the trans-ß-farnesene distillation residue (FDR) was used as the crude oil which was epoxidized with performic acid in situ. This reaction was followed by an oxirane ring opening with phosphoric acid. This technique has been used to insert hydroxyl groups in the structure exploring carbon-carbon double bonds and ester linkages present in natural oils. The reaction yield (%) was determined by Eq. (1). ^^^^ ^^^^ ^^^^ ^^^^ ^^^^ (%) = _{^^^^ ^^^^ ^^^^ ^^^^ ( ^^^^)} × 100 Eq. (1) PATENT ATTORNEY DOCKET: 51494-028WO2 Water-blown polyurethane foams preparation A formulation of water-blown polyurethane foam (Table 1) was developed. In the first stage all ingredients, with the exception of 4,4-MDI, were weighed into a beaker and melted in a hotplate while hand-mixed for 5–20 s. In the second stage, the pre- measured MDI was added, and the content was manually stirred for 8–20 s. The foam was left to cure and stabilize for 48 h, at room temperature. Table 1. Components of the polyurethane foam Sample Role Amount (%) FDR Polyol Monomer 17.7 Water Blowing agent 1.3 Glycerol Chain-extender 19.0 DBTDL Catalyst 0.8 PDMS Emulsifier 2.8 4,4’-MDI Monomer 58.5 2) Making flexible thermoset aliphatic FDR-based polyester Procedure FDR pretreatment (FDR _w ): Dewaxing or winterization, was a physical pretreatment used to remove waxes by crystallization in the industrial refining of vegetable oils. The residue, FDR, had a biphasic nature, therefore winterization was applied to purify and provide uniformization of the residue between different batches. The residue was thoroughly mixed with warm ethanol 96 %, ratio (ETOH:FDR = 4:1) for 30 min, followed by overnight decantation at 4.0 ± 2.0 °C in a refrigerator. The suspension was then centrifuged (5000 rpm, 15 min) and the ethanol was recovered to be recycled in a rotary evaporator. Polyol synthesis: The pretreatment was followed a typical two-step reaction of epoxidation (oxirane-ring formation) with in situ performic acid, followed by the ring-opening step with fatty acids found in castor oil. 1 ^st step Epoxidation (FDR epoxide) was performed with slight modifications, and optimized to this feedstock. FDRw (200 g), ethyl acetate (100 g), and formic acid (12 g) were weighed and placed on a heating/stirring plate with controlled temperature. After a few minutes of constant stirring, refrigerated hydrogen peroxide (320 g) was slowly poured to avoid exothermic foaming. The epoxidation took place at 85 °C, for 3 h with constant stirring, followed by decantation of the organic phase in a separatory funnel and a neutralization/washing operation with water and sodium bicarbonate solution (10 %). The epoxide was then dried overnight at 80 °C in a vacuum oven. PATENT ATTORNEY DOCKET: 51494-028WO2 2 ^nd step Ring-opening reaction (Polyol, -OH) following the epoxidation procedure, the FDR epoxide (300 g) was mixed with castor oil (100 g) in a tall beaker and the hydroxylation was carried out at 160 °C for 7 h under nitrogen purge. No further purification was necessary. The reaction yield (%) for polyol synthesis was determined by equation (2). _{^^^^ ^^^^ ^^^^ ^^^^ ^^^^ =} ^{^^^^ ^^^^ ^^^^ ^^^^ ^^^^ ^^^^ ^^^^ ( ^^^^)} × 100 (2) Polyester synthesis: The prepolymer was prepared using the eco-friendly solvent and catalyst-free melt-polycondensation method, under nitrogen purge, using the prepared polyol (-OH), azelaic acid (saturated diacid); citric acid (cross-linker), 1,4-butanediol and sorbitol (chain-extender/mechanical enhancer), where the reagents were in a ratio of polyol: azelaic acid: citric acid: butanediol: sorbitol was 6:4:3:1:1. All the reagents, except sorbitol, were melted at 160 °C for 1.5 h with constant stirring, after that period, the sorbitol was mixed, and the reaction was prolonged for 30 min. The polymer was quickly poured into a PTFE mold, and the cure was carried under a vacuum drying oven for 3 days at 140 °C. This resulted in an unsaturated aliphatic and linear polyester. Porous scaffold production (salt-leaching): – The flexible thermoset aliphatic FDR based polyester previously described could be used to produce scaffolds with biomedical application. These can be produced trough several methodologies such as salt leaching, electrospinning, etc. This application describes the salt leaching method which was performed by taking a known quantity of sieved sodium chloride crystals with particle size between 315 and 500 mm, mixing in the prepolymer right before casting. For 2D films, the content was poured into the square PTFE mold. To obtain 3D scaffolds, the content was poured into polypropylene tubes (10 mL) and quickly centrifuged at 10000 rpm. Both molds were placed in the drying oven under vacuum and cured at 140 °C for 3 days. After cooling to room temperature, the tubes were cut in slices of similar dimensions and cooled down in the refrigerator at 4 ± 2 °C to allow the polymer detachment. The retained salt porogens were then dissolved with warm deionized water. To control the leaching process, conductivity measurements were periodically made, until the registered value was like the solvent. 3) Synthesis of the rigid thermoset FDR-based non-isocyanate poly(ester-urethane) (NIPEU) Procedure FDR pretreatment (FDR _w ): The residue, FDR, had a biphasic nature, therefore winterization was applied to purify and provide some uniformization of the residue between different batches. The residue was thoroughly mixed with warm ethanol 96%, ratio (ETOH:FDR = 4:1) for 30 min., followed by overnight decantation at 4.0 ± 2.0 ºC in a refrigerator. The suspension was then centrifuged (5000 rpm, 15 min) and the ethanol was recovered to be recycled in a rotary evaporator. Polyol synthesis: The FDR product underwent a typical two-step reaction, an epoxidation (oxirane- ring formation) with in situ performic acid followed by a ring-opening step with glycerol. PATENT ATTORNEY DOCKET: 51494-028WO2 1 ^st step Epoxidation (FDR epoxide) was performed according to Uprety et al., 2017 with slight modifications, and optimized to the feedstock. FDR _w (200 g), ethyl acetate (100 g), and formic acid (12 g) were weighed and placed on a heating/stirring plate with controlled temperature. After a few minutes of constant stirring, refrigerated hydrogen peroxide (320 g) was slowly poured to avoid exothermic foaming. The epoxidation took place at 85ºC, for 3h with constant stirring, followed by decantation of the organic phase in a separatory funnel and a neutralization/washing operation with water and sodium bicarbonate solution (10%). The epoxide was then dried overnight at 80 °C in a vacuum oven. 2 ^nd step Ring-opening reaction (Polyol, -OH): the FDR epoxide (160 g) was then mixed with glycerol (40 g) and the reaction was carried out at 60 ºC for 6h in the presence of tetrafluorboric acid catalyst (0.05 %) with constant stirring. The content was then washed neutralized and washed with water and sodium bicarbonate solution (10%). After decantation in a separatory funnel any remaining solvent was removed on a rotary evaporator. Polyglycerol carbonate synthesis (PGC) Polyol (76.5 g), dimethyl carbonate (45 g) and sodium carbonate catalyst (0.05 %) were loaded in a 250 mL three-neck flask equipped with a condenser, a temperature sensor, and a mechanical stirring system. The mixture was refluxed at 75 ºC for 2 h. After cooling, the content was then quickly centrifuged, and the separated lighter organic phase (a cyclic carbonate) was reserved to the next step. PHU synthesis was performed as a ring-opening polymerization of the cyclic carbonate (PGC, 4 g) with the cycloaliphatic amine (isophorone diamine, 4g) in a closed vessel for 2 h at 50 ºC, with constant stirring. NIPEU synthesis was performed with a ratio of PHU: phthalic acid: citric acid: butanediol of 3:4.5:0.5:0.5. The esterification was then performed in a closed reactor with controlled heated stepwise until 160 ºC for 2 h with N2 purge. The mixture was then poured in a 5 cm Petri dish lined with baking sheet and cured at 120 ºC for 72 h. 4) Bio-based polyurethanes synthesis using microbial crude oil residue Procedure Synthesis of polyols: For the polyol synthesis a microbial oil residue resultant from the industrial β- farnesene production trough fermentation by a genetic modified Saccharomyces Cerevisiae. Epoxidation: Epoxidation of oils was carried out chemically as follows: 10 g of oil was weighed and transferred into a 250 mL Erlenmeyer flask. To this, 11 g of ethyl acetate was added followed by 0.9 g of formic acid, 11 ml of hydrogen peroxide was then added dropwise (to control reaction temperature) to this solution by using a burette. The solution mixture was then heated on a heating PATENT ATTORNEY DOCKET: 51494-028WO2 plate at 60 ºC for 6 h with constant stirring speed of 900 rpm. At the end of reaction time, the aqueous layer was removed, and oil layer was washed with distilled water in the ratio of 1:1. The residual solvents and water in the resulting oil layer was removed by drying at 100 ºC for about 3 h. Hydroxylation. Polyols were produced by taking 10 g of epoxidized oils and heating it on a hot plate until the temperature of the oils reached 85 ºC. To this warm solution, 1 g of phosphoric acid was added and was stirred at 300 rpm for 1 h. After that the solution was washed with 10% calcium carbonate (Na2CO3), followed by two washes with distilled water. During washes the polyols were recovered by centrifugation at 8000 rpm for 10 min. Those final washes were necessary to equilibrate the polyol pH because they presented previously a high acid value. Preparation of rigid polyurethane foams: The rigid polyurethane was prepared by mixing the polyols with other additives (i.e., catalysts, cocatalyst and surfactant) as described in Table 2. To produce polyurethanes, the formulated polyol was mixed with methylene diphenyl di-isocyanate (4,4’-MDI). All the ingredients except MDI were melt and weighed into a beaker and hand mixed for 5–20 s. The pre- measured MDI was then added into the beaker and stirred vigorously by hand mixing for 8–20 s and allowed to expand. The foams were cured for 48 days at room temperature before taking measurements. Table 2. Components of polymer film reaction Sample Role Amount (%) FDR Polyol Monomer 18 Glycerol Monomer 18 DBTDL Catalyst 2.72 PDMS Surfactant 0.68 4,4’-MDI Monomer 56.2 5) Fire-resistant bio-based polyurethane foams designed with two by-products derived from the sugarcane fermentation process Procedure Polymer synthesis: Pretreatment of the filler sugarcane bagasse ash (SCBA) was subjected to a thermochemical pretreatment to oxidize the organic matter present in the received samples. The ash was loaded in a porcelain crucible placed in a laboratory muffle and heated from room temperature to 600 °C at a rate of 10 °C min ^-1 , followed by a stage at 600 °C for 5 h. After cooling to room temperature, a few drops of hydrogen peroxide were thoroughly mixed, and the sample proceeded to another 600 °C cycle. The ash was used without further treatment in the polyurethane formulation at 4.5 % w/w. PATENT ATTORNEY DOCKET: 51494-028WO2 Polyol synthesis was performed by a simple two-step mechanism where the trans-ß-farnesene distillation residue (FDR) was used as the crude oil was epoxidized with performic acid formed in situ, followed by oxirane ring opening with phosphoric acid. The reaction yield (%) was determined by Eq. (3). ^ _{^^^ ^^^^ ^^^^ ^^^^ ^^^^} ⁽ _% ⁾ ₌ ^{^^^^ ^^^^ ^^^^ ^^^^ ^^^^ ^^^^ ^^^^ ( ^^^^)} × 100 Eq. (3) Water-blown polyurethane foams preparation – Two formulations (Table 3) were developed for both bio-based polyurethane foams with ash (PFA) and without ash (PF). In the first stage all ingredients, with exception of 4,4-MDI, were weighed into a beaker and melted in a hotplate while hand-mixed for 5–20 s. In the second stage, the pre-measured MDI was added, and the content was manually stirred for 8–20 s. The foam was left to cure and stabilize for 48 h, at room temperature. Table 3. Components of polymer film reaction Amount (%) Sample Role PF PAF FDR Polyol Monomer 17.7 18.1 Water Blowing agent 1.3 1.3 Glycerol Chain-extender 19.0 18.1 DBTDL Catalyst 0.8 0.7 PDMS Emulsifier 2.8 2.6 4,4’-MDI Monomer 58.5 55.8 SCBA Fire-retardant ˗ 4.5

PATENT ATTORNEY DOCKET: 51494-028WO2 5) Synthesis of thermoset elastomer from microbial oil Residue derived from fermentation of sugarcane Pre-treatment – The β-farnesene distillation residue (FDR) was submitted to a cold-ethanol winterization to remove wax-esters through a crystallization process and uniformize the feedstock. Briefly, the residue was mixed for 30 min with ethanol 96 % using a mass ratio EtOH: FDR = 4:1 wt., followed by overnight decantation at 4.0 ± 2.0 °C in a refrigerator. The suspension was then centrifuged and the ethanol was recovered at 50 °C and 175 mbar in a rotary evaporator. Epoxidation (Epoxide, EBT) – The reaction was carried out by the Prilezhaev method, where the winterized residue was epoxidized with performic acid formed in situ. Pretreated FDR (200 g), ethyl acetate (100 g), and formic acid (12 g) were weighed in a closed borosilicate vessel with a three-way lid and placed on a heating/stirring plate with temperature control. After a few minutes of constant stirring, refrigerated hydrogen peroxide (320 g) was slowly poured to avoid exothermic foaming, and the reaction temperature was taken to 85 °C for 3 h, under constant stirring. For the neutralization/purification procedure the contents were poured in a separatory funnel and the recovered organic phase was neutralized with sodium bicarbonate solution (10 %) and washed with plain water. The product was dried for 48 h at 80 °C in a vacuum oven. Ring-opening (Polyol, UPT) – The resulting epoxide (EBT) and phosphoric acid (ratio 7:1 wt.) were reacted at 85 ^o C for 1 h. After that, the organic phase was removed by decantation and the neutralization/purification operation was conducted as described above. Esterification (Polyester, PES) - The esterification took place by melt polycondensation in an open vessel. The polyol UPT (12 g) was mixed with phthalic acid (20 g), 1,4–butanediol (5 g), and citric acid (8 g) in a beaker and melted together for 1.0 h under N2 purge . After adding sorbitol (2.5 g), the reaction was prolonged for 30 min. The vessel content was quickly poured into a PTFE mold and placed in the oven at 150 °C for 48 h. Example 2. Characterization of polymer films The experiments conducted in this example characterize the materials produced in Example 1. The sections below describe these experiments in further detail. 1) Flexible thermoset aliphatic FDR-based polyester The biobased polyurethane foams synthesized as described above in Example 1, part 2 and summarized in FIG.7 were characterized according to the following methods: Stream Characterization PATENT ATTORNEY DOCKET: 51494-028WO2 After epoxidation, the unsaturation degree suffered about 76% of reduction. FDR pretreatment resulted in a great reduction in epoxide and polyol viscosity. Polyol M _w is high (above 2000 Da) and has a narrow molecular distribution. Polyester synthesis structural analysis FTIR: The epoxide, polyol found in the FDR distillate residue, and synthesized polyester were characterized using FTIR. The results showed that the increment of the band at 1734 cm ⁻¹ after esterification characteristic of C=O stretching and the arising of the band at 1171 cm ⁻¹ due to C-O stretching, which confirmed the signature bands for ester linkages, therefore the polyester synthesis (FIG.1). The hydroxyl (-OH) groups attached to the carbon backbone contribute to the hydrophilicity of the polymer.). For the elastomeric polyester, the ATR-FTIR profile of the feedstock FDR (FIG.16) revealed a prominent band centered around 3442 cm ^-1 , which was indicative of the presence of hydroxyl groups. Furthermore, distinct bands at 1647 and 1594 cm ^-1 were attributed to the -C=C- stretching vibrations, while the strong band at 1088 cm ^-1 indicated the -C-O-C stretching mode. Following hydroxylation, the polyol UPT exhibited a slight enhancement of the –OH stretching band at approximately 3442 cm- ¹ , providing further evidence of the increase in hydroxyl value from 63.5 to 82.3 mg KOH/g (FIG.19). These results indicated the successful incorporation of additional hydroxyl groups into the polyol structure. The additional band at 1774 cm ^-1 was specific of –C=O stretching vibrations. The UPT polyol exhibited a combination of a low hydroxyl value (82.3 mg KOH/g) and a high equivalent weight (E) of 681.7 g OH/eq.. The ATR-FTIR profile of the PES demonstrated the presence of characteristic bands commonly associated with aromatic polyesters. The sharp peaks around 1721 cm ^-1 and 1264 cm ^-1 were appointed to aromatic C=O and C-C-O stretches. The relatively stronger absorption bands around 1596 and 1580 cm ^-1 and the weaker absorption band around 1493 cm ^-1 were due to aromatic ring vibrations and C=C bending modes of unsaturated carbons, respectively. The intense peak at 1121 cm ^-1 was assigned to O-C-C stretch of aromatic esters and 1071 cm ^-1 of saturated ester -CO stretch. Polyester surface wettability: The sessile-dop method was the technique used to assess the contact angle meter and therefore the surface wettability of the polymer. Both water and squalane were tested as solvents at a temperature of 22 ^o C (FIG.2). The absorption and spreading were the key factors governing the overall mechanism of surface wetting although spreading provided the largest contribution for all biopolymers. This study showed that the polyester was hydrophilic, having an angle of less than 90 ^o and showed compatibility with squalane. Polyester in vitro degradation: In vitro degradation in physiological conditions was determined in accordance with ISO 175:2010, in a climatized chamber (Climacell Ecoline) under accelerated conditions i.e. with a temperature of 40.0±2.0 °C and relative humidity (RH) of 75±5%. Pre-weighed (m _i ) dried disks of very similar dimensions (10.7±0.01 mm and thickness of 1.18±0.02 mm) were individually placed in closed PATENT ATTORNEY DOCKET: 51494-028WO2 glass vessels containing 10 mL of PBS solution (pH of 7.4±0.1) and placed in the controlled environment chamber. Weekly, one of the vessels was retrieved and the disk was dried at 50 °C for 48 h. The sample final weight (m _f ) was registered, along with the pH of the remaining saline solution. The mass loss (%) related with sampling time, was determined using equation 6. ^^^^ ^^^^ ^^^^ ^^^^ ^^^^ ^^^^ ^^^^ ^^^^ (%) = ^{^^^^ ^^^^− ^^^^ ^^^^ ^^^^} × ^^^^ ^^^^ ^^^^ Eq. (6) a two-step mechanism of bulk erosion where about 87% of degradation occurs under 11 weeks under accelerated conditions ≅ 13 months in real time (FIG.3). Polyester safety assessment (In vitro cytotoxicity): In vitro cytotoxicity of the cured polyester was evaluated by indirect contact. The human keratinocyte cell line HaCaT (CLS) was kept in culture in DMEM media (Gibco) supplemented with 10 % FBS (Gibco) and 1 % antibiotic (Gibco) at 37 °C, with 5 % CO2 in a humidified atmosphere. To perform assays with cell lines, polymer discs were sterilized by immersion in ethanol for 1 h and briefly washed with sterile PBS prior to the experiment. Polymer discs were incubated with media in 24 well plates for 3 min and 24 h at 37 °C, with 5 % CO ₂ in a humidified atmosphere. Then, a previously seeded 96-well plate with HaCaT at 1x10 ⁴ cells/well was incubated with the conditioned media in quadruplicate. Wells with only conditioned media (without cells) were used to subtract a possible influence of the samples in the PrestoBlue fluorescence signal. Cells treated with 10% DMSO (dimethyl sulfoxide) were used as a negative control. After 24 h of exposure to the conditioned media, cytotoxicity was evaluated by the metabolic inhibition using a PrestoBlue assay (Thermo Fischer), according to the manufacturer’s instructions. PrestoBlue reagent was added to the media and incubated for 2 h at 37 °C, with 5 % CO ₂ in a humidified atmosphere. The fluorescence signal was read in a Synergy H1 microplate reader (BioTek). The results are expressed in percentage of cell viability as compared with a control (cells with plain media). At least two independent experiments were performed. The cytotoxicity results are presented in FIG.4. For incubation periods of 3 min and 24 h, the polymer did not affect the viability of the cells. The polymer was considered biocompatible with skin. Polyester thermal and mechanical performance: Thermal Performance: Thermal performance of the polyester film was assessed by differential scanning calorimetry (DSC) using a NETZSCH DSC 204 calorimeter and nitrogen as the purge gas (40 mL·min ⁻¹ ). Approximately 2 mg of each sample was placed in aluminum pans and the thermal properties were recorded between −70 and 300 °C at 10 °C ·min−1 to observe the melting temperature (T _m ), glass transition temperature (T _g ), and decomposition temperature. Glass transition temperature was measured on the second heating ramp to erase the thermal history of the polymer. Analyzing the polyester thermogram (FIG.5), the material showed glass transition temperature taken at midpoint of -49.8 °C and a melting temperature (Tm) of 169.6 °C, hence a semi-crystalline nature, and non-glassy behavior at room temperature. Additional thermal analysis of the polymer was performed to gain insight into the thermal properties, processing conditions, and potential applications of polyesters. The thermal transitions PATENT ATTORNEY DOCKET: 51494-028WO2 were, in a first approach, investigated using DSC (FIG.19). DSC of the elastomeric polymer was performed to find relevant thermal transitions in the polymer. Nitrogen was used as the purge gas at 50 mL/min. Approximately 8 mg of the sample was placed in an aluminium crucible and the thermal properties were recorded between − 30 and 200 °C at 10 °C/min. The curves were analysed on the second heating ramp, after a fast quenching to erase the thermal history of the polymer. Two different thermal program cycles were analyzed. The first program cycle (1P) included heating from 20 to 120 °C followed by cooling to -30 °C and isotherm of 10 min, and heating up to 200 °C. This program was carried out with a heating ramp of 10 °C/min. The second program cycle (2P) included heating from 20 to 120 °C with a heating ramp of 20 °C/min, fast quenching to -30 °C at 200 °C/min, isotherm of 10 min, and heating up to 200 °C with a heating ramp of 20 °C/min. This experiment showed the main thermal transitions of this polymer expected during heating, namely glass transition and melting point, were not found in the analysed range of temperatures via DSC. Due to the elastomeric behaviour of this polymer, the Tg was probably below -30°C, a fact that was further corroborated via dynamic mechanical analysis (DMA) (FIG.20) performed between - 100 and 100 °C to observe the presence of a relevant transition. DMA was performed on the elastomeric polyester by applying an oscillatory force or deformation to a material and monitoring the response. The tests were performed using a mechanical analyser (Triton Dynamic, New York, EU) with a temperature swept between -100 and 100 °C in tensile mode. The heating rate used was 1 °C/min, with the oscillating frequency of 1 Hz, and a strain amplitude of 0.02 mm according to the procedure of ASTM E1640. All the samples were measured with the dimensions of 20 × 4 × 1 mm and results are presented by the analysis of tan delta and modulus E’. FIG.20 presents the storage modulus (E’) and Tan delta curves indicated in blue and red, respectively. The curve showed a cyclic behavior in which the glassy structure was predominant at low temperatures where the polymer chains were restricted in their movement. As the temperature increased, the storage modulus decreased due to the imminence of the glass transition of the material, defined as the maximum point of the peak of the Tan delta curve, which was obtained at - 47.2 °C. In this region, the polymer chains acquired sufficient mobility to slide between each other due to their high energy level. Then, an inflection point was observed which pointed out the beginning of the elastic recovery of the material. In this transition region between -37.6 and -6.1 °C, the material presented a stiffening, which may indicate a recovery behavior associated with shape memory properties. Beyond -6.1 °C, the storage modulus curve showed the rubbery plateau up to 90 °C indicating a loss of mechanical properties and a lessening loss factor. It is worth noting that at room temperature, the storage modulus of the material was in accordance with that observed from the tensile test, with a value of 3.8 MPa. Finally, the Tan delta curve showed another peak of high energy dissipation at a temperature of 11.8 °C, which indicated the presence of the glass transition associated with the second relaxation stage of the material after the recovery of its shape. The glass transition observed after elastic recovery of the polymer, i.e., at temperatures circa 11.8 °C, was not detected by DSC analysis. Probably, a mechanical excitation of the material was necessary to allow energy storage and its subsequent relaxation, which would not be possible only with thermal stimulation via DSC, hence the DMA test was the appropriate technique to PATENT ATTORNEY DOCKET: 51494-028WO2 determine the behavior of this material and its intrinsic ability to recover its shape within the established temperature ranges. Mechanical Performance: The mechanical performance of the polyester was assessed using a Texture Analyser (model TA.XT plus C) with data acquisition and treatment software Express Connect. Several longitudinal strips with dimensions 100 × 10 × 2 mm were cut from the polyester mat and each one was attached to miniature tensile grips. The experiment was carried out at room temperature using a 30 Kg load cell with a strain rate of 2 mm.min ^-1 . Tensile strength, elastic modulus (Young’s modulus), and percent elongation were the determined properties. Mechanical analysis resulted in tensile strength of about 0.19 MPa, elongation values between 102% and 153.2%, and low Young’s elastic modulus between 1.9×10-3 and 2.2×10-3 MPa. These studies showed that the polymer was soft (low Young’s modulus) with relevant elasticity. Low Tg of the amorphous phase and high T _m of the crystalline phase showed elastomeric properties. Tensile, residual strain, and stress-relaxation tests were all performed in a universal testing machine shown in FIG.14. The tensile test was performed following the ASTM D638 guidelines. A set of 8 coupons was cut with a metal die, presenting a type IV geometry (FIG.15), and evaluated at 25 ± 2 °C and 50 ± 3 % of relative humidity with a testing speed of 20 mm/min and a preload of 0.001 N. A screening of residual strain (or creep test) was carried out to observe the percentage of the natural recovery of the polymer length after load removal. Several rectangular strips (40 x 5 x 0.65 mm) were subjected to 100 and 150 % of constant strain for 5-min and 20-min tests according to a factorial Design of Experiment to observe the residual strain after 1 min of load removal. The statistical analysis was developed using Minitab® for samples in duplicate with a central point, as shown in Table 4. Testing speed, load, and other parameters were developed in accordance with the tensile test. To analyse which of the factors of time and strain have a greater influence on the response an ANOVA was performed for a p-0.05 of significance. Table 4: Statistical analysis tested conditions 1 100 5 PATENT ATTORNEY DOCKET: 51494-028WO2 7 100 20 A stress-relaxation study was performed with three different samples cut from the same material following the parameters presented in Table 5. Table 5: Testing parameters in the stress-relaxation experiment. Parameters Value Testing speed (mm/min) 20 Preload (N) 0.001 Force (N) 0.6/0.9/1.2 Coupon width (mm) 5 Coupon thickness (mm) 0.65 Distance between grips (mm) 25 Overall coupon length (mm) 50 Time (min) 0/20 Among the 8 coupons tested, only 6 coupons presented the appropriate rupture in the middle zone, and when examining the related tensile stress-strain curves (FIG.6) it was revealed a predominant linear relationship between stress and strain in the elastic region, referred to the material's ability to return to its original shape after the applied stress is removed. The curves demonstrated no indications of plastic behavior immediately after the yield point, which, in this case, corresponded to the point of rupture at the maximum stress. In other words, the polyester exhibited a high degree of resilience, with minimal permanent deformation or plasticity typical of elastomeric materials. It was observed that the stress-strain rate increased for all samples after 50-60 % of the tensile strain. This rise was associated with the strain-hardening phenomena which indicated an alignment of the polymer chains related to strain-induced crystallization of the amorphous polymer. Polymers exhibiting stress-hardening behaviour were associated with better toughness properties due to the suppression of localized strains. The Young’s modulus (E max.), maximum tensile stress (σ max.) and elastic strain (ε max.) of this material are also displayed in Table 6. Table 6. PES tensile properties. σ max. (KPa) ε max. (%) E max. (MPa) 185.4 ± 510 ± 76 _13.0 ^{3.9 ± 1.3} PATENT ATTORNEY DOCKET: 51494-028WO2 As expected due to the relatively low cross-linking density , the material presented a high elastic strain of 185.4 %, low elasticity modulus (3.9 MPa), and very low tensile stress (510 kPa), a combination that inferred elastomeric “rubber-like” properties. To perform the residual strain experiment after 1 and 60 min of natural recovery, force-to- strain values were selected within safe limits to maintain the integrity of the polymer according to the tensile test. For this reason, a range between 100 and 150 % of the deformation was used (FIG.17). It was observed that after 20 min of testing there was no difference if the material was elongated at 100 or 150 % of strain. In both cases, the residual strain of samples was close to 2.2 % based on the initial dimension of samples. In contrast, at 5 min the residual strain was dependent on the strain level indicating that higher strain levels yield lower residual strains. The values indicated by the ANOVA test showed that, even though the time factor seemed to be more influential, both factors showed p-values greater than 0.05, which indicated no statistical significance in the response of residual strain after 1 min. Following the experiment, the length of the samples was also measured after 60 min of the load removal, resulting in a total length recovery at room temperature for all sample conditions. At this point, a stress relaxation test was developed to observe the free shape recovery of this polymer at room temperature. FIG.18 show the behaviour of the material which was subjected to the stress conditions presented in Table 5. It was evident from the figure, that an elastic recovery was achieved in all samples with values of 23, 25, and 23 % for 0.6, 0.9, and 1.2 N of peak forces, respectively. The minimal differences in the values may be attributed to microstructural defects in the sample affecting the stress relaxation. A variation was observed in the rate of relaxation, which indicated an abrupt and almost instantaneous change for the sample subjected to a minimal peak force, which exhibited a relaxation time during the first 2 min. The rapid decrease of force in the first period of relaxation was due to chemical degradation resulting in chain scission and breakage, whereas over prolonged periods it was due to physical factors like viscous flow and reversible relaxation. The rate of stress relaxation increased directly with increasing load. For values of 0.6 N, there was a rapid relaxation observed during the first minute of testing, meanwhile for higher load values, the stress-relaxation showed a stable behavior after 10 min. Scaffold morphology analysis: The resulting polyester films were analyzed with SEM technology at 25 ^o . For the 2D structure, the homogenous structure with well-formed pores (size ≅ 500 mm), which only presented on the scaffold’s bottom surface (FIG.8A). For the 3D structure, the pores were smaller and with an irregular distribution and were present on the scaffold’s inner core and in the annular region (FIG.8B). Scaffold Performance test for drug delivery: To determine the ability of the polyester films to act as a scaffold for drug delivery, in vitro dye release studies were performed with rhodamine B base (RBB) and curcumin (CRC) dyes. In vitro dye adsorption/release was monitored with a UV-Vis spectrophotometer (Shimadzu model UV-1900), using water-soluble dye (Rhodamine B base, RBB) on 3D scaffolds and PATENT ATTORNEY DOCKET: 51494-028WO2 hydrophobic curcumin (CRC) in 2D scaffolds, to study the behavior of previously prepared scaffolds disks. With that purpose, 100 mL of each dye were prepared dissolving a certain quantity of RBB in deionized water, and CRC in phosphate-buffered saline (PBS) ethanolic solution (EtOH 35 % v/v). Sets of pre-weighed and dried scaffold disks were immersed in 20 mL of dye solution at 20.0 mg /mL and 7.2 mg/mL for RBB and CRC, respectively, and the vessels were placed in an incubator shaker (Innova 40, series S) at 30 °C and 120 rpm for 7 h. After that period, the scaffolds were removed, the excess liquid absorbed with paper filter and the disks dried overnight at 50 °C. The 3D scaffolds (RBB dye) were then placed in 20 mL of aqueous solution and the 2D disks (CRC loaded) were immersed in 20 mL of the PBS ethanolic solution. The amount of dye released was quantified hourly until equilibria conditions were achieved or within an established period of 48 h. The concentration of the entrapped dyes was determined using standard calibration curves in the linear range at the wavelength of maximum absorbance, (RBB, 544 nm) and (CRC, 430 nm). The loading capacity (L.C.) was calculated from the following formula (7): ^^^^ ^{^^^^ ^^^^} W _di and W _df are the initial and final amount of dye in the contact solution (mg), and W _scf the scaffold initial weight, expressed in g. To evaluate the diffusional mechanism regarding the release kinetics of both dyes, the Korsmeyer-Peppas model was applied. The empirical equation (8) shown below allows the analysis of both Fickian and non-Fickian release of drug from swelling and non-swelling polymeric delivery systems. ^^^^ In this equation, M _t /M¥ is the fraction of dye delivered at time t, k is the transport constant (dimension of time ⁻¹ ), and n is the transport exponent (dimensionless). The release constant k provides mostly information on the drug formulation such as structural characteristics, whereas n is important since it is related to the release mechanism (i.e. Fickian diffusion or non-Fickian diffusion). When RBB dye was evaluated, the 3D scaffolds presented a loading capacity in 7 h, of 1.60 mg dye.g ^-1 , and 29.3 % of the dye was released within 48 h. Nevertheless, when the contact water was replaced, after 10 days the dye was still being released to the medium. When CRC dye was evaluated, the 2D disks loading capacity within 7 h was 0.64 mg dye.g ^-1 and in the same period of time about 50.4 % of the dye was released in the ethanolic contact solution. No further release occurred when replacing the contact solution, although the polymer still presented some coloration. PATENT ATTORNEY DOCKET: 51494-028WO2 After application of the Korsmeyer-Peppas model to the release data set, correlation coefficients (R ² ) were 0.987 (RBB) and 0.996 (CRC), respectively, indicating a good adjustment between the model and the experimental data. From the data fitting, the transport constant for CRC was k = 29.1 h ^-1 and the transport exponent n = 0.31 and for RBB, k = 11.9 h ^-1 and n = 0.24 (Table 7). Since n < 0.5, the diffusional model is a quasi-Fickian model, i.e. a non-swellable matrix-diffusion. Table 7. In vitro dye adsorption/release, sorption, and kinetic parameters. Scaffold Dye Type L.C. (mgdye g ^-1 ) Release (%) k (h ^-1 ) n 3 2 Our curcumin release data are consistent with those obtained using other polymers. For example, curcumin release from poly(lactic acid)/polycaprolactone electrospun fibers also followed a diffusion-controlled mechanism, with a good fitting to the Peppas- Korsmeyer model, and yielded a diffusion coefficient of n ≤ 0.5. (See, Sharma, D. and Satapathy, B.K., (2021) J. Mech. Behav. Biomed. Mater. p.120). Similarly, a poly(lactic acid)/polycaprolactone polyester (which had been developed for potential use in wound dressing, drug delivery, and regenerative systems) was evaluated with a complex of curcumin and β-cyclodextrin and demonstrated a release efficacy of 20 %. (See, Sharma, D. et al., (2022) Int. J. Biol. Macromol.,vol.216, pp.397–413). Additionally, chitosan/poly (lactic acid) nanofibers loaded with curcumin demonstrated wound healing properties and displayed a faster release of curcumin - reaching release saturation after 180 min. (See, Dhurai, B. et al., (2013) Front. Mater. Sci., vol.7, pp.350–361). Peppas- Korsmeyer modeling has been used widely to describe bioactive compound release from polymers, namely grape seed extract from nanofibrous membrane made with polylactic acid and polyethylene oxide (See, Li, B. and Yang, X. (2020) Mater. Sci. Eng., vol.109), and rutin release from cellulose acetate/poly(ethylene oxide) (See, El Fawal, G. et al. (2022) Int. J. Biol. Macromol.,vol.204, pp.555–564). The obtained 3D scaffold showed a higher loading capacity to entrap hydrophilic molecules, and lower release rate than the 2D structure for the lipophilic molecule. This demonstrates that this polymer could also be used to deliver drugs, with hydrophilic characteristics, into the skin as in the case of hyaluronic acid and ascorbic acid in PCL. The results of the kinetic study obtained permitted the conclusion that the fabricated polymer delivered the drug through diffusion as the dominant mechanism. Conclusions • Elastomeric properties (Relevant elasticity, low Young’s modulus, low Tg, and high Tm and degradation temperature). PATENT ATTORNEY DOCKET: 51494-028WO2 • Hydrophilic nature that explains in vitro swelling properties and bulk degradation in a relatively short period of time (about 12 months) – a high probability to be biodegradable under anaerobic conditions (landfill). • Good compatibility with squalane – active role in skin regeneration and carrier of healing molecules • Non-toxic to Human keratinocyte cells and the dye release showed a diffusion-controlled mechanism. • This polymer offers a sustainable and eco-friendly alternative for the potential use of controlled release of active principles for wound dressing applications. • A summary of each of the films generated is provided in FIG.9 as well as the intermediates generated in FIG.21. 2) Fire-resistant bio-based polyurethane foams designed with two by-products derived from the sugarcane fermentation process The biobased polyurethane foams synthesized as described above in Example 1, part 5 were characterized according to the following methods. Materials Characterization Sugarcane bagasse ash (SCBA): Quantification of minerals in SCBA was performed by Inductively Coupled Plasma – Atomic Emission Spectrometry (ICP-AES). Briefly, 250 mg of the oxidized ash was mixed in a Teflon vessel with 2 mL of HNO3 and 2 mL of HF and heated in a microwave system (Berghof, Eningen, Germany). The digestion procedure was conducted in four steps: 140 ˚C and 40 bar for 5 min; 160 ˚C and 40 bar for 10 min; 200 ˚C and 40 bar for 30 min; 100 ˚C and 20 bar for 5 min. After microwave digestion, the samples were cooled down to room temperature and diluted to a final volume of 50 mL. Microwave-digested samples were then analyzed through ICP-AES (PerkinElmer, Massachusetts, USA) and quantified through external standard calibration. All the analyses were performed in triplicate. Polyol: Acid number and hydroxyl (-OH) value, were determined by titrimetric analysis following (ASTM D 4662-08, 2011) and (ASTM D 1957-86, 2001), respectively. Viscosity was measured at 25.0 ± 0.1 ºC, following the standard (ASTM D 4678-15, 2015) using a rotational viscometer from Rheology Instruments, model Lamy B-One Plus. Molecular weight distribution of the FDR-based polyol was determined by high-performance liquid chromatography (HPLC). The chromatograms were acquired using an HPLC (model 1260 Infinity II, Agilent Technologies, Santa Clara, CA, USA) attached to an Evaporative Light Scattering Detector (ELSD, 1290 Infinity II, Agilent Technologies, Santa Clara, CA, USA) with evaporation temperature at 70 °C and nebulization at 65 °C, using nitrogen as nebulizing gas coupled to a TSK gel GMHxL column for insoluble polymers. The isocratic analysis was carried out with tetrahydrofuran as the mobile phase; flow rate of 0.6 mL min ^-1 ; sample concentrations of 20-25 mg mL ^-1 dissolved in THF and injection PATENT ATTORNEY DOCKET: 51494-028WO2 volumes of 20 μL. The molecular weight was estimated by calibration curve of polystyrene standards 400–303.000 Da (Agilent (Waldbronn, Germany). Polyol functionality (f) was calculated based on the average molecular weight (M _w ) and equivalent weight (E) based on the -OH value, defined by Eq. (4). ^^^^ = ^{^^^^ ^^^^} where ^^^^ = ^{1000 × 56.1} Ash content was determined by gravimetric analysis at 525 °C for 5 h following AOAC International Standard. Fourier Transform Infrared Spectroscopy (FTIR) was used to envision the chemical structure of all materials in the near-infrared range. Analyses were conducted in the absorbance range of 4000 to 500 cm-1, using a Perkin Elmer FT-IR spectrophotometer, fitted with a Pike Miracle ATR accessory containing Zn/Se crystal. Polyurethane foams: Apparent density was determined as the ratio of sample weight to its volume following (ASTM D1622/D1622M − 14, 2020). The results presented are the mean values calculated from six independent measurements. Compressive strength was determined, following the (ASTM D1621 -00, 2000) guidelines. The test samples were cut into squares with (3.0 (W) × 3.5 (L) × 2.5 (H)) cm ³ , and the experiment was carried out using a heavy-duty platform (HDP/90) with a 5 mm stainless steel cylindrical probe (P/0.5R) with a 30 kg load cell attached to a TA.XT 2i Texture Analyzer (Stable Micro Systems, Godalming, U.K.). The pre-test speed was set at 1 mm. s ^-1 , the test speed was 1.70 mm. s ^-1 , and the post-test speed was 10 mm. s ^-1 . Three measurements for each replica were performed at each experimental condition tested. The compressive strength was calculated as the value of the maximum force divided by the initial cross-sectional area of each sample when the maximum applied force occurred approximately at 13 % of deflection. Thermal properties were determined by differential scanning calorimetry (DSC) analyses were carried out using a NETZSCH DSC204 calorimeter. Nitrogen was used as the purge gas at 40 mL. min ⁻¹ . Approximately 2 mg of each sample was placed in aluminum pans and the thermal properties were recorded between −50 and 200 °C at 10 °C·min ⁻¹ to observe the glass transition temperature. The glass transition temperatures (Tg) were measured on the second heating ramp to erase the thermal history of the polymer. Morphology analysis was performed by Scanning Electron Microscopy (SEM) using a JSM- 5600LV (JEOL; Tokyo, Japan). Samples with 3 mm × 5 mm sliced with a scalpel from the center of the foam were placed directly on top of double-sided adhesive carbon tape (NEM tape, Nisshin, Japan), covering metallic stubs, and coated with gold/palladium using a sputter coater (Polaron, Bad Schwalbach Germany). All observations were performed using the secondary electron (SE) detector, with the SEM operated in high-vacuum, at an acceleration voltage of 15 kV and a spot size of 20. Flammability test of rigid polyurethane was performed following (ASTM D 3014-04, 2004). This test method measures the burning characteristics of cellular polymeric materials with a small standard PATENT ATTORNEY DOCKET: 51494-028WO2 test specimen of 50 (W) × 150 (L) × 15 (H) mm. The two commercial samples were used to compare performance: one conventional (Soudafoam 1K ^® ; SF) and another one with fire-resistant properties (Soudafoam FR 2K ^® ; SFRH). Results and Discussion Sugarcane bagasse ashes (SCBA): The mineral composition of the sugarcane bagasse ash used in this study is detailed in Table 5. As expected, silica was the major mineral component, reaching almost 60 wt.%. Although the composition was dependent on several factors such as region or local temperature range, sugarcane bagasse is described to have a silica composition ranging from 55 to 90 %, and some authors described sugarcane ash with a similar silica concentration. Iron oxide was the second most abundant element in sugarcane ash, similar concentrations of iron oxide in sugarcane bagasse, ranging from 14.95 to 29.18 wt.% have been described. Table 5. Sugarcane bagasse ash element composition. Element Concentration (g/100 g) SiO2 59.490 ± 3.05 Fe ₂ O ₃ 17.806 ± 0.02 K ₂ O 2.517 ± 0.01 CaO 2.204 ± 0.200 P2O5 1.285 ± 0.138 Al ₂ O ₃ 0.899 ± 0.07 MgO 0.869 ± 0.011 Na 0.188 ± 0.012 MnO2 0.091 ± 0.004 ZnO 0.023 ± 0.002 Polyol chemical and physical characterization: Polyol’s reactivity depends upon characteristic properties such as chemical structure, hydroxyl (-OH) value, and acid number and functionality. The characteristics of the FDR-based polyol are described in Table 6. The results showed a relatively low molecular weight (around 2711 Da), paired with a relatively high functionality (around 4), a low -OH value (82 mg KOH/ g polyol), and a high viscosity (13256 mPa.s) at 25 ºC. PATENT ATTORNEY DOCKET: 51494-028WO2 Table 6. Bio-based polyol characterization. Measured property Units FDR-based Polyol Acid value (mg KOH/g polyol) 3.3 ± 1.0 Hydroxyl (-OH) value (mg KOH/g polyol) 82.3 ± 0.9 Viscosity at 25 ºC (mPa.s) 13256 Molecular weight (Da) 2711.3 ± 10.0 Functionality (f) - 4.0 ± 0.1 Ash content (%) 0.31 ± 0.1 Yield (%) 80.3 ± 11.4 The formation of hydroxyl groups with the ability to form intramolecular H-bonding or the higher content of oligomers may contribute to the high viscosity observed on the polyol (Coman et al., 2021). The hydroxyl value obtained may be very variable when compared with other values reported for polyols synthesized from vegetable oils. Examples of that, are the canola and palm oils with higher - OH values of 266.86, 222.32 mg KOH/g of sample, respectively (Uprety et al., 2017), while others obtained from soybean, linseed, and palm oil, presented lower values around 90 and 78 mg KOH/g. The polyol functionality provided information about chemically active atoms or groups per molecule and high values of functionalities (3-5) produced rigid foams since they have greater chances of being incorporated into the network due to a great number of reactive sites. The use of natural oils to produce polyols was generally associated with some difficulties in the synthesis of polyurethane foam due to high viscosity, and low hydroxyl numbers which may affect foam properties like stability, low strength, and glass transition. However, the material has a versatile composition, is biodegradable, non-toxic, and environmentally friendly. Structural analysis (FTIR): Progression of the polyol and polyurethane synthesis was monitored by Fourier transform infrared spectroscopy (FTIR) (Figure 10a). The FDR lipidic content was characterized by the presence of a band at 1744 cm ⁻¹ assigned for C = O stretches of the ester functional groups from lipid triglycerides and fatty acids, CH2 bands of unsaturated fatty acids that were exhibited in the range 2868 to 2969 cm ^-1 . In the first reaction stage, the epoxide structure presented carbonyl –C=O stretching vibrations at 1729 cm ^-1 and the enhancement of the bands characteristic of epoxy groups/oxirane rings at 866 and 833 cm ^-1 , already present in the condensed residue. In the second stage, when the polyol was produced, those bands decreased in intensity and emerged the typical band of –OH stretching (Figure 10a) at about 3462 cm ^-1 . The presence of such bands confirmed the attachment of the hydroxyl group. FTIR spectroscopy was also used to monitor the polyurethane production. The developed bio- based formulations (PF and PAF in Table 7) allowed the synthesis of hard and rigid polyurethane (PUR) PATENT ATTORNEY DOCKET: 51494-028WO2 foams. In Figure 10b is made a comparative structural analysis together with the fossil-based benchmarks (SF and SFHR). Visually, it was observed a similar FTIR screening profile for all the foams despite their source, safeguarding the intensity of the bands. Looking specifically into PF and PFA results, it was found that the polyol related -OH stretching band at 3462 cm ^-1 disappears (Figure 10b) and new bands emerged following the reaction between - OH, -NCO (from 4,4- MDI) and additives. For instance, at 3309 cm ^-1 it was detected a band assigned to -NH stretching, as well C=O stretching (amide I) band at 1702 cm ⁻¹ , the amide II band at 1507–1540 cm ⁻¹ and the amide III band at 1210–1260 cm ⁻¹ . Bands characteristic of C–O stretching of the carbonate group emerged at 1210 and 1260 cm ^-1 along with 798 cm ^-1 characteristic out-of-plane bending of O– CO–O) and 1590 cm ^-1 (C–C stretching) of benzene ring. The three bands presented in the range 2969 and 2860 (asymmetric and symmetric C–H stretching) remain. This structural analysis corroborates the expected results according to previously published articles for this type of material. The polyurethane foam with bagasse ash (PAF) spectrum overlapped with the spectrum of polyurethane foam without ash (PF) (Figure 10b). Both formulations presented similar bands and intensities without additional bands that belong to other chemical species, suggesting that sugarcane bagasse ash was not chemically bound to the polymer and consequently not incorporated in the molecular structure. Similar results were reported for polyurethane made with fly ash, where only slight changes were observed in the composite foam spectrum with additional bands at about 680, 610, 595 and 460 cm ^-1 from the presence of aluminosilicate and silica. Foams density and mechanical compressive strength: Attending to the mechanical performance of both bio and fossil-based foams (Table 7), the former foams presented higher compressive strengths (PF, 22.0 kPa versus SF, 4.9 kPa) and (PAF, 21.0 kPa versus SFHR, 12.9 kPa). This is somehow expected since the bio-based foams also presented higher apparent densities (PF, 134.7 kg.m ^-3 versus SF 22.7 kg.m ^-3 ) and (PAF, 101.0 kg.m ^-3 versus SFHR, 29.6 kg.m ^-3 ). Table 7. Bio-based and commercial PUR foams, density, compressive and specific strength for all samples. Density Compressive Strength (at 13%) Specific strength Sample (kg.m ^-3 ) (kPa) (Pa⋅m³.kg ^-1 ) S ^{F 22.7 ± 4.3 4.9 ± 1} _215.9 S ^{FRH 29.6 ± 2.7 12.9 ± 3} _435.8 P ^{F 134.7 ± 3.6 22.0 ± 14} _163.3 P ^{AF 105.7 ± 10.1 21.0 ± 14} _198.7 PATENT ATTORNEY DOCKET: 51494-028WO2 The apparent density of polyurethane foams was one of the most important features in determining the mechanical properties of foams and as filler content increase, the density tend to decrease. The filler particles act as nucleation sites that promote an increase in the number of cells formed with increasing filler content. The addition of 4.5 % sugarcane bagasse ash was not enough to change the compressive strength (PF, 22.0 ± 14.0 versus PAF, 21.0 ± 14.0 kPa). It was been described previously that ash used as filler improved compressive strength by around 14 % when used 10 % wt. of fly ash , 20 % wt. waste ash. The specific compressive strength was determined as the compressive strength divided by foam density to normalize the mechanical properties. The bio-based foams presented specific strength values lower than the correlated fossil-based selected foams (PF, 163.3; SF, 215.9 Pa⋅m³.kg ^-1 ) and (PAF, 198.7; SF, 435.8 . A NCO/OH ratio increases the crosslinking and hard segment. Also, the fossil-based a lower density contributing to a higher specific compressive strength. Foams thermal behavior: Observing the comparative thermal profile obtained by DSC in Figure 11, both PF and PAF presented similar bands and intensities, suggesting that sugarcane bagasse ash was not incorporated in the polyurethane molecular structure. In Table 8 different thermal events were identified, namely glass transition temperature (T _g ) and melting point (T _m ), which was indicative of initial polymer degradation. The T _g values of 74.0 and 71.8 °C were found for both PF and PAF polyurethanes respectively, with a slight decrease associated with the incorporation of ash content. Commercial foams presented a T _g of 55.2 and 67.7 °C for SF and SFHR respectively, with a slight difference that may be associated with the fire resistance additives incorporated in the latter formulation. In addition, such difference may also be related to the type of petrochemical-based macrodiol used in the commercial brand synthesis. Table 8. Bio-based and commercial PUR foams, thermal (DSC) analysis. Sample T _g (ºC) T _m (ºC) SF 55.2 202.0 SFHR 67.7 212.0 PF 7–.0 215.0 - 238.0 PAF 7–.8 230.0 - 247.0 Melting points were observed as endothermic peaks in all samples above 200 °C indicating the beginning of the thermal degradation. As shown in the thermogram (Figure 11), broader melting bands were obtained for the commercial foams and presented starting points for SF and SFHR conditions at 202 and 212 °C, respectively. In contrast, the bio-based PUR resulted in narrow peaks that introduced began degrading at 215 and 230 °C for PA and PAF conditions respectively. Interestingly, the conditions PF and PAF presented overlapped melting intervals related to the bio-polyol backbone in both materials. PATENT ATTORNEY DOCKET: 51494-028WO2 For the PAF condition an endothermic peak was observed at a higher temperature (247 °C) which may be related to the presence of silica in the ash. Foams Morphology; A visual inspection of the bio-based foams (Figure 12) showed that the foam with ash (PAF) resulted in a darker foam with smaller inner cells and more homogenously distributed than the formulation (PF) without ash. Analyzing SEM images (Figures 13A-13D), the first visible feature is the smooth surface of cells observed in SFHR foams, and the wrinkled cells associated with plastic-like behavior in SF foams. These images contrast with the irregular structure presented by the bio-based PUR in both PF and PAF conditions, with the latter presenting apparent damage of cells likely due to sample brittleness that hindered sampling preparation. In the bio-based foams, several micro-lumps were observed on the cell’s surface possibly an indication of insufficient dispersion of all components during preparation. Additional to surface heterogeneity, PAF samples also presented micro-holes, in this case, due to the introduction of solid particles into the polyol premix that might significantly alter bubble nucleation conditions, which directly affects the size, shape, and number of pores, as well as pore wall thickness in the final materials. The finer cell structure, related to different nucleation points in the reaction media was observed for the bio-based foams and it was also responsible for the higher stiffness values obtained. A decrease in foam density after the incorporation of particles showed a strong relationship with the increase of nucleating points in the reaction media facilitating, among other things, the process of bubbles formation. The SEM imaging allowed a better understanding of the physical properties of the examined materials, revealing a correlation between lower density, lower compressive strength and increased friability of the fossil-based foams (SF and SFHR) was also related to their bigger porous structure when compared with bio-based foams (PF and PFA). Flammability test: Fire resistance of polymeric materials has received a lot of attention from scientific and industrial fields. To reduce combustibility and suppress toxic fumes or smoke production flame retardants have been used. They can be inorganic fillers, organic phosphorous compounds, nitrogen-based materials, and halogenated materials (Mngomezulu et al., 2014). In this manuscript the use of sugarcane ash was tested in combination with a bio-based polyol as a potential barrier to flame spread. To evaluate the composites' flammability and limit their use for thermal insulation a horizontal flame test was performed. The results from the flame retardant behavior of PUR’s are compiled in Table 9 and the specimens after the ignitability test under open flame are represented in Figure 14. Polyurethane foams produced with bio-based polyol pa resented higher burning length (132 mm) and burning time (252 s) than the polyurethane foams produced with ash (56 mm and 90 s), the remaining amount of sample after burning was about 57 and 87 %, respectively. The regular commercial foam, SF presented the higher burning length (140 mm) with the faster burning rate (9.4 cm.min ^-1 ), where the entire specimen has burned, remaining only 17 % of the weight. On the other side the SFHR foam did not burn after flame exposure for 60 s. PATENT ATTORNEY DOCKET: 51494-028WO2 Table 9. Results from horizontal flammability tests to the bio-based and commercial PUR foams. Time S ^FHR _{0.0 ± 0.0 31.7 ± 2.9 60.0 ± 0.05 90.74 ± 1.0 0.0 ± 0.0} PF 252.0 ± 51.0 132.0 ± 2.5 255.0 ± 116.7 57.4 ± 7.7 3.3 ± 3.8 PAF 90.3 ± 30.0 56.7 ± 20.8 116.7 ± 20.8 87.4 ± 9.5 3.8 ± 0.7 T extinguishment- time between application of burner flame and specimen flame extinguishment, s. Afterglow shall not be included in this time. PMR- percentual mass retained by the entire specimen. PMR=(S2/S1) × 100, where S2 is the mass of specimen after ignition (g) and S1 before ignition (g). It was shown that ash from wastes rich in Si and Ca elements which are assigned for SiO2 and CaCO ₃ , respectively, had a positive effect on flame retardancy of PU foams since silica (SiO ₂ ) was the predominant mineral in the added ash accounting for 59.5 % wt. (Table 5). With the addition of 4.5 % ash to the foam formulation, the total amount of SiO2 added was 2.7 % wt. The Fe2O3 was the second most abundant compound (17 % wt.) in the ash, and this was also tested for its flame-retardant potential in previous works. Hollow glass microspheres coated with Fe ₂ O ₃ enhanced the flame retardant and smoke suppression in thermoplastic polyurethane. Comparing both commercial and FDR-based foams, the difference in melting points suggests a superior thermal behavior of the latter indicating a visible impact of the ash in the thermal properties, thus meeting the fire protection standard according to UL 94HB, where the burning rate should be less than 7 mm min ^-1 for a specimen less than 3 mm thick and burning stops before 100 mm. Conclusions A bio-based polyurethane foam was produced through the valorization of two by-products derived from an industrial fermentation process, which includes a microbial crude oil after the distillation process, and the ash obtained after sugarcane bagasse burning for energy generation. The final polymer presented an absence of chemical interaction between ash filler and the polyurethane matrix; however, foam structure suggests that ash as a filler have a plasticizing effect increasing the polymer chain mobility, thus decreasing the glass transition temperature of the foam, delaying melting and consequently the temperature of degradation. This also correlates with the mechanical behavior suggesting a relation between high crosslinking densities and high compressive strength which implies higher glass and melting temperatures. The superior thermal behavior observed for bio-based polyurethane with sugarcane ash meets the fire protection standard according to UL 94HB. The presented results corroborate the idea that polyurethane foams derived from suitable and renewable waste by-products constitute a relevant sustainable green alternative to both edible and fossil-based sources, and that overall, sugarcane bagasse ash can be a suitable source of silica for PATENT ATTORNEY DOCKET: 51494-028WO2 the reinforcement of new sustainable composites replacing harmful chemicals that are used with the same purpose. Other Embodiments All publications, patents, and patent applications mentioned in this specification are incorporated herein by reference to the same extent as if each independent publication or patent application was specifically and individually indicated to be incorporated by reference. While the invention has been described in connection with specific embodiments thereof, it will be understood that it is capable of further modifications and this application is intended to cover any variations, uses, or adaptations of the invention following, in general, the principles of the invention and including such departures from the invention that come within known or customary practice within the art to which the invention pertains and may be applied to the essential features hereinbefore set forth, and follows in the scope of the claims. Other embodiments are within the claims.