Methods of texturizing mannan-based ingredients Introduction Current consumer trends show an increased demand for plant-based products. A potential answer to this trend is the development of plant-based analogue products that imitate, for example, meat and fish. The consumer expects these analogue products to be as close as possible in their textural, sensorial, and nutritional properties to the original animal-derived product. Many offerings on the market do not meet these expectations and so new processes need to be developed by the food industry. One promising process in the food industry is the use of the hydrocolloid (fibre) konjac glucomannan to texturize plant-based products. To achieve a good texturization of konjac glucomannan-containing food products, these hydrocolloids need to be structurally modified by a non-specific alkaline pre-treatment. After such an alkaline pre-treatment, chemicals must be either removed or neutralized. A main challenge is the functionalization of glucomannan in the presence of proteins using as an alkaline pre-treatment. Proteins can undergo unwanted site reactions at high pH values, which could impact, for example, sensorial, textural, and nutritional aspects. Summary of the invention The present invention relates to a method of producing a texturized plant-based product that comprises konjac glucomannan as a fibre source using enzymes, for example certain acetyl esterases with a high deacetylating activity towards konjac glucomannan. This allows the incorporation of protein into a food matrix. The objective is to develop a process to functionalize mannan, in particular konjac glucomannan from the tuberous roots of the konjac plant, to texturize plant-based products using acetyl esterases. The method of the invention is advantageous because it allows to (i) achieve a texturized plant-based product that comprises proteins, such as plant and animal-derived proteins, (ii) enable a texturization of a plant-based product in the presence of other ingredients, such as fibres (starch and non-starch fibres), and flavours, and (iii) minimize harsh process conditions, such as an alkaline treatment. The invention relates in general to a method of texturizing a mannan-based ingredient. The invention further relates to a method of texturizing a mannan-based ingredient, said method comprising, adding a carbohydrate esterase enzyme to a mannan-based ingredient, and forming a texturized mannan-based ingredient. The invention further relates to a method of texturizing a mannan-based ingredient, said method comprising hydrating a mannan-based ingredient; adding a carbohydrate esterase enzyme; incubating; heat treating; and cooling down to form a texturized mannan-based ingredient. The invention further relates to a method of texturizing a mannan-based ingredient, said method comprising hydrating a mannan-based ingredient; adding a carbohydrate esterase enzyme to form a mixture; incubating the mixture; heat treating the mixture to deactivate the enzyme; and cooling down the mixture to form a texturized mannan-based ingredient. The invention further relates to a method of texturizing a mannan-based ingredient, said method comprising a) hydrating a mannan-based ingredient; b) adding a carbohydrate esterase enzyme to form a mixture; c) incubating the mixture; d) heat treating the mixture to deactivate the enzyme; and e) cooling down the mixture to form a texturized mannan-based ingredient, wherein starch, fiber, and/or protein are added to the mixture before step d).. In some embodiments, the mannan-based ingredient is konjac glucomannan, or galacto glucomannan, preferably konjac glucomannan. In some embodiments, starch, fiber, and/or protein are added to the mixture, preferably after step a) and/or after step c), but before step d). In some embodiments, at least 1% (w/w) protein, preferably at least 2.5%(w/w) protein, is preferably added in step a). In some embodiments, the starch is pea starch and the fiber is pea fiber. In some embodiments, the protein is whey protein, soy protein, pea protein, or mung bean protein, preferably whey protein or soy protein. In some embodiments, the carbohydrate esterase is derived from Aspergillus species or Emericella species. In some embodiments, the carbohydrate esterase has an amino acid sequence which is at least 65% identical to the amino acid sequence of one or more of UniProt identifiers Q75P26, G3XVM1, Q5B037, A0A1L9X540, and A0A401L9L4. In some embodiments, the carbohydrate esterase has an amino acid sequence which is at least 70% identical to the amino acid sequence of one or more of UniProt identifiers Q75P26, G3XVM1, Q5B037, A0A1L9X540, and A0A401L9L4. In some embodiments, the carbohydrate esterase has an amino acid sequence which is at least 75% identical to the amino acid sequence of one or more of UniProt identifiers Q75P26, G3XVM1, Q5B037, A0A1L9X540, and A0A401L9L4. In some embodiments, the carbohydrate esterase has an amino acid sequence which is at least 80% identical to the amino acid sequence of one or more of UniProt identifiers Q75P26, G3XVM1, Q5B037, A0A1L9X540, and A0A401L9L4. In some embodiments, the amino acid sequence of the carbohydrate esterase is at least 90% identical to the amino acid sequence of UniProt identifiers Q75P26 and G3XVM1. In some embodiments, the texturized mannan wherein the mannan has a degree of deacetylation of at least 10%, preferably between 25 to 75%. In some embodiments, the mannan-based ingredient is incubated with between 0.01 to 3 %(w/w) enzyme, preferably between 0.1 to 1 % (w/w) enzyme. The invention further relates to a texturized mannan-based ingredient, preferably made by a method according to the invention, wherein the mannan has a degree of deacetylation of at least 10%, preferably between 25 to 75%. The invention further relates to a food product comprising the texturized mannan-based ingredient according to the invention. Preferably, the food product is a vegetarian or vegan food product. In some embodiments, the food product is a plant-based seafood product. The invention further relates to the use of a carbohydrate esterase with an amino acid sequence having at least 65% identity to the amino acid sequence of one or more of UniProt identifiers Q75P26, G3XVM1, Q5B037, A0A1L9X540, and A0A401L9L4, for texturization of a mannan-based ingredient. Detailed description of the embodiments Method of texturizing a mannan-based ingredient The invention relates to a method of texturizing a mannan-based ingredient. The mannan- based ingredient is preferably konjac glucomannan. The mannan-based ingredient is preferably hydrated in water and preferably then agitated. Agitation is preferably for at least 30 minutes. The hydration is typically performed at low temperature, for example at 8°C or less. Other ingredients are added, for example proteins, starch, and/or fibers and thoroughly mixed. The surprising benefits of adding these ingredients is shown, for example, in Examples 15 to 26 of the present application. The carbohydrate esterase, for example an acetyl esterase-containing enzyme preparation, is then added and incubated with the enzyme preparation. This incubation is long enough to ensure a sufficient functionalization of the mannan-based ingredient. The incubation is then stopped, and heat treated, for example at about 90 °C for about 50 minutes. The product is then cooled down, for example to room temperature. Alternatively, the mannan-based ingredient is functionalized during the incubation with the carbohydrate esterase, for example an acetyl esterase-containing enzyme preparation, before the addition of other ingredients, for example proteins, starch, and/or fibers. Mannan-based ingredient The mannan-based ingredient is konjac glucomannan, or galacto glucomannan, preferably konjac glucomannan. The mannan-based ingredient can be a powder. Where the mannan-based ingredient is konjac glucomannan, then up to 0.5 w/w (%) or less of the konjac glucomannan is hydrated. The mannan-based ingredient may have one or more of the following characteristics: the moisture content is between 1 to 15%; the glucomannan content is equal or greater than 25%, or between 60 to 100%; the pH is between pH 3.5 to 7.0; the ash content is up to 6%. The konjac glucomannan may be granulated. The granulated konjac glucomannan may have one or more of the following characteristics: the viscosity is equal or greater than 35,000 mPa s; the moisture content is equal or less than 8%; the glucomannan content is equal or greater than 95%; the pH is between pH 4.0 to 7.0; the ash content is up to 2%. The granulated konjac glucomannan may be powdered. The powdered granulated konjac glucomannan may have one or more of the following characteristics: the viscosity is about 22,600 mPa s; the moisture content is about 8.2%; the glucomannan content is about 74.2%; the pH is about 6.0; the ash content is about 1.67%. The mannan-based ingredient may be konjac flour. The konjac flour may have one or more of the following characteristics: the viscosity is about 16,600 mPa s; the moisture content is about 6.0%; the glucomannan content is between 70 to 75%, or about 72.5%; the pH is about 5.8; the ash content is about 3.67%. Carbohydrate esterase The carbohydrate esterase enzyme can be an acetal esterase. The acetyl esterase may have a sequence which is identical to a sequence of any acetyl esterase as described herein. The acetyl esterase may be, for example, UniProt identifiers Q75P26, Q5B037, G3XVM1, A0A401L9L4 or A0A1L9X540. Preferably, the acetyl esterase is selected from UniProt identifiers Q75P26, Q5B037, or G3XVM1. Preferably, the acetyl esterase is Q75P26. The acetyl esterase may be over 99%, or 98%, or 97%, or 96%, or 95%, or 94%, or 93%, or 92% or 91% or 90% identical to UniProt identifiers Q75P26, Q5B037, G3XVM1, A0A401L9L4 or A0A1L9X540. Alternatively, the acetyl esterase may be over 89%, or 88%, or 87%, or 86%, or 85%, or 84%, or 83%, or 82% or 81%, or 80%, or between 80% to 90%, or between 80% to 100% identical to UniProt identifiers Q75P26, Q5B037, G3XVM1, A0A401L9L4 or A0A1L9X540. Alternatively, the acetyl esterase may be over 79%, or 78%, or 77%, or 76%, or 75%, or 74%, or 73%, or 72% or 71%, or 70% or between 70% to 80%, or between 70% to 90%, or between 70% to 100% identical to UniProt identifiers Q75P26, Q5B037, G3XVM1, A0A401L9L4 or A0A1L9X540. Alternatively, the acetyl esterase may be over 69%, or 68%, or 67%, or 66%, or 65%, or 64%, or 63%, or 62% or 61%, or 60% or between 60% to 70%, or between 60% to 80%, or between 60% to 90%, or between 60% to 100% identical to UniProt identifiers Q75P26, Q5B037, G3XVM1, A0A401L9L4 or A0A1L9X540. The acetyl esterase may have an amino acid sequence identical to or substantially similar to an amino acid sequence shown in Example 27. The acetyl esterase may have an amino acid sequence identical to or substantially similar to an amino acid sequence shown in Example 28. The acetyl esterase may have an amino acid sequence identical to or substantially similar to an amino acid sequence shown in Example 29. The amino acid sequence identity may be determined using a CLUSTAL Omega multiple sequence alignment. The carbohydrate esterase may be expressed substantially as shown in Example 2. The carbohydrate esterase enzyme can be expressed in yeast, for example Pichia pastoris. The enzyme may have an EA value of between 350 to 3000 µkat/L. The enzyme may have a sequence and an EA value substantially as shown in table 1. Typically, starch, fiber, and/or protein are added to the mixture. These other ingredients are added preferably after step a) and/or after step c), but before step d) in the method of the invention. In some embodiments, whey protein is added, for example about 2.5 (w/w) % whey protein is added. In some embodiments, whey protein and/or soy protein are added, for example about 2.5 (w/w) % whey protein and/or about 0.2 (w/w)% soy protein is added. In some embodiments, pea starch and/or pea fiber is added, for example about 3 (w/w)% pea starch and/or 6 (w/w) % pea fiber is added. In some embodiments, whey protein, pea starch, and/or pea fiber is added, for example about 2.5 (w/w) % whey protein and/or about 3 (w/w)% pea starch and/or 6 (w/w) % pea fiber is added. In some embodiments, pea fiber, pea starch is added in combination with carbohydrate esterase CE8 enzyme corresponding to sequence CE8, or a functional derivative thereof, for example about 3 (w/w)% pea starch and/or 6 (w/w) % pea fiber is added in combination with enzyme CE8. In some embodiments, pea fiber, pea starch is added in combination with carbohydrate esterase CE10 enzyme corresponding to sequence CE8, or a functional derivative thereof, for example about 3 (w/w)% pea starch and/or 6 (w/w) % pea fiber is added in combination with enzyme CE10. The protein, starch and/or fibers can be added before incubation with enzyme. Alternatively, they can be added after incubation with enzyme. Where soy protein is added, preferably this is after incubation with enzyme. The mannan-based ingredient is preferably konjac glucomannan. As used herein, the term “about” is understood to refer to numbers in a range of numerals, for example the range of -30% to +30% of the referenced number, or -20% to +20% of the referenced number, or -10% to +10% of the referenced number, or -5% to +5% of the referenced number, or -1% to +1% of the referenced number. All numerical ranges herein should be understood to include all integers, whole or fractions, within the range. As used herein, the term "analogue" is considered to be an edible substitute of a substance in regard to one or more of its major characteristics. As used herein, the term “vegan” refers to an edible composition which is entirely devoid of animal products, or animal derived products, for example eggs, milk, honey, fish, and meat. As used herein, the term “vegetarian” relates to an edible composition which is entirely devoid of meat, poultry, game, fish, shellfish or by-products of animal slaughter. Those skilled in the art will understand that they can freely combine all features of the present invention disclosed herein. In particular, features described for the compositions of the present invention may be combined with the method or uses of the present invention and vice versa. Further, features described for different embodiments of the present invention may be combined. Where known equivalents exist to specific features, such equivalents are incorporated as if specifically referred to in this specification. Further advantages and features of the present invention are apparent from the figures and non-limiting examples. Examples Example 1: Method of making a texturized plant-based ingredient using Konjac Glucomannan (KGM) A procedure was developed for preparing the texturized plant-based ingredient of the invention. Firstly, KGM was added to water and then agitated to ensure sufficient hydration of the KGM for at least 30 min. The hydration was performed at low temperature (<8°C). Afterwards, other ingredients were added under agitation, such as proteins, starch, and fibers. After thorough mixing, the acetyl esterase-containing enzyme preparation was added under agitation. The whole mixture was incubated with the enzyme preparation to ensure a sufficient functionalization of the KGM (deacetylation). The incubation was then stopped, and the gelation induced via a heat-treatment at 90 °C for 50 min in a water bath. The product was cooled down to room temperature and the formed texturized product was analyzed via visual inspection and texture analysis using a Texture analyzer TA.HDplus from Stable MicroSystems, England. As an alternative, KGM was functionalized (deacetylated) during the incubation with the acetyl esterase-containing enzyme preparation before the addition of other ingredients, such as proteins, starch, and fibers. The latter were added after the incubation of KGM with the acetyl esterase-containing enzyme preparation. The gelation of the whole ingredient preparation was induced via the same heat-treatment (90 °C for 50 min). KGM preparations used: Example 2: Method for the expression of acetyl esterase-containing enzyme preparations From five genomes, five sequences (Q75P26, Q5B037, G3XVM1, A0A401L9L4 and A0A1L9X540) were selected. The sequences were expressed and produced in a P. pastoris strain (Table 1). The amino acid sequence identity of the five acetyl esterases was determined using a CLUSTAL Omega multiple sequence alignment (Table 2). The gene sequences encoding the different acetyltransferases were codon-optimized and ordered from Twist Bioscience. DNA fragments were cloned into pBSY21Z vector (Bisy, Graz, Austria) by Golden Gate cloning using SapI sites, transformed into chemically competent E. coli DH5a (NEB) by heat-shock and selected on low salt LB agar plates containing 25 µg ml ^-1 zeocin. Vectors were sequence-verified by Sanger sequencing at Genewiz Europe. Competent Pichia pastoris BSGBY10 (Bisy, Hofstaetten an der Raab, Austria) cells were prepared using the Pichia EasyComp™ Transformation Kit (Thermo Fisher).3 µg of the cloned vectors were linearized with SacI (Thermo Fisher) and transformed according to the manufacturer’s instructions. The entire reaction was plated on YPD (Yeast extract Peptone Dextrose) agar plates containing 100 µg*ml ^-1 zeocin. Plates were incubated for 3-5 days until colonies appeared. Seven individual colonies were picked for each transformed vector, transferred into 1 ml BMGY medium (Buffered Glycerol Complex Medium) in 24-well microtiter plates and incubated for 24 hours at 30°C and 200 rpm on an orbital shaker. For test expressions, the cells were diluted to an OD600 of 1 in BMMY medium (Buffered Methanol-Complex Medium) and the test fermentation was incubated for 72 hours at 30°C and 200 rpm with supplementation of 0.5 % methanol every 24 hours to maintain induction. After 72 hours, the cells were centrifuged at 3000 x g and the supernatant was analyzed by SDS-PAGE gel electrophoresis. The strongest expressing clone for each transformed vector was stored in 15 % glycerol (v/v) at -80°C for protein production. For protein production, a single Pichia pastoris colony was picked from an YPD-agar plate into a 50 ml BMGY pre-culture and incubated for 24 hours at 30°C and 200 rpm. The next day, cells were diluted to and OD ₆₀₀ of 1 in 400 ml BMMY medium. The protein production was conducted for 72 hours at 30°C and 150 rpm with supplementation of 0.5 % methanol every 24 hours to maintain induction. After 72 hours, the cells were centrifuged at 3000 x g, the supernatant further clarified by sterile filtration and concentrated to a final volume of 10 ml using Centricon Plus concentrators (Merck Millipore) (Table 1). The activity of the expressed acetyl esterases was determined using the chromogenic substrate 1-Napthyl-acetate. Therefore, 150 µl buffer (50 mM MES pH 6.7 + 0.005% Tween 20) was mixed with 30 µl Fast Blue (3.45 mM in H ₂ O _dd ) and 5 µl substrate (160 mM 1-Napthyl- acetate). After the chemicals were well mixed, 15 µl appropriately diluted acetyl esterase culture supernatant was added. The kinetic measurement was performed at 510 nm. The amino acid sequences and UNIProt ID of the expressed acetyl esterases are listed below (Table 1): Table 1: Identification and activity and protein content of the expressed carbohydrate Esterases (CE) 8 to 12. CE8 (Q75P26) MILLSYLLTYLLCALTCSARAIHNGRSLIPRAGSLEQVTDFGDNPSNVKMYIYVPTNLAS NPGIIVAIHYCTGTAQAYYQGSPYAQLAETHGFIVIYPESPYEGTCWDVSSQATLTHNGG GNSNSIANMVTWTTKQYNADSSKVFVTGTSSGAMMTNVMAATYPNLFAAGVAYAGVPAGC FLSTADQPDAWNSTCAQGQSITTPEHWASIAEAMYPDYSGSRPKMQIYHGNVDTTLYPQN YEETCKQWAGVFGYNYDAPESTESNTPEANWSRTTWGPNLQGILAGGVGHNIQIHGDEDM KWFGFTN CE9 (Q5B037) MVKLQYLLSILLYAYSCTALMLDRRDPTPGQLSQVTDFGDNPTNVGFYIYVPQNLASNPA IIVAIHYCTGTAQAYYSGTPYAQYAETYGFIVIYPESPYSGTCWDVSSQSTLTHNGGGNS NSIANMVDWTINQYNADASRVYVTGTSSGAMMTNVMAATYPNLFAAGIAYAGVPAGCFYS EANVEDQWNSTCAQGQSISTPEHWAQIAQAMYSGYEGSRPKMQIYHGSADATLYPQNYYE TCKQWAGVFGYNYDSPQEVQNDTPVAGWAKTIWGENLQGILADGVGHNIQIQGEEDLKWF GFTS CE10 (G3XVM1) MLSTHLLFLATTLLTSLFHPIAAHVAKRSGSLQQITDFGDNPTGVGMYIYVPNNLASNPG IVVAIHYCTGTGPGYYSNSPYATLSEQYGFIVIYPSSPYSGGCWDVSSQATLTHNGGGNS NSIANMVTWTISEYGADSKKVFVTGSSSGAMMTNVMAATYPELFAAGTVYSGVSAGCFYS DTNQVDGWNSTCAQGDVITTPEHWASIAEAMYPGYSGSRPKMQIYHGSVDTTLYPQNYYE TCKQWAGVFGYDYSAPESTEANTPQTNYETTIWGDNLQGIFATGVGHTVPIHGDKDMEWF GFA CE11 (A0A401L9L4) MLSTHLLFLATTLLTSLFHPIAAHVAKRSGSLQQITDFGDNPTGVGMYIYVPNNLATNPG IVVAIHYCTGTGPGYYSNSPYATLSEQYGFIVIYPSSPYSGGCWDVSSQATLTHNGGGNS NSIANMVTWTINEYGADSKKVYVTGSSSGAMMTNVMAATYPELFAAGTVYSGVSAGCFYS DTNQVDGWNSTCAQGDVITTPEHWASIAEAMYPGYSGSRPKMQIYHGSVDTTLYPQNYYE TCKQWAGVFGYDYSAPESTEANTPQTNYETTIWGDNLQGIFATGVGHTVPIHGDKDMEWF GFETLGDEVEKLEGMLLKEGVLPHLWQRVAGVLEGFVFDKYNMNPAVRDAFITTPAYPTS HLYPQHTLGIFKA CE12 (A0A1L9X540) MLCLSLLLTCVLCALSCRAGVLGNRDSVVYPRAGSLQQVTNFGSNPTNVGMYIYVPTNLA TKPGIIVAIHYCTGTASAYYSGSPYATLAEQYGFIVIYPQSPYSGTCWDVSSPATLTHNG GGNSNSIANMVIWTIAKYNADTSKVFVTGSSSGAMMTNVMAATYPNLFAAATVYSGVPAG CFYSATHQVDAWNSTCALGESITTPAHWASIAEAMDPGYAGARPRMQIYHGSVDTTLYPQ NYYETVKQWAGVWGYNYDAPQATEASVPEANYETTVWGPGLQGIFATGVGHTVPIHGERD MVWFGFA Table 2: Amino acid sequence identity of the five acetyl esterases based on a CLUSTAL Omega (1.2.4) multiple sequence alignment: Examples 3 - 7: Method to deacetylate and to determine the degree of deacetylation of KGM incubated with acetyl esterases The total amount of acetic acid liberated from KGM by saponification was measured (free acetic acid). These values were used as reference values (100%) for the determination of the degree of deacetylation (DD) when KGM was deacetylated by using acetyl esterases. The substrate (20 mg) was weighed into a HPLC vial.500 µL of pre-cooled 0.4 M NaOH pre- dissolved in an isopropanol - water mixture was added. During this procedure, samples were kept on ice to avoid the evaporation of acetic acid and the samples were vortexed immediately to avoid lump formation. An additional reference vial was prepared, which was not saponified (isopropanol solution only). The vial was mixed by vortexing. Samples were incubated at room temperature (RT) for 18h. Afterwards, vials were cooled down on ice and the solution was neutralized using approximately 500 µL of precooled 0.4 mM HCl. The pH was checked using pH paper and the amount of HCl was noted to calculate the dilution factor for the correct quantification.800 µL of the neutralized sample were transferred into a fresh 1.5 mL tube and centrifuged for 10 min at 20817 x g. The supernatant was analysed using the acetic acid kit from Megazyme (Wicklow, Irland). Alternatively, for HPLC analysis, the supernatant could be obtained by centrifugation of the samples at 14000 rpm for 20 min at 4 °C. If required, the supernatant was further purified by filtration using Vivaspin Amicon 3 K filters (Merck). Free acetic acid was measured using high performance liquid chromatography (HPLC) coupled to a refractive index (RI) detector. The HPLC was equipped with an Aminex HPX-87H ion exclusion column of 300 mm x 7.8 mm that was preceded by a guard column (125-0131) (Bio-Rad Laboratories, Hercules, CA, USA). The column temperature was set at 40 °C. The elution was performed at a flow rate of 0.6 ml/min using 0.05M H2SO4 as an eluent. The DA was calculated using acetic acid as a standard (0.1-10 mM). KGM was incubated with five acetyl esterase-containing enzyme preparations (See Example 3 -7). The enzyme preparations were dissolved in MiliQ water (20 % (w/v)).5 mg of KGM were weighed in a HPLC vial. The liquid enzyme preparations were diluted 1:2 and 1:4, respectively. 1 mL dilution was added into the HPLC vial. An enzyme reference for each enzyme preparation and a substrate reference (KGM in 50 mM sodium phosphate buffer, pH 5.0) was prepared. The pH was measured using pH paper and the lid of the vial was closed properly using parafilm. Samples were mixed using a vortexer and incubated for 4 h at 50 °C and 150 rpm in a heating oven. The pH was measured and 800 µL of the sample were transferred into a fresh 1.5 mL tube which was centrifuged at 20817 x g for 5-8 min. The acetic acid content in the supernatant was measured using either an acetic acid kit from Megazyme or using the HPLC, as described above. The highest deacetylation degree (DD) of 38.33 ± 2.34 % was reached for KGM incubated with the acetyl esterase-containing enzyme preparation CE8 for 24 h. The lowest DD% was measured for KGM incubated with the preparations CE11 and CE12. which led to an acetic acid release of about 15 % after 24 h. A complete overview of the released amount of acetic acid and the DD after the incubation of KGM with the five enzyme preparations is presented in Table 3. Table 3: Time-dependent activity of five acetyl esterase-containing enzyme preparations towards KGM ^a Degree of deacetylation (DD) – percentage of removed acetic acid moieties from KGM ^b Absolute release of acetic acid (mg) per g of KGM substrate Examples 8 - 14: Method of making a texturized KGM gel without protein addition The ability of five acetyl esterase-containing enzyme preparations (CE8- 12) to form gels after their addition to KGM was investigated. Granulated KGM (0.4 g) was hydrated in 19 mL of a 50 mM sodium phosphate buffer (pH 5.0). The mixture was mixed on a magnetic stirrer while the KGM was hydrated for 20 min. 1 mL of acetyl esterase-containing enzyme preparation solution was added and the mix was stirred with a spatula. The mixing was repeated every hour at RT for the first 3 h of incubation. After 24 h of incubation the gels were transferred into 50 mL falcon tubes and heated in a water bath at 90 °C for 50 min. The formed gels were cooled down to RT in a water bath before analysis using the texture analyser (Figure 1). Table 4: Composition and texture of texturized KGM gel using acetyl esterase-containing enzyme preparations n.d. – not determined, DD% degree of deacetylation ^a the estimated DD% was 25% percent, as CE8 and CE9 showed the same activity in initial trials (See Example 3 and 4) The DD (%) was not determined for Example 11 (CE9). Based on the results of the time conversion, the expected DD % of this sample was around 25 %, as DD% of KGM incubated with the enzyme preparation CE8 and CE9 was similar (Example 3 and 4). In general, the measured DD% of KGM incubated with the enzyme preparations was lower than expected. It is hypothesized that the higher viscosity of the prototype samples, as the KGM concentration was increased from 0.5 to 2.0 % (w/w)) and the thereby accompanied decrease in the mixing efficiency, lowered the enzyme-substrate interaction. The enzyme CE8 (8 and 16 mg per 20 mL gel; DD: 28.2 and 26.9 %, respectively) was the only enzyme leading to a clear texturization of the KGM gel compared to the reference gel. Even if the amount of enzyme was doubled from 8 to 16 mg per gel, the deacetylation degree was similar for both gels. Notably, the deacetylation degrees of the KGM incubated with CE10, 11 and 12 (CE10: 56.2 %; CE11: 40.8 %; CE12: 46.5 %) was higher than for KGM that was incubated with CE8. Figure 1 shows a process flow of enzymatically deacetylated KGM gels without protein addition. Example 15 - 20: Method of making a texturized KGM gel with protein addition The prototype production was also tested with addition of protein. Either 2.5 % (w/w) of whey protein or 0.2 % (w/w) of soy protein was added before or after the enzymatic incubation, respectively. The process flow chart is shown in Figure 2. Different prototype gels were prepared like described in the section of Example 15 – 20. The DD% of the prototypes was measured (Table 5). Table 5: Composition and texture of texturized KGM gel with protein addition using acetyl esterase-containing enzyme preparations n.d. – not determined, DD% degree of deacetylation The incorporation of protein into gel matrices is one advantage of using the enzymatic texturization compared to the chemical approach. Therefore, we investigated the ability of protein incorporation into KGM gels within the enzymatic process. The reference gel without protein showed a DD% of 26.9. The gel containing 2.5 % (w/v) whey protein showed the highest DD% of 67.5. Touching of the gel indicated that this was the gel with the highest firmness. It might be that the protein stabilized the enzymes during the enzymatic treatment, leading to higher DD% compared to the blank gel (KGM incubated with enzymes in the absence of protein). The DD% of the soy protein gel was 54.0. It must be mentioned, that for the soy gel the protein was added after the enzymatic treatment. Figure 2 shows a process flow (Example 3) of enzymatically deacetylated KGM gels with protein addition after enzyme incubation. Given concentrations are final concentrations in the gel. Figure 3 is an illustration of texturized KGM gels after the incubation with and without an acetyl esterase-containing enzyme preparation (CE8) in the presence of absence of proteins. Top left to right – Example 15, 16, 17 and 18; Bottom left to right – Example 19 and 20. Examples 21 - 26: Method of making a texturized KGM gel with protein, starch, and fibre addition The prototype production was also tested with addition of protein, pea fibre and pea starch to resemble a plant-based food product.2.5 % (w/w) of whey protein, 3 % (w/v) pea starch and 6 % (w/v) pea fibre were added to a KGM solution. Different prototype gels were prepared like described in the section of Example 21 – 26. The DD% of the prototypes was measured (Table 6). Table 6: Composition and texture of texturized KGM gel with protein addition using acetyl esterase-containing enzyme preparations n.d. – not determined, DD% degree of deacetylation Strong differences in the texturization between enzymatic and non-enzymatic treated samples were observed. The highest firmness of 4.3 N was reached for the KGM gel which contained 3 % (w/v) pea starch and 6 % (w/v) pea fiber and was incubated with enzyme preparation CE8. The addition of 2.5 % (w/v) whey isolate led to a softer gel (1.5 N), but a texturization was still achieved compared to the reference gels (no enzyme addition). Interestingly, enzyme preparation CE10 led to an improved firmness of the gel when present a matrix with pea starch, fiber and/ or protein, but KGM incubated with this enzyme was not texturized (Example 12). The DD% for the formed gels with only pea starch and pea fiber and in combination with the added protein are for enzyme CE854.9 and 63.8 % and for CE1057.7 and 59.7 %, respectively. It can be concluded that the DD% of the enzymatic treated gels with and without protein are similar comprising a DD% of approximately 60 %. In contrast to the pure KGM gels using CE10 (Example 12), in those prototypes the enzymes seem to lead to an improved texturization of the KGM gels. Figure 4 is an illustration of texturized KGM gels after the incubation with and without an acetyl esterase-containing enzyme preparation (CE8) in the presence and absence of pea fibre, pea starch and whey protein. Results of the texture analysis are presented in Table 6. Left to right – Examples 21, 22, 24 and 25. Figure 5 is an Illustration of texturized KGM gels after the incubation with and without an acetyl esterase-containing enzyme preparation (CE10) in the presence and absence of pea fibre, pea starch and whey protein. Results of the texture analysis are presented in Table 6. Left to right – Examples 21, 23, 24 and 26. Figure 6 shows a process flow (Example 3) of enzymatically deacetylated KGM gels with protein addition in the beginning, including other ingredients such as fibre and starch. Given concentrations are final concentrations in the gel. Examples 27 and 28: Listing of sequences comprising a high amino acid sequence identity with the one of CE8 and CE10. The amino acid sequences of CE8 and CE10 were used for a BLAST search. In total, 25 amino acid sequences were identified which encode proteins with a putative CE8 and CE10-like carbohydrate-esterases activity towards konjac glucomannan. Activities of the expressed enzymes towards KGM are presented in Example 30, Tables 7 – 9. Example 27: Amino acid sequence of CE8-like carbohydrate-esterases: XP_041150427 (99.3% amino acid sequence identity with the one of CE8), origin: Aspergillus flavus NRRL3357 or KAB8272531 from Aspergillus minisclerotigenes (same amino acid sequence) RAIHNGRSLI PRAGSLEQVT DFGDNPSNVK MYIYVPTNLA SNPGIIVAIH YCTGTAQAYY QGSPYAQLAE THGFIVIYPE SPYEGTCWDV SSQATLTHNG GGNSNSIANM VTWTTKQYNA DSSKVFVTGT SSGAMMTNVM AATYPDLFAA GIAYAGVPAG CFLSTADQPD AWNSTCAQGQ SITTPEHWAS IAEAMYPDYS GSRPKMQIYH GNVDTTLYPQ NYEETCKQWA GVFGYNYDAP ESTESNTPEA NWSRTTWGPN LQGILAGGVG HNIQIHGDED MKWFGFTN KOC14042 (99.0% amino acid sequence identity with the one of CE8), origin: Aspergillus flavus AF70 RAIHNGRSLI PRAGSLEQVT DFGDNPSNVK MYIYVPTNLA SNPGIIVAIH YCTGTAQAYY QGSPYAQLAE THGFIVIYPE SPYEGTCWDV SSQATLTHNG GGNSNSIANM VTWTTKQYNA DSSKVFVTGT SSGAMMTNVM AATYPDLFAA GIAYAGVPAG CFLSTADQPD AWNSTCAQGQ SITTPEHWAS IAEAMYPDYS GSRPKMQIYH GNVDTTLYPQ NYEETCKQWA GVFGYNYDAP ESTESNTPET NWSRTTWGPN LQGILAGGVG HNIQIHGDED MKWFGFTN KAE8337525 (97.9% amino acid sequence identity with the one of CE8), origin: Aspergillus arachidicola RAIHNGRSLI PRAGSLEQVT DFGDNPSNVK MYIYVPTNLA SNPGIIVAIH YCTGTAQAYY QGSPYAQLAE THGFIVIYPE SPYEGTCWDV SSQATLTHNG GGNSNSIANM VTWTTKQYNA DSSKVFVTGT SSGAMMTNVM AATYPNLFAA GIAYAGVPAG CFLSTADQPD AWNSTCAQGQ SITTPEHWAS VAEAMYPGYS GSRPKMQIYH GSVDTTLYPQ NYEETCKQWA GVFGYDYDAP KSTESNTPEA NWSRTTWGPN LQGILAGGVG HNIQIHGDED MKWFGFTN KAB8220000 (97.9% amino acid sequence identity with the one of CE8), origin: Aspergillus novoparasiticus RAIHNGRSLI PRAGSLEQVT DFGDNPSNVK MYIYVPTNLA SNPGIIVAIH YCTGTAQAYY QGSPYAQLAE THGFIVIYPE SPYEGTCWDV SSQATLTHNG GGNSNSIANM VTWTTKQYNA DSSKVFVTGT SSGAMMTNVM AATYPDLFAA GIAYAGVPAG CFLSTADQPD AWNSTCAQGQ SITTPEHWAS IAEAMYPGYS GSRPKMQIYH GSVDTTLYPQ NYEETCKQWA GVFGYDYDAP KSTESNTPEA NWSRTTWGPN LQGILAGGVG HNIQIHGDED MKWFGFTN KAE8316944 (96.5% amino acid sequence identity with the one of CE8), origin: Aspergillus transmontanensis RAIHNGRSLV PRAGSLEKVT DFGDNPSNVA MYIYVPTNLA SNPGIIVAIH YCTGTAQAYY QGSPYAQLAE THGFIVIYPE SPYEGTCWDV SSQATLTHNG GGNSNSIANM VTWTTKQYNA DSSKVFVTGT SSGAMMTNVM AATYPDLFAA GIAYAGVPAG CFLSTADQPD AWNSTCAQGQ SITTPEHWAS IAEAMYPGYT GDRPKMQIYH GDVDTTLYPQ NYEETCKQWA GVFGYDYDAP ESTESNTPEA NWSRTTWGPN LQGILAGGVG HNIQIHGDED MKWFGFTN KJK61460 (96.2% amino acid sequence identity with the one of CE8), origin: Aspergillus parasiticus SU-1 RAIHNGRSLV PRAGSLEKVT DFGDNPSNVA MYIYVPTNLA SNPGIIVAIH YCTGTAQAYY QGSPYAQLAE THGFIVIYPE SPYEGTCWDV SSQATLTHNG GGNSNSIANM VTWTTKQYNA DSSKVFVTGT SSGAMMTNVM AATYPDLFAA GIAYAGVPAG CFLSTADQPD AWNSTCAQGQ SITTPEHWAS VAEAMYPGYT GDRPKMQIYH GDVDTTLYPQ NYEETCKQWA GVFGYDYDAP ESTESNTPEA NWSRTTWGPN LQGILAGGVG HNIQIHGDED MKWFGFTN KAE8329211 (96.2% amino acid sequence identity with the one of CE8), origin: Aspergillus sergii RAIHNGRSLV PRAGSLEKVT DFGDNPSNVA MYIYVPTNLA SNPGIIVAIH YCTGTAQAYY QGSPYAQLAE THGFIVIYPE SPYEGTCWDV SSQATLTHNG GGNSNSIANM VTWTTKQYNA DSSKVFVTGT SSGAMMTNVM AATYPDLFAA GIAYAGVPAG CFLSTADQPD AWNSTCAQGQ SITTPEHWAS IAEAMDPGYT GDRPKMQIYH GDVDTTLYPQ NYEETCKQWA GVFGYDYDAP ESTESNTPEA NWSRTTWGPN LQGILAGGVG HNIQIHGDED MKWFGFTN KAE8158545 (94.4% amino acid sequence identity with the one of CE8), origin Aspergillus tamarii RAIHNGRSLV PRAGSLEKVT DFGDNPSNVG MYIYVPTNLA PNPAIIVAIH YCTGTAQAYY QGSPYAQQAE THGFIVIYPE SPYEGTCWDV SSQATLTHNG GGNSNSIANM VTWTTKQYNA DASKVFVTGT SSGAMMTNVM AATYPELFAA GIAYAGVPAG CFLSTADQPD AWNSTCAQGQ SITTPEHWAS IAEAMYPGYS GSRPKMQIYH GSVDATLNPQ NYEETCKQWA GVLGYNYDAP ESTEPNTPEA NWSRTTWGPN LQGILAGGVG HNIQIHGDED MKWFGFTS XP_031925812 (93.8% amino acid sequence identity with the one of CE8), origin Aspergillus caelatus RAIHNGRSLV PRAGSLEKVT DFGDNPSNVG MYIYVPTNLA PNPAIIVAIH YCTGTAQAYY QGSPYAQQAE THGFIVIYPE SPYEGTCWDV SSQATLTHNG GGNSNSIANM VTWTTKQYNA DASKVFVTGT SSGAMMTNVM AATYPELFAA GIAYAGVPAG CFLSTADQPD AWNSTCSQGQ SITTPEHWAS IAEAMYPGYS GSRPKMQIYH GSVDATLYPQ NYNETCKQWA GVFGYNFDAP ESTEPNTPEA NWSRTTWGPN VQGILAGGVG HNIQIHGDED MKWFGFTS XP_031914251 (93.8% amino acid sequence identity with the one of CE8), origin Aspergillus pseudotamarii RAIHNGRSLV PRAGSLEKVT DFGDNPSNVG MYIYVPTNLA PNPAIIVAIH YCTGTAQAYY QGSPYAQQAE THGFIVIYPE SPYEGTCWDV SSQATLTHNG GGNSNSIANM VTWTTKQYNA DASKVFVTGT SSGAMMTNVM AATYPELFAA GIAYAGVPAG CFLSTADQPD AWNSTCSQGQ SITTPEHWAS IAEAMYPGYS GSRPKMQIYH GSVDATLYPQ NYNETCKQWA GVFGYDYDAP ESTEPNTPEA NWSRTTWGPN VQGILAGGVG HNIQIHGDED MKWFGFTS amino acid sequence identity with the one of CE8), origin Aspergillus pseudocaelatus RAIHNGRSLV PRAGSLEKVN DFGDNPSNVG MYIYVPTNLA PNPAIIVAIH YCTGTAQAYY QGSPYAQQAE THGFIVIYPE SPYEGTCWDV SSQATLTHNG GGNSNSIANM VTWTTKQYNA DASKVFVTGT SSGAMMTNVM AATYPELFAA GIAYAGVPAG CFLSTADQPD AWNSTCSQGQ SITTPEHWAS IAEAMYPGYS GSRPKMQIYH GSVDATLYPQ NYNETCKQWA GVFGYNFDAP ESTEPNTPEA NWSRTTWGPN VQGILAGGVG HNIQIHGDED MKWFGFTS KAE8383458 (91.0% amino acid sequence identity with the one of CE8), origin Aspergillus bertholletiae RAIHNGRSLV PRAGSLEKVT NFGDNPTNVA MYIYVPNNLA SNPGIIVAIH YCTGTAQAYY QGSPYAQLAE KHGFIVIYPE SPYEGTCWDV SSQASLTHNG GGNSNSIANM VSWTTKQYNA DSSKVFVTGT SSGAMMTNVM AATYPELFAA GIAYAGVAAG CFLSTANQPD AWNSTCSQGQ SITTPEHWAS IAEAMYPGYS GSRPKMQIYH GSADATLYPQ NYYETCKQWA GVFGYNYDAP ESTQPNTPEA NWQTTTWGPN VQGILAGGVG HNIQIHGDAD MKWFGFTS Example 28: Amino acid sequence of CE10-like carbohydrate-esterases: Q96W96 (99.6% amino acid sequence identity with the one of CE10), origin Aspergillus ficuum HVAKRSGSLQ QITDFGDNPT GVGMYIYVPN NLASNPGIVV AIHYCTGTGP GYYSNSPYAT LSEQYGFIVI YPSSPYSGGC WDVSSQATLT HNGGGNSNSI ANMVTWTISE YGADSKKVYV TGSSSGAMMT NVMAATYPEL FAAGTVYSGV SAGCFYSDTN QVDGWNSTCA QGDVITTPEH WASIAEAMYP GYSGSRPKMQ IYHGSVDTTL YPQNYYETCK QWAGVFGYDY SAPESTEANT PQTNYETTIW GDNLQGIFAT GVGHTVPIHG DKDMEWFGFA XP_026628468 (99.3% amino acid sequence identity with the one of CE10), origin Aspergillus welwitschiae HVAKRSGSLQ QITDFGDNPT GVGMYIYVPN NLASNPGIVV AIHYCTGTGP GYYSNSPYAT LSEQYGFIVI YPSSPYSGGC WDVSSQATLT HNGGGNSNSI ANMVTWTISE YGANSKKVYV TGSSSGAMMT NVMAATYPEL FAAGTVYSGV SAGCFYSDTN QVDGWNSTCA QGDVITTPEH WASIAEAMYP GYSGSRPKMQ IYHGSVDTTL YPQNYYETCK QWAGVFGYDY SAPESTEANT PQTNYETTIW GDNLQGIFAT GVGHTVPIHG DKDMEWFGFA XP_025474521 (95.7% amino acid sequence identity with the one of CE10), origin Aspergillus neoniger CBS 115656 HAVKRSGSLQ QVTDFGDNPT NVGMYIYVPN NLASNPGIVV AIHYCTGTGP GYYSASPYAT LSEQYGFIVI YPSSPYSGGC WDVSSQATLT HNGGGNSNSI ANMVTWTISE YGADSSKVFV TGSSSGAMMT NVMAATYPEL FAAATVYSGV SAGCFYSNTN QVDGWNSTCA QGDVITTPEH WASIAEAMYS GYSGSRPKMQ IYHGSVDTTL YPQNYYETCK QWAGVFGYDY SAPEKTEANT PETNYETTIW GDSLQGIFAT GVGHTVPIHG DKDMEWFGFA XP_025389145 (95.4% amino acid sequence identity with the one of CE10), origin Aspergillus eucalypticola CBS 122712 HAVKRSGSLQ QVTDFGDNPT NVGMYIYVPN NLASNPGIVV AIHYCTGTGP GYYSASPYAT LSEQYGFIVI YPSSPYSGGC WDVSSQATLT HNGGGNSNSI ANMVTWTISE YGADSSKVFV TGSSSGAMMT NVMAATYPEL FAAGTVYSGV SAGCFYSNTN QVDGWNSTCA QGDVITTPEH WASIAEAMYS GYSGSRPRMQ IYHGSIDTTL YPQNYYETCK QWAGVFGYDY SAPEKTEANT PETNYETTIW GDSLQGIFAT GVGHTVPIHG DKDMEWFGFA OJI80539 (95.4% amino acid sequence identity with the one of CE10), origin Aspergillus tubingensis CBS 134.48 HAVKRSGSLQ QVTDFGDNPT NVGMYIYVPN NLASNPGIVV AIHYCTGTGP GYYSASPYAT LSEQYGFIVI YPSSPYSGGC WDVSSQATLT HNGGGNSNSI ANMVTWTISE YGADSSKVFV TGSSSGAMMT NVMAATYPEL FAAATVYSGV SAGCFYSNTN QVDGWNSTCA QGDVITTPEH WASIAEAMYS GYSGSRPRMQ IYHGSVDTTL YPQNYYETCK QWSGVFGYDY SAPEKTEANT PQTNYETTIW GDSLQGIFAT GVGHTVPIHG DKDMEWFGFA XP_025516937 (95.0% amino acid sequence identity with the one of CE10), origin Aspergillus piperis CBS 112811 HAVKRSGSLQ QVTDFGDNPT NVGMYIYVPN NLASNPGIVV AIHYCTGTGP GYYSDSPYAT LSEQYGFIVI YPSSPYSGGC WDVSSQATLT HNGGGNSNSI ANMVTWTISK YGADSSKVFV TGSSSGAMMT NVMAATYPEL FAAATVYSGV SAGCFYSNTN QVDGWNSTCA QGDVITTPEH WASIAEAMYS GYSGSRPRMQ IYHGSIDTTL YPQNYYETCK QWAGVFGYDY SAPEKTEANT PQTNYETTIW GDSLQGIFAT GVGHTVPIHG DKDMEWFGFA XP_041546395 (94.6% amino acid sequence identity with the one of CE10), origin Aspergillus luchuensis HAVKRSGSLQ QVTDFGDNPT NVGMYIYVPN NLASNPGIVV AIHYCTGTGP GYYGDSPYAT LSEQYGFIVI YPSSPYSGGC WDVSSQATLT HNGGGNSNSI ANMVTWTISK YGADSSKVFV TGSSSGAMMT NVMAATYPEL FAAATVYSGV SAGCFYSNTN QVDGWNSTCA QGDVITTPEH WASIAEAMYS GYSGSRPRMQ IYHGSIDTTL YPQNYYETCK QWAGVFGYDY SAPEKTEANT PQTNYETTIW GDSLQGIFAT GVGHTVPIHG DKDMEWFGFA XP_025535988 (94.6% amino acid sequence identity with the one of CE10), origin Aspergillus costaricaensis CBS 115574 HAVKRSGSLQ QVTDFGDNPT NVGMYIYVPN NLASNPGIVV AIHYCTGTGP GYYSASPYAT LSEQYGFIVI YPSSPYSGGC WDVSSQATLT HNGGGNSNSI ANMVTWTISE YGADSTKVFV TGSSSGAMMT NVMAATYPEL FAAATVYSGV SAGCFYSNTN QVDGWNSTCA QGDVITTPEH WASIAEAMYS GYSGSRPRMQ IYHGSIDTTL YPQNYYETCK QWSGVFGYDY SAPEKTEANT PETNYETTIW GDSLQGIFAT GVGHTVPIHG DKDMEWFGFA OJJ67302 (92.9% amino acid sequence identity with the one of CE10), origin Aspergillus brasiliensis CBS 101740 HVAKSSSSLQ QVTDFGDNPT NVGMYIYVPN NLASNPGIVV AIHYCTGSGP AYYSGSPYAT LSEQYGFIVI YPSSPYSGSC WDVSSQATLT HNGGGNSNSI ANMVTWTISK YGADSSKVFV TGSSSGAMMT NVMAATYPEL FAAATVYSGV SAGCFYSASN QVDAWNSTCA QGEVITTPEH WAQIAEAMDS GYSGSRPKMQ IYHGSVDTTL YPQNYYETCK QWAGVFGYDY SAPEKTEANT PQTNYETTIW GDSLQGIFAT GVGHTVPIHG DKDMEWFGFA Example 29: Amino acid sequences of CE10- and CD8-like carbohydrate-esterases with a lower amino acid sequence identity: GES663842, origin Aspergillus terreus LLPRAGSLEQVTDFGDNPTNVGMYIYVPNNLASSPGIVVAIHYCTGTAEAYYTGSPYAQL AEQYGFIVIYPQSPY EGTCWDVSSQATLTHNGGGNSNSIANMVTWTISKYNADSSKVFVTGSSSGAMMTNVMAAT YPELFAAATVYSGVP AGCFYSSSNQQDGWNSTCAQGQVITTPENWANVAKGMYPGYNGTRPKMQIYHGSVDTTLL PQNYYETCKQWAGVF GYNYDSPQQVQDNTPESNYATTTWGDDLQGIFATGVGHTVPIRGDDDMAWFGFA KAG2005192, origin Aspergillus fischeri VVKRVTSGSLQQVTNFGSNPSGTLMYIYVPKNLATKPGIVVAIHYCTGTAQAYYTGSPYA QLAEQYGFIVIYPQS PYSGTCWDVSSQSALTHNGGGDSNSIANMVTWTISQYNADTSKVFVTGSSSGAMMTNVMA ATYPELFAAATVYSG VSAGCFYSSSNQVDAWNSSCAQGNVISTPEVWGGIAKAMYPGYTGPRPRMQIYHGSTDTT LYPQNYYETCKQWAG VFGYNYNSPQSTQSNTPQANYQTTIWGPNLQGIFATGVGHTVPIHGEQDMEWFGFA KAH1272276, origin Aspergillus fumigatus VAKRVTSGSLQQVTNFGSNPSGTLMYIYVPNNLATKPGIVVAIHYCTGTAQAYYTGSPYA QLAEKYGFIVIYPQS PYSGTCWDVSSQSALTHNGGGDSNSIANMVTWTISQYNADTSKVFVTGSSSGAMMTNVMA ATYPELFAAATVYSG VPAGCFYSSSNQVNGWNSSCAQGNVISTPEVWGGIAKAMYPGYTGPRPRMQIYHGSVDTT LYPQNYYETCKQWAG VFGYNYNSPQSTQSNTPQANYQTTIWGPNLQGIFATGVGHTVPIHGEQDMEWFGF XP_001267861, origin Aspergillus clavatus NRRL 1 ALLPRAGSLQQVTNFGDNPTNVGMYIYVPNNLASNPGIIVAIHYCTGTAEAYYNGSPYAK LAEKHGFIVIYPESP YQGKCWDVSSRASLTHNGGGNSNSIANMVKWTIKKYKTNTSKVFVTGSSSGAMMTNVMAA TYPDMFAAGVVYSGV AAGCFMSNTNQQAAWNSTCAHGKSIATPEAWAHVAKAMYPGYDGPRPRMQIYHGSADTTL YPQNYQETCKEWAGV FGYDYNAPRSVENNKPQANYKTTTWGKELQGIYATGVGHTVPINGDRDMAWFGF XP_025429150, origin Aspergillus saccharolyticus JOP 1030-1 RALLVGSRDAVYPRAGSLQQVTNFGSNPTNVGMYIYVPTNLASKPGIIVAIHYCTGTASA YYSDSPYATLAEQYG FIVIYPQSPYSGTCWDVSSQATLTHNGGGNSNSIANMVTWTIAQYNADTSKVFVTGSSSG AMMTNVMAATYPALF NAATVYSGVPAGCFYSATNTPDAWNSTCAQGQSITTPAHWAAIAEAMDPGYRGARPRMQI YHGSVDTTLYPQNYY ETVKQWAGVWGYDYDAPQKTEASTPEANYVTTIWGKGLQGIYATGVGHTVPIHGEGDMEW FGF KAB8079110, origin Aspergillus leporis RAVGNVKSSLIPRAGSLEQITNFGSNPSNVAMYIYVPKNLASNPGIIVAIHYCTGTAQAY YNGSPYAQLAEKHGF IVIYPESPYSGKCWDVSSKATLTHNGGGNSNSIANMVTWTTSKYNANPNKVFVTGTSSGA MMTNVMAATYPNLFA AGIAYSGVPAGCFVSTANQAAAWNSTCAQGQSITTPEHWASIAKAMYPGYSGSRPKMQIY HGSTDSTLYPQNYQE TTKQWAGVFGYNYGSPQSKQGNTPEANYETTTWGEKLRGVYATGVGHSVPIHGDADMKWF GF Example 30: Activity of acetyl esterases comprising a high and lower amino acid sequence identity with the one of CE8 and CE10. Table 7: Time-dependent activity of CE8-like acetyl esterase-containing enzyme preparations towards KGM (See Example 27 for details about sequences) g/g] ^b 8,3 6,4 1,2 ,8 5,6 3,4 3,1 3,4 0,8 1,5 ,1 8,1 4,1 a Degree of deacetylation (DD) – percentage of removed acetic acid moieties from KGM b Absolute release of acetic acid (mg) per g of KGM substrate 5 Table 8: Time-dependent activity of CE10-like acetyl esterase-containing enzyme preparations towards KGM (See Example 28 for details about sequences) g] ^b C a e C 3 O O Q X 7 X 9 X 1 X _ , , , , , , , , , , , ,2 XP_026628468 14,5 6,3 16,4 7,0 16,0 6,9 15,4 6,6 16,4 7,0 34,2 13,4 X a Degree of deacetylation (DD) – percentage of removed acetic acid moieties from KGM b Absolute release of acetic acid (mg) per g of KGM substrate 5 Table 9: Time-dependent activity of acetyl esterase-containing enzyme preparations with a lower sequence identity with CE8 and CE10-like enzymes towards KGM (See Example 29 for details about sequences) I b i Ti ] ^b G K K K X X 10 a Degree of deacetylation (DD) – percentage of removed acetic acid moieties from KGM b Absolute release of acetic acid (mg) per g of KGM substrate 15