Description of Related Art In printing of textiles it is common to use print paste containing a dye and/or a pigment and a thickener. The function of the thickener is to help localize the dye and/or pigment to the specific area being printed. With most printing methods, the thickener (a polymer) and excess dye or pigment must be removed by treatment with water after the fixation of the print.

Generally, a large amount of water is required for complete removal due to the high viscosity and low water solubility of the thickener. Insufficient removal leads to unsatisfactory quality of the finished (printed) textile for the following reasons: 1) dye and/or pigment may be transferred to other parts of the printed textile or to other garments during subsequent processing steps or laundering by the consumer. 2) Residual thickener will make printed areas stiff. It is the object of this invention to decrease process time as well as the amount of energy and water needed to achieve a satisfactory quality of the textile and to increase the quality which can be obtained regarding color fastness and"hand".

SUMMARY OF THE INVENTION The present invention relates to a method for removing the thickener component in print paste used on printed textile, said print paste comprising a dye and/or a pigment and a xyloglucan-containing thickener.

The invention provides a method for removing print paste thickener from printed textile, wherein the print paste comprises a dye and/or a pigment and a xyloglucan-containing thickener, comprising the steps of (a) treating the printed textile in an aqueous solution containing a xyloglucan- degrading enzyme, and (b) optionally rinsing the treated printed textile.

BRIEF DESCRIPTION OF THE DRAWING Fig. 1 shows the standard curve of tamarind kernel powder (TKP), pH 6.5 and 45°C.

Fig. 2 shows xyloglucanase degradation of tamarind kernel powder-Initial measurement. Initial measurement = add enzyme, vortex sample and measure viscosity.

Fig. 3 shows xyloglucanase degradation of tamarind kernel powder-30 minutes incubation.

Fig. 4 shows xyloglucanase degradation of tamarind kernel powder-60 minutes incubation.

Fig. 5 shows xyloglucanase degradation of tamarind kernel powder-120 minutes incubation.

DETAILED DESCRIPTION OF THE INVENTION The present invention relates to a method for removing print paste thickener from printed textile, comprising a dye and/or a pigment and a xyloglucan-containing thickener.

The present inventors have found that the removal of print paste thickener from printed textile comprising a dye and/or a pigment and a xyloglucan-containing thickener can be made efficient by treating the printed textile with a xyloglucan-degrading enzyme. The enzymatic breakdown of the thickener will decrease process time as well as the amount of energy and water needed to achieve a satisfactory quality of the textile.

Accordingly, the invention provides a method for removing print paste thickener from printed textile, wherein the print paste comprises a dye and/or a pigment and a xyloglucan- containing thickener, comprising the steps of: (a) treating the printed textile in an aqueous solution containing a xyloglucan- degrading enzyme, and (b) optionally rinsing the treated printed textile.

The term"thickener"means an agent that increases the viscosity of print paste.

The term"xyloglucan-containing"thickener means a thickener comprising a significant amount of xyloglucan ingredient (s). It is to be understood that the thickener may contain other thickening ingredients besides xyloglucan.

Thickener The thickener may in one embodiment of the invention comprise from 0.005 to 50% (w/w) xyloglucan, preferably 0.01 to 10% (w/w) xyloglucan, more preferably 0.05 to 5% (w/w) xyloglucan, especially 0.1-3% (w/w) of the print paste.

In another embodiment the xyloglucan-containing thickener comprises a combination of thickening ingredients, i. e. , besides xyloglucan. The xylolglucan ingredient may in one preferred embodiment of the invention be tamarind kernel powder or the like or may alternatively be prepared from tamarind kernels. Examples of further thickening ingredients according to the invention are alginate, a modified alginate, starch, a modified starch, a modified cellulose, carrageenan, laminarin (1, 3-beta-D-glucan), a galactomannan, a modified galactomannan, guar gum or locust bean gum, particularly triethanolalginate, etherified starch, esterified starch, ethoxylated starch, carboxymethyl starch, oxidized starch, cross-linked starch, ethoxylated galactomannan, carboxymethyl galactomannan, carboxyethyl galactomannan, carboxymethyl cellulose or carboxyethyl cellulose, xanthan gum, arabic gum, tragacath gum, and synthetic thickeners, including polyacrylic acid and modified polyacrylic acid.

Xvloalucan Xyloglucans occur widely in the primary walls of higher plant cells, where they are bound in close association with cellulose microfibrils. Xyloglucans are linear chains of (14) beta-D-glucan, but, unlike cellulose, they possess numerous xylosyl chain units added at regular sites of the 0-6 position of the glucosyl units of the chain (Carpita, N. C. & Gibeaut, D. M. (1993), The Plant Journal, 3, pp. 1-30).

Species-specific differences occur as to the distribution of additional branching fucosyl- galactosyl residues (Hayashi, T. & Maclachlan, G. (1984), Plant Physio., 75, pp. 596-604). For <BR> <BR> instance, tamarind xyloglucan is not fucosylated (Vincken, J. -P. (1996), Enzymic modification of cellulose-xyloglucan networks, Thesis Wageningen Agricultural University).

Commercially available xyloglucan may be purchased in purified form from Megazyme (Australia) or as raw tamarind kernel powder from Polygal (POLYGUM 55).

According to the present invention xyloglucan obtained from monocotyledons and/or dicotelydons are preferred, in particular tamarind seeds.

The xyloglucan used according to the invention may also be a chemically or enzymatic modified xyloglucan.

Textile The process of the invention is applicable to all types of printed textiles. In context of the invention the term printed"textiles"includes printed fabrics and garments.

Fabric can be constructed from fibers by weaving, knitting or non-woven operations.

Weaving and knitting require yarn as the input whereas the non-woven fabric is the result of random bonding of fibers (paper can be thought of as non-woven). In the present context, the term"fabric"is also intended to include fibers and other types of processed fabrics.

Woven fabric is constructed by weaving"fiiling"or weft yarns between wrap yarns stretched in the longitudinal direction on the loom. The wrap yarns must be sized before weaving in order to lubricate and protect them from abrasion at the high speed insertion of the filling yarns during weaving. The filling yarn can be woven through the warp yarns in a"over one-under the next"fashion (plain weave) or by"over one-under two" (twill) or any other myriad of permutations. Strength, texture and pattern are related not only to the type/quality of the yam but also the type of weave. Generally, dresses, shirts, pants, sheeting's, towels, draperies, etc. are produced from woven fabric.

Knitting is forming a fabric by joining together interlocking loops of yarn. As opposed to weaving which is constructed from two types of yarn and has many"ends", knitted fabric is produced from a single continuous strand of yarn. As with weaving, there are many different ways to loop yam together and the final fabric properties are dependent both upon the yam and the type of knit. Underwear, sweaters, socks, sport shirts, sweat shirts, etc. are derived from knit fabrics.

Non-woven fabrics are sheets of fabric made by bonding and/or interlocking fibers and filaments by mechanical, thermal, chemical or solvent mediated processes. The resultant fabric can be in the form of web-like structures, laminates or films. Typical examples are disposable baby diapers, towels, wipes, surgical gowns, fibers for the"environmental friendly" fashion, filter media, bedding, roofing materials, backing for two-dimensional fabrics and many others.

According to the invention, the method of the invention may be applied to any textile known in the art (woven, knitted, or non-woven). The method of the invention may be applied to cellulose-containing or cellulosic fabrics, such as cotton, viscose, rayon, ramie, linen, lyocell (e. g., TENCELTM, produced by Courtauds Fibers), or mixtures thereof, or mixtures of any of these fibers together with synthetic fibres (e. g., polyester, polyamid, nylon) or other natural fibers such as wool and silk., such as viscose/cotton blends, lyocell/cotton blends, viscose/wool blends, lyocell/wool blends, cotton/wool blends ; flax (linen), ramie and other fabrics based on cellulose fibers, including all blends of cellulosic fibers with other fibers such as wool, polyamide, acrylic and polyester fibers, e. g., viscose/cotton/polyester blends, wool/cotton/polyester blends, flax/cotton blends etc. The term"wool,"means any commercially useful animal hair product, for example, wool from sheep, camel, rabbit, goat, llama, and known as merino wool, Shetland wool, cashmere wool, alpaca wool, mohair, etc. and includes wool fiber and animal hair. The method of the invention can be used with wool or animal hair material in the form of top, fiber, yarn, or woven or knitted fabric. The method of the invention may also be applied to synthetic textiles, e. g., polyester, polyamid, nylon. The textile fabric may be dyed or undyed.

Printing method The method of the invention is suited for removing print paste from printed textile after any kind of printing. Examples of commonly used techniques are printing on a Rotation film, a Rouleaux, a Flash film, a Transfer film device.

Dyes and pigments The term"dye"includes all substances that add color to textiles. They may be incorporated into the textile fiber by chemical reaction, absorption or dispersion. The term "pigment"includes insoluble, finely divided substances, such as titanium dioxide, used to deluster or color fibers, yarns or fabrics. For further details-see Hoechst Celanese.

Dictionary of Fiber and Textile Technology. 4th ed. Charlotte : Hoechst Celanese Corporation, 1990, which is hereby incorporated by reference. The method of the invention can be used for improved removal of any kind of print paste comprising a xyloglucan- containing thickener, including print paste comprising synthetic and natural dyes. Typical printing dyes are those with anionic functional groups (e. g. , acid dyes, direct dyes, Mordant<BR> dyes and reactive dyes), those with cationic groups (e. g. , basic dyes), and those chemically<BR> reacting with the fabric (e. g. , reactive dyes) as well as vat dyes, sulphur dyes, disperse dyes and solvent dyes, including napthol and metalized dyes. For example, pigments can be based on azo or phthalocyanine compounds.

Enzymes EC-numbers are often used for classification of enzymes. Reference is made to International Union Of Biochemistry and Molecular Biology (IUBMB) Enzyme Nomenclature.

It is to be understood that the term enzyme, as well as the various enzymes or enzyme classes mentioned herein, encompass wild-type enzymes, as well as any variant thereof that retains the activity in question. Such variants may be produced by recombinant techniques.

The wild-type enzymes may also be produced by recombinant techniques, or by isolation and purification from the natural source. In an embodiment the enzyme in question is well-defined, meaning that only one major enzyme component is present. This can be inferred, e. g. , by fractionation on an appropriate size-exclusion column. Such well-defined, or purified, or highly purified, enzyme can be obtained as is known in the art and/or described in publications relating to the specific enzyme in question.

Even if not specifically mentioned in connection with treatment of textiles with (an) enzyme (s) or agent (s) according to the method of the invention, it is to be understood that the enzyme (s) or agent (s) is (are) used in an"effective amount"to degrade xyloglucan so that the print paste thickener is removed from the printed textile in accordance with the method of the invention. The enzyme which is capable of degrading xyloglucan may be added at a concentration of 0.001-25, 000 micro gram enzyme protein/gram textile, preferably 0.01-10, 000 micro gram enzyme protein/g textile, more preferably 0.05-1, 000 micro gram enzyme protein/g textile, in particular 0.5-500 micro gram enzyme protein/gram textile.

The term"applied together with"or"used together with"means that the additional enzyme may be applied in the same, or in another step of the method of the invention. The other treatment step (s) in the method of the invention may be carried out upstream or downstream in the textile treatment method, as compared to the step in which the textile is treated with a xyloglucan-degrading enzyme.

Xyloglucanase Xyloglucanase activity has been believed to be identical to cellulolytic activity (EC 3.2. 1.4), i. e. , activity against beta-1, 4-glycosidic linkages in cellulose or cellulose derivative substrates, or at least to be a side activity in enzymes having cellulolytic activity. However, at least according to the present invention a true"xyloglucanase"is a true xyloglucan specific enzyme capable of catalyzing the solubilization of xyloglucan to xyloglucan oligosaccharides, but which does not exhibit substantial cellulolytic activity, e. g. , activity against the conventionally used cellulose-like substrates CMC (carboxymethylcellulose), HE cellulose and Avicel (microcrystalline cellulose). According to IUBMB Enzyme Nomenclature (2003) a xyloglucanase is classified as EC 3.2. 1.151. Pauly et al. Glycobiology 9 (1999) p.

93-100, discloses a xyloglucan specific endo-beta-1, 4-glucanase from Aspergillus aculeatus. Preferably the xyloglucanase according to the invention is produced by micro- organisms such as fungi or bacteria. Examples of useful xyloglucanases are family 12 xyloglucan hydrolyzing endoglucanases, in particular family 12 xyloglucan hydrolyzing endoglucanases, obtained from, e. g., Aspergillus aculeatus as described in WO 94/14953.

Another useful example is a xyloglucanase produced by Trichoderma, especially EGIII. The xyloglucanase may also be an endoglucanase with xyloglucanase activity and low activity towards insoluble cellulose and high activity towards soluble cellulose, e. g., family 7 endoglucanases obtained from, e. g., Humicola insolens. The used xyloglucanase may also be an enzyme which activity has been enhanced by adding a binding domain, e. g. , a cellulose binding domain, to said enzyme. Further, xyloglucanases tested in Example 1 are also specifically contemplated according to the invention.

Xvloqlucan endotransqlycosylase (XET) According to International Union Of Biochemistry and Molecular Biology (IUBMB) Enzyme Nomenclature (1999) XETs are classified as EC 3.4. 1.207. XETs breaks a beta- (1 ~4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to 04 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan. Stephen C. Fry et al. suggest in Biochem. J. (1992), 282, pp. 821-828 that XET is responsible for cutting and rejoining intermicrofibrillar xyloglucan chains and that XET thus causes the wall-loosening required for plant cell expansion.

Preferred XETs derived from fungi which belong to Basidiomycota, Zygomycota, Ascomycota or a Mitosporic fungus or gram-positive bacteria strains belonging to the genus Bacillus. A number of specifically contemplated XETs are disclosed in WO 98/28288 (which reference is hereby incorporated by reference).

Other Enzymes According to the invention, the xyloglucan-degrading enzyme (s) may be used together with (i. e. , combined with) other enzymes selected so that it can depolymerize other thickening ingredients used. Endo-acting enzymes are preferred. Thus, alginate lyase can be used to treat alginate and modified alginate. The alginate lyase may be derived from microbial strains of Bacillus stearothermophilus (e. g. , NRRL B-18394 described in WO 90/02974), Bacillus circulans and Klebsiella aerogenes. Starch and modified starch can be treated with amylase, e. g. , derived from strains of Bacillus, particularly B. amyloliquefaciens, B. licheniformis or B. stearothermophilus or Aspergillus, particularly A. oryzae or A. niger.

Endo-1, 4-beta-D-mannanase (EC 3.2. 1.78) can be used to treat galactomannans, guar gum and locust bean gum. This enzyme may be derived from Aspergillus, Humicola, or Tricoderma. Carrageenanase (EC 3.2. 1.83) may be used to treat carrageenan. Modified cellulose can be treated with a cellulase, e. g. , derived from Humicola, Tricoderma or Aspergillus. Advantageously, in the case of cellulose fibers the cellulase may be used to achieve softening of the textile simultaneously with the dye and thickener removal.

Laminarin may be treated with endo-1, 3-beta-D-glucanase (laminarinase, EC 3.2. 1.39). Thus, alginate containing laminarin is preferably treated with alginate lyase together with laminarinase.

In one embodiment the xyloglucan-degrading enzyme is used together with an esterase, preferably a cutinase and/or a lipase.

Process conditions The printed textile may first be rinsed with cold water, and then washed at high temperature with the addition of a detergent and sometimes also a suitable additive to decrease back-staining. This may be repeated until satisfactory amount of print paste thickener has been removed. The enzyme treatment can be applied in one of the hot washes of the printed textile, preferably the first hot wash. The process may be run in batch mode or continuous mode. The process may be applied on a winch, a beck, a jet dyer, a jig, a open- width washing machine, a pad roll or any other equipment available suitable for a washing process or a incubation of the enzyme with the textile before washing. The conditions applied for enzymatic removal of print paste thickener depend on the type of enzyme/thickener and the selected equipment.

According to the invention the printed textile may be optionally rinsed after the treatment with the xyloglucan-degrading enzyme. In an embodiment the rinsing is carried out in the presence of a surfactant.

The process conditions must be chosen according to the characteristics of the enzyme in question. They are generally in the range 20-120°C, pH 3-11, typically 30-90°C, pH 4-10 (or 4-9), especially 40-80°C (or 40-75°C), pH 5-9 (or 5.5-8. 5).

Surfactants As mentioned above the optional rinsing step may be carried out in the presence of a surfactant. Examples of surfactants suitable for use in practicing the present invention include, without limitation, nonionic (see, e. g. , U. S. Patent No. 4,565, 647); anionic; cationic; and<BR> zwitterionic surfactants (see, e. g. , U. S. Patent No. 3,929, 678); which are typically present at a concentration of between about 0.2% to about 15% by weight, preferably from about 1 % to about 10% by weight. Anionic surfactants include, without limitation, linear alkylbenzenesulfonate, alpha-olefinsulfonate, alkyl sulfate (fatty alcohol sulfate), alcohol ethoxysulfate, secondary alkanesulfonate, alpha-sulfo fatty acid methyl ester, alkyl-or alkenylsuccinic acid, and soap. Non-ionic surfactants include, without limitation, alcohol ethoxylate, nonylphenol ethoxylate, alkylpolyglycoside, alkyldimethylamineoxide, ethoxylated fatty acid monoethanolamide, fatty acid monoethanolamide, polyhydroxy alkyl fatty acid amide, and N-acyl N-alkyl derivatives of glucosamine ("glucamides").

All references referred to herein are hereby incorporated by reference.

MATERIALS & METHODS Enzymes : All of the below identified enzymes used in Example 1 are available on request from Novozymes A/S, Denmark Enzyme Organism Sample A SEQ ID NO: 2 and Example 3 of WO Tiarosporella phaseolina 98/38288 B SEQ ID NO: 2 of U. S. Patent No. 6,630, 340 Bacillus licheniformis C WO 01/12794 Malbranchea cinnamonas D EGIII disclosed in Example 4 of WO Aspergillus aculeatus 94/14953 E SEQ ID NO: 2 of WO 99/02663 Bacillus licheniformis Tamarind kernel powder was purchased from Bharat Gum Industries, India.

The tamarind kernel de-oiled powder has the following characteristics: Color : Off White powder Viscosity: 6000-7000 cps Charatertics: Free flowing Particle size: 98% through 300 mesh Protein: 17-18% Oil Content: Below 1.5% Viscometer: Sofraser Laboratory Viscometer Methods: Determination of xyloglucanase units (XGU or XyloU) : The xyloglucanase activity is measured using AZCL-xyloglucan from Megazyme, Ireland, as substrate.

A solution of 0.2 % of the blue substrate is suspended in a 0.1 M phosphate buffer pH 7.5 under stirring. The solution is distributed under stirring to 1.5 ml Eppendorf tubes (0.75 ml to each), 50 microL enzyme solution is added and they are incubated in an Eppendorf Thermomixer model 5436 for 20 min. at 40°C with a mixing of 1200 rpm. After incubation the colored solution is separated from the solid by 4 min. centrifugation at 14,000 rpm and the absorbance of the supernatant is measured at 600 nm. The assay is done in duplicates and the background done in duplicates is subtracted. The reading at 600 nm has to be between 0.2 and 1.5 for use in calculation of catalytic activity.

One XyloU unit is defined as the amount of enzyme resulting in an absorbance of 0.24 in a 1 cm cuvette at 600 nm.

EXAMPLES Example 1 Viscosity reduction of xyloglucan with xvloalucan degrading enzymes A dispersion of 2% tamarind kernel powder (TKP) was prepared in buffer (pH 6.5, 50 mM Potassium di-Hydrogen Phosphate + 26 mM di-Sodium Hydrogen Phosphate). This dispersion was treated with the various xyloglucanase disclosed in Table 1 below. Viscosity measurements were taken over time at 45°C.

Along with enzyme additions, blank trials were performed. Blanks are defined as tamarind kernel powder and buffer only. A standard curve of increasing TKP % was also included. The standard curves for each incubation time are shown in Figure 1.

The below Table lists the experimental conditions used Substrate: Tamarind Kernel Powder, 2% solution in buffer Std. curve 0,0. 1,0. 5,1, and 2% solution Buffer: pH 6.5, 50 mM Potassium Di-hydrogen Phosphate (6.81 9/l) + 26 mM Di-Sodium Hydrogen Phosphate (3.72 g/I) Total Volume : 8 ml Enzymes: Sample Organism A Tiarosporella phaseolina B Bacillus licheniformis C Malbrancea D Aspergillus aculeatus E Bacillus licheniformis Enzyme dose: 0, 0.001, 0.004 and 0.01 mg protein/ml solution Temperature: 45°C Time : Initial, 30,60 and 120 minutes (longer if needed) Viscometer: Sofraser Laboratory Viscometer Stirring: Moderate with small stir bars Figures 2 and 3 illustrate viscosity reduction with increased enzyme dose for initial measurements and 30 minutes respectively. 60 and 120 minute measurements were also taken (see Figures 4 and 5).

Table 1: Viscosity Measurements over time, Viscosity is measured in mV. Incubation Enzyme A B C D E time dose Minutes Micro gram/mL Initial 0 471 471 471 471 471 1 283 288 481 534 446 4 170 176 440 521 310 10 130 122 376 485 220 30 0 527 527 527 527 527 1 64 65 115 248 94 4 58 53. 5 71 158 70 10 56 56. 5 60 129 62 60 0 556 556 556 556 556 1 57 62 93 208 79 4 57 53 65 137 62 10 57 57 57 114 59 120 0 599 599 599 599 599 1 50. 5 56 77 181 68 4 53. 5 51 58 121 60 10 53 55 53 101 57 Note that the lower mV measured; the lower the viscosity is.