MXPA97003931A - A method for obtaining a cellulose textile fabric with reduced tendency to fris formation - Google Patents

Abstract

The present invention relates to a method for obtaining a cellulosic textile fabric which has a strongly reduced tendency to form frising, preferably corresponding to a note or rating of frising of at least 4, more preferably of at least 4.5, which method comprises treating the fabric with a cellulase capable of carrying out a partial hydrolysis of the surface of the fiber corresponding to a loss in weight of less than 2%, based on the untreated cellulose fabric. The cellulase is preferably a 43 kD endoglucanase derived from or producible from Humicola insolens, DSM 1800, SEQ ID No: 1, or a functional analogue of said cellulase such as a variant that is modified by substitution of one or more amino acid residues in one or more of positions 8, 55, 58, 62, 67, 132, 147, 162, 221, 222, 223, 280, or modified by truncation, preferably genetic truncation, in any position from position 2

Description

A METHOD FOR OBTAINING A CELLULOSE TEXTILE FABRIC WITH REDUCED TENDENCY TO THE FORMATION OF FRISADO The present invention relates to a method for obtaining a cellulosic textile fabric that has a strongly reduced tendency for the formation of frising. More specifically, the invention relates to a method wherein the cellulosic textile fabric is subjected to an enzymatic treatment with a cellulase without substantial loss of weight.

BACKGROUND OF THE INVENTION Without the application of the finishing components, most cotton fabrics and cotton blend fabrics have a tactile appearance that is rather hard and rigid. The surface of the fabric is also not smooth because small microfibrils of lint that project on it. In addition, after a relatively short period of wear, the frisado appears on the surface of the fabric, which gives it a worn, unattractive appearance. REF: 24745 A known method for obtaining a soft and smooth fabric is to hold the cellulosic fabrics to treatment by cellulolytic enzymes during their manufacture. This treatment is known as Bio-Polishing (hereinafter referred to as bio-polishing), see Bazin J. and Sasserod, S .: Enzymatic Bio-Polishing of Cellulosic Fabric, document presented on October 25, 1991, at "58 ° Congress of the Association of Chemicals of the Textile Industry ", Mulhouse, France, which is incorporated by reference herein. The biopolishing is a specific treatment of the yarn surface which improves the quality of the fabric with respect to the touch and appearance, without loss of the wettability of the fabric. The most important effects of biopolishing can be characterized by less linting and frising, increased gloss / luster, improved fabric feel, increased durable softness and improved water absorbency. Biopolishing usually takes place in the wet processing of the manufacture of knitted and woven fabrics. Wet processing comprises steps such as, for example, scouring, thorough washing, bleaching, washing, staining / printing and finishing. During each of these steps, the fabric can be subject to mechanical action. However, since cellulolytic enzymes catalyze the hydrolysis of the cellulosic fiber surface, the enzymatic action will eventually result in a loss in fiber weight of the fabric. Although the biopolishing is carried out in such a way as to obtain partial, controlled hydrolysis of the surface of the fiber, an appropriate polishing effect has been obtained to date without excessive loss of fabric strength, at a loss in fabric weight of 3-5% w / w. Such loss in weight is undesirable for the textile industry and, for economic reasons, makes the biopolishing process less desirable. Thus, an object of the present invention is to provide a method for obtaining a cellulosic textile fabric with a greatly reduced tendency to form frost, but without substantial loss of fabric weight.

BRIEF DESCRIPTION OF THE INVENTION Surprisingly it has been found that it is possible to obtain a cellulosic textile fabric which has a strongly reduced tendency to frizz formation, at a significantly reduced weight loss by clamping the fabric to a biopolishing process, preferably using single component cellulases. Accordingly, the method of the invention comprises the treatment of a textile fabric containing cellulose fibers with a cellulase capable of performing a partial hydrolysis of the surface of the fiber, corresponding to a weight loss of less than 2% w / w , based on untreated cellulosic textile fabric, or corresponding to a weight loss of less than about 2%, calculated as the difference, in percentage terms, of the weight loss of the textile fabric treated with cellulase and the Weight loss of the textile fabric treated without cellulase (control).

DETAILED DESCRIPTION OF THE INVENTION The fabric In the present context, the terms "cellulosic textile fabric" and "textile fabric containing cellulose fiber" are intended to indicate any type of fabric, in particular woven or knitted fabric, prepared from a cellulose-containing material , which contains cellulose or cellulose derivatives, for example, from paper pulp and cotton. Also in the present context, the term "fabric" is intended to include garments and other types of processed fabrics. Examples of cellulosic textile fabric is cotton, viscose (rayon); lyocell; flax (flax); all viscose, cotton or lyocell blends with other fabrics such as polyester; viscose / cotton blends, lyocell / cotton blends, viscose / wool blends, lyocell / wool blends, cotton / wool blends; flax (flax), 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, for example, viscose / cotton / polyester blends, blends of wool / cotton / polyester, flax / cotton blends, etc. In the present context, the term "strongly reduced tendency to frizz formation" is meant to imply a permanent (and excellent) resistance to the formation of specks or pellets on the surface of the treated fabric (biopolished) compared to the fabric that has not been subjected to the method of the present invention. The tendency of the formation of frits or pellets can be tested according to the Swiss standard SN 198525, published in 1990 by Schweizerische Normen-Vereinigung, Kirchenweg 4, Postfach, CH-8032 Zürich, Switzerland, which describes a resistance test framing for textiles, which in turn is based on the Swiss standards SNV 95 150 (Standard climatic conditions for textiles and test conditions for physical tests under standard climatic conditions) and SN 198 529 (Textile test - "Scheuerfestigkeit" - Martindale method). The results of the test are expressed in terms of "frisado notes" which is a rating on a scale from note 1 of frisado (strong formation of balls) to frisado of note 5 (little or no formation of balls), allowing frisado notes of 1/2. In a preferred embodiment of the present invention, the method provides a textile fabric preferably having a frill note of at least 4, more preferably at least 4.5, especially 5, measured according to SN 198525 (1990). In another preferred embodiment, the method of the invention provides a textile fabric having a rating that is at least 1, preferably at least 2, especially at least 3, note (s) of frising, higher than the corresponding textile fabric not treated; Absolute fringe notes are measured according to SN 198525 (1990). According to the method of the invention, the partial hydrolysis of the surface of the fiber corresponds to a weight loss of less than about 2% w / w, preferably a weight loss of less than about 1.8% w / w, more preferably less than about 1.5% w / w. The loss in weight is determined under controlled conditions, for example according to SNV 95150, see above. The loss in weight is expressed as the difference, in terms of the percentage, of the weight loss of the textile fabric treated with cellulase and the loss in weight of the textile fabric treated without cellulase (control).

The process As mentioned above, the treatment of the fabric with cellulase can be carried out simultaneously with other fabric manufacturing processes, for example the scouring or after the "whitening" of the fabric, it is understood that the method of the invention can be carried out in any step of the conventional wet textile processing, preferably after scouring or whitening of the textile fabric, either simultaneously with a conventional process step (well known) or as an additional process step.

The method will typically be achieved in high speed circular systems such as jet overflow dyeing machines, high speed hoists and dye boats. An example of a useful high-speed system is the "Aero 1000" manufactured by Biancalani, Italy. Alternatively, the method can be carried out in a two-step biopolishing process, for example, as described in the International Patent Application published as WO 93/20278, wherein the first step is a separate treatment with cellulase which it is carried out essentially without mechanical treatment, and followed by a second case wherein the fabric is subjected to a mechanical treatment. This treatment with cellulase can be carried out in a J-chamber or fulfilled-rolled or in padded-bath. The cellulase treatment according to the present invention and the scouring are reconcilable processes that can be conducted under the same conditions, for example pH, temperature, dosage / time ratio, etc. By performing these processes simultaneously, the entire process of manufacturing the fabric is shortened. Such time-saving arrangements are a major benefit of the process of the invention. The enzyme dose depends to a large extent on the reaction time of the enzyme, for example, a relatively short enzymatic reaction time requires a relatively increased dose of enzyme, and vice versa. In general, the dose of the enzyme can be stipulated according to the available reaction time. In this way the cellulase treatment, of fabric according to the present invention, can be brought into conformity for example with the conditions of scouring, if for example these two reactions are to be carried out simultaneously. An enzyme / time dose ratio can be used, similar to what is known from conventional biopolishing. Preferred doses of enzyme are from about 100 to about 100,000 ECU / kg of fabric, more preferably, from about 500 to about 20,000 ECU / kg of fabric, especially from about 1,000 to about 5,000 ECU / kg of fabric. Typically, the reaction time is from about 10 minutes to about 4 hours, preferably from about 20 minutes to about 2 hours, but the reaction can be carried out for any period of time between about 1 minute and about 24 hours, depending on the specific type of processing equipment. The method of the invention can be carried out in the presence of certain components which can be added to the cellulase, for example, the formulated cellulase composition, or separately to wash the liquor where the enzyme treatment takes place. Examples of such components include a stabilizer, a wetting agent, a buffer and a spraying agent. The stabilizer can be an agent that stabilizes the cellulolytic enzyme. The wetting agent serves to improve the wettability of the fiber, whereby rapid and uniform scouring can be obtained. The wetting agent is preferably of a type stable to oxidation. The buffer may suitably be a phosphate, borate, citrate, acetate, adipate, triethanolamine, monoethanolamine, diethanolamine, carbonate (especially alkali metal or alkaline earth metal carbonate, in particular sodium or potassium or ammonium and HCl salts), diamine, especially diaminoethane, imidazole, or amino acid buffer. Preferably, the buffer is a buffer of mono-, di-, or triethanolamine. The spraying agent can suitably be selected from nonionic, anionic, cationic, ampholytic or amphoteric surfactants. More specifically, the spraying agent can be selected from carboxymethylcellulose, hydroxypropylcellulose, alkyl-aryl sulfonates, long-chain alcohol sulphates (primary and secondary alkyl sulfates), sulfonated olefins, sulfated monoglycerides, sulfated ethers, sulfosuccinates, sulfonated methyl ethers, alkane sulfonates, phosphate esters, alkyl isothionates , acrylic sarcosides, alkyl taurids, fluorosurfactants, fatty alcohol condensates and alkylphenol, fatty acid condensates, condensates of ethylene oxide with an amine, condensates of ethylene oxide with an amide, block polymers (polyethylene glycol, polypropylene glycol, ethylene diamine) condensed with ethylene or propylene oxide), sucrose esters, sorbitan esters, alkylamides, fatty amine oxides, ethoxylated monoamines, ethoxylated diamines, ethoxylated polyamines, ethoxylated amine polymers and mixtures thereof. Preferably, the dispensing agent is an ethoxylated fatty acid ester, or a nonylphenyl polyethylene glycol ether. In addition, the method of the invention can be carried out in the presence of a conventional anti-redeposition agent, for example, polymeric agents such as polyvinylpyrrolidone (PVP), carboxymethylcellulose (CMC), and polyacrylates.

The enzyme In the present context, the term "cellulase" or "cellulolytic enzymes" refers to an enzyme that catalyzes the degradation of cellulose to glucose, cellobiose, triose and other cellooligosaccharides. In the present context, the term "enzyme" or "cellulase enzyme" is understood to include a mature protein or a precursor form thereof, as well as a functional fragment thereof, which essentially has the activity of the length enzyme. complete In addition, the term "enzyme" is intended to include homologs or analogues of said enzyme. Such homologs comprise a sequence of amino acids that show a degree of identity of at least 60% with the amino acid sequence of the progeny enzyme, for example, the progenitor cellulase. The degree of identity can be determined by conventional methods, see for example Altshul et al., Bull. Math. Bio. 48: 603-616, 1986. and Henikoff and Henikoff, Proc. Nati Acad. Sci '. USA 89: 10915-10919, 1992. In summary, two amino acid sequences are aligned to optimize the alignment qualifications using a penalty of 10 empty space aperture, a penalty of 1 empty space extension, and the matrix of qualification "blosu 62" by Henikoff and Henikoff, upra. Alternatively, the homologue or analogue of the enzyme can be one encoded by a nucleotide sequence hybridizing with an oligonucleotide probe prepared based on the nucleotide sequence or an amino acid sequence under the following conditions: pre-rinse in 5 x SSC and prehybridization by 1 hour at about 40 ° C in a 20% formamide solution, 5 x Denhardt's solution, 50 mM sodium phosphate, pH 6.8, and 50 μg of calf thymus DNA, sonicated, denatured, followed by hybridization in the same solution supplemented with 100 μM ATP for 18 hours at about 40 ° C, followed by a wash in 0.4 x SSC at a temperature of about 45 ° C. The molecules to which the oligonucleotide probe is hybridized under these conditions are detd using standard deton methods (for example Sourthern spotting). Homologs of the present enzyme may have one or more amino acid substitutions, deletions or additions. These changes are preferably of a minor nature, which are conservative substitutions of amino acids that do not significantly affthe folding or activity of the protein, small deletions, typically from one to about 30 amino acids; small amino- or carboxyl-termini extensions, such as an amino-terminal methionine residue, a small peptide linker of up to about 20-25 residues, or a small extension that facilitates purification, such as a poly-histidine moiety, a antigenic epitope or a linkage domain. See generally Ford et al., Protein Expression and Purification 2: 95-107, 1991. Examples of conservative substitutions are within the group of basic amino acids (such as arginine, lysine, histidine), acidic amino acids (such as glutamic acid and aspartic acid), polar amino acids (such as glutamine and asparagine), hydrophobic amino acids (such as leucine, isoleucine, valine), aromatic amino acids (such as phenylalanine, tryptophan, tyrosine) and small amino acids (such as glycine, alanine, serine, threonine , methionine). It will be apparent to those skilled in the art that such substitutions can be made outside the critical regions for the function of the molecule, and still result in an active enzyme. The essential amino acids for the activity of the enzyme of the invention, and therefore preferably not subjto substitution, can be identified according to methods known in the art, such as site-dird mutagenesis or alanine scanning mutagenesis. (Cunningham and Wells, Science 244, 1081-1085, 1989). In the latter technique mutations are introduced into each residue in the molecule and the resulting mutant molecules are tested for cellulolytic activity, to identify the amino acid residues that are critical for the activity of the molecule. The ligand-receptor interaction sites can also be determined by analysis of the crystal structure as determined by techniques such as nuclear magnetic resonance, crystallography or photoaffinity labeling. See, for example, de Vos et al., Science 255: 306-312, 1992; Smith et al., FEBS Lett. 309: 59-64, 1992. The homolog may be an allelic variant, for example, an alternative form of a gene arising through mutation, or an altered enzyme, encoded by the mutated gene, but having substantially the same activity than the enzyme of the invention. Hence, the mutations can be silent (without change in the encoded enzyme) or can encode enzymes that have altered amino acid sequence. The homologue of the present enzyme can also be a homologous species or genus, for example an enzyme with a similar activity derived from another species. A homolog of the enzyme can be isolated by preparing a genomic or cDNA library from a cell of the species in question, and selecting the DNA sequences that code for all or part of the homolog, by using the synthetic oligonucleotide probes according to standard techniques, for example, as described by Sambrook et al., Molecular Cloning: A Laboratory Manual, 2nd Ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, 1989, or by means of the chain reaction of polymerase (PCR) using specific primers as described by Sambrook et al., upra. Preferably, the cellulolytic enzyme to be used in the method of the invention is a single component (recombinant) cellulase, for example a cellulase essentially free of other proteins or cellulase proteins. A recombinant cellulase component can be cloned and expressed according to conventional standard techniques for the skilled person. In a preferred embodiment of the invention, the cellulase to be used in the method is an endoglucanase (EC 3.2.1.4), preferably a single component (recombinant) endoglucanase. Preferably, the cellulase is a microbial cellulase, more preferably a bacterial or fungal cellulase. Examples of bacterial cellulose are cellulases derived from or produced by bacteria from the group of genera consisting of Pseudomonas or Bacillus lautus. The cellulase or endoglucanase can be an acid, neutral or alkaline endoglucanase cellulase, for example that exhibits maximum cellulolytic activity in the acid, neutral or alkaline range, respectively. Accordingly, a useful cellulase is a cellulase that is acidic, preferably an acid, fungal cellulase, more preferably an acid, fungal cellulase enzyme with substantial cellulolytic activity to acidic conditions, which is derived or producible by fungi from the groups of genera consisting of Trichoderma, Actinomyces , Mirothecium, Aspergillus, and Botrytis. A useful, preferred acidic cellulase is derived or produced by fungi from the group of species consisting of Trichoderma viride, Trichoderma reesei, Trichoderma longibrachiatum, Myrothecium verrucaria, Aspergillus niger, Aspergillus oryzae, and Botrytis cin rea. Another useful cellulase or endoglucanase is a neutral or alkaline cellulase, preferably a fungal, neutral or alkaline cellulase, more preferably a fungal alkaline cellulase or endoglucanase, with substantial cellulolytic activity at alkaline conditions, which is derived from or producible by fungi from the group of Consistent genera of Aspergillus, Penicillium, Myceliophthora, Humicola, Irpex, Fusarium, Stachibotrys, Scopulariopsis, Chaetomium, Mycogone, Verticillium, Myrothecium, Papulospora, Gliocladium, Cephalosporium and Acremonium. A preferred alkaline cellulase is derived from or producible by fungi from the group of species consisting of Humicola insolens, Fusarium oxysporum, Myceliopthora thermophile, or Cephalosporium sp. , preferably from the group of species consisting of Humi cola insol ens, DMS 1800, Fusarium um oxysporum, DSM 2672, Mycel and opthora termophil e, CBS 11 7. 65, or Cephal ospori um sp. , RYM-202. A preferred example of a native or progenitor cellulase is an alkaline endoglucanase which is immunologically reactive with an antibody raised against a highly purified endoglucanase of approximately 43 kD derived from Humi col a insol ens, DMS 1800, or which is a derivative of the endoglucanase of approximately 43 kD showing cellulase activity. A preferred endoglucanase component has the amino acid sequence described as SEQ ID No. 1, which is also described in International Patent Application published as WO 91/17243, SEQ ID No. 2, which is incorporated by reference in the I presented. Another preferred endoglucanase component is the nuclear enzyme corresponding to the amino acid sequence described as SEQ ID No. 1, but having the amino acid sequence corresponding to position 1-213, for example truncated at position 213. It is contemplated that other useful endoglucanases are enzymes having amino acid sequences corresponding to the amino acid sequence described as SEQ ID No. 1, but which are truncated, preferably genetically truncated, at any position between position 213 and position 247 of SEQ ID. No. 1, for example having a consistent amino acid sequence between 213 and 247 amino acid residues. Other examples of useful cellulases are variants which have, as a progenitor cellulase, a cellulase of fungal origin, for example a cellulase derivable from the fungus strain of the genus Humi col a, Tri choderma or Fusari um. For example, the parent cellulase may be derivable from a strain of the fungus species H. insol ens, Tri choderma reesei or F. oxy sporum, preferably the endoglucanase preferably approximately 43 kD derived from Humi col a insol ens, DMS 1800, or is a functional analog of any of the progenitor cellulases which i) comprises an amino acid sequence that is at least 60% homologous to the amino acid sequence of the parent cellulase, ii) reacts with an antibody produced against the progenitor cellulase, and / or iii) is encoded by a DNA sequence that hybridizes with the same probe as a DNA sequence that codes for the progenitor cellulase.

Property i) of the analogue is intended to indicate the degree of identity between the analog and the progenitor cellulase, indicating a derivation of the first sequence from the second. In particular, a polypeptide is considered to be homologous to the progenitor cellulase if a comparison of the respective amino acid sequences reveals an identity greater than about 60%, such as above 70%, 80%, 85%, 90% or even 95%. Sequential comparisons can be made via algorithms, such as that described as Lipman and Pearson (1985). The additional properties ii) and iii) of the parent cellulase analog can be determined as follows: Property ii), for example immunological cross-reactivity, can be assayed using an antibody produced against or reactive with at least one epitope of the progenitor cellulase. The antibody, which can be either monoclonal or polyclonal, can be produced by methods known in the art, for example as described by Hudson et al., 1989. Immunological cross-reactivity can be determined using assays known in the art., examples of which are Western blotting or radial immunodiffusion assay, for example, as described by Hudson et al., 1989. The oligonucleotide probe used in the characterization of the analogue according to property iii) defined above, can be suitably prepared based on the complete or partial nucleotide or amino acid sequence of the parent cellulase. Hybridization can be carried out under any appropriate conditions that allow the DNA sequences to hybridize. For example, such conditions are hybridization under specific conditions, for example involving pre-rinse in 5xSSC and prehybridization for about 1 hour at 40 ° C in a 20% formamide solution, 5x Denhardt's solution, 50 sodium phosphate. mM, pH 6.8, and 50 μg of sonicated calf thymus DNA, denatured, followed by hybridization in the same solution supplemented with 100 μM ATP for 18 hours at about 40 ° C, or other methods described for example by Sambrook et al. 1989. Examples of useful cellulase variants are variants of the 43 kD endoglucanase derived from or producible by Humi col a insol ens, DMS 1800, SEQ ID No: 1, modified by substitution by one or more amino acid residues in one or more of the positions 8, 55, 58, 62, 67, 132, 147, 162, 221, 222, 223, 280; and optionally further modified by truncation, preferably genetic truncation, at any position from position 213. Preferred cellulase variants are variants of the 43 kD endoglucanase derived or producible by Humi cola insol ens, DSM 1800, SEQ ID No: 1, modified by substitution of one or more amino acid residues as follows: Y8F S55E / D D58A / S / N W62E D67R / N F132A / D / E / G Y147S A162P V221S N222S Q223T Y280F Surprisingly, it has been found that in the case of the use of an alkaline endoglucanase such as the endoglucanase of DSM 1800 of H. insol ens of 43 kD, or the aforementioned modified variants thereof, may be advantageous for carrying out the method of the present invention, at a pH below about 9, preferably at a pH below 6, more preferably at a pH from about 4.5 to about 5.5, especially at a pH of about 5.0. In the context of this invention, the cellulase activity can be expressed in ECU. The cellulolytic enzymes hydrolyze CMC, which increases the viscosity of the incubation mixture. The resulting reduction in viscosity can be determined by a vibration viscometer (for example, MIVI 3000 from Sofraser, France). The determination of the cellulolytic activity, measured in terms of ECU, can be determined according to the following analysis method (test): 'the ECU test qualifies the amount of catalytic activity present in the sample, by measuring the ability of the sample to reduce the viscosity of a solution of carboxymethylcellulose (CMC). The test is carried out at 40 ° C; pH 7.5; 0.1 M phosphate buffer; 30 minutes time; using a relative enzyme standard, for the reduction of the viscosity of the CMC (carboxymethylcellulose Hercules 7 LFD) as a substrate; The concentration of the enzyme is approximately 0.15 ECU / l. The standard is defined for 8200 ECU / g. Although useful cellulase can be used as such in the method of the present invention, it is preferred that it be formulated in an appropriate composition. In this way, the useful cellulase can be used in the form of a granulate, preferably a non-powdered granulate, a liquid, in particular a stabilized liquid, a suspension, or in a protected form. Dust-free granulates can be produced, for example as described in U.S. Patent Nos. 4,106,991 and 4,661,452 (both to Novo Nordisk A / S) and can optionally be coated by methods known in the art. The liquid enzyme preparations can, for example, be stabilized by the addition of a polyol such as, for example, propylene glycol, a sugar or sugar alcohol or acetic acid, according to established methods. Other enzyme stabilizers are well known in the art. Protected enzymes can be prepared according to the method described in European Patent No. EP 238,216. The functioning of the enzymes depends to a large extent on the process conditions such as, for example, the pH and the temperature. In carrying out the process of this invention, of course, factors such as, for example, pH-dependent functioning and thermal stability, in the choice of the cellulolytic enzyme must be taken into consideration. Other conditions such as, for example, the addition of wetting agents, etc., also depend on the complete process to be performed, as well as on the enzyme used. The invention is further illustrated by the following non-limiting example.

EXAMPLE Apparatus: The test was carried out on an apparatus of the Launder-O-Meter Atlas LP2 using 2 sample cut-outs per container.

Textile: 100% cotton fabric knitted by interlocking, bleached, 205 g / m2. The fabric was cut into pieces of a size of 14 x 12 pm (approximately 3.5 g each) and conditioned overnight at 20 ° C and 65% relative humidity under constant conditions.

Enzymes: A: Reference (Cellusoft L, a commercial preparation of acid cellulase, produced and sold by Novo Nordisk A / S, DK-2880 Basvaerd, Denmark). B: 43 kD endoglucanase from Humi cola insol ens, DSM 1800. C: Variant of B (substitution D58A) D: Variant of B (substitution F132D) E: Variant of B (substitution Y280F) F: Variant of B (substitution D67R) G: Variant of B (substitution Y147S) H: Variant of B (substitution S55E) J: Variant of B (substitutions Y8F, W62E, A162P, V221S, N222S, Q223T) K: Variant of B (substitution Y147N) Experimental conditions: [Biopolished with Launder-O-Meter) Four containers (8 samples) were used for each test.

Liquor ratio 1:20 Liquor volume 140 mi Abrasive agent 20 steel balls (d = 14 mm, 11 g) PH 5.0 Shock absorber 1 g / 1 acetate Time 60 minutes Temperature 55 ° C Inactivation: Each test was terminated by washing all the samples at 70 ° C followed by rinsing three times in a standard European household laundry machine, AEG oko-Lavamat 665.

Drying: The samples were air dried and conditioned overnight at 20 ° C and 65% relative humidity.

Tests : The commercial enzyme preparation A was tested in 4 doses in the range of 0-4.0% w / w, based on the weight of the textile. Each of the B-K enzyme preparations were tested in 4 doses in the range of 0-5.0 ECU / g of textile.

Results: The following parameters were measured / calculated: * Loss in weight, in percentage terms, of the weight loss of the textile fabric treated with cellulase, and the loss in weight of the textile fabric treated without cellulase (control).

* Qualification of frisado (PN), measured according to SN 198525 (1990) using a Martindale Frisado Tester at 500 revolutions.

The qualification of frisado of the untreated textile, as well as of the textile treated without cellulase (witness) was 1.

The following table shows the measured weight loss corresponding to a score or scoring rating resulting from 4.5 of the textile treated with cellulase.

Table LIST OF SEQUENCES (1) GENERAL INFORMATION: (i) APPLICANT: NOVO NORDISK A / S (ii) TITLE OF THE INVENTION: A Method for Obtaining a Cellulose Textile Fabric with Reduced Tendency to the Formation of Frisado (iii) NUMBER OF SEQUENCES: 1 (iv) ADDRESS FOR CORRESPONDENCE: (A) RECIPIENT: NOVO NORDISK A / S, Patent Corporation (B) STREET: Novo Alie (C) CITY: Bagsvaerd (E) COUNTRY: Denmark (F) CÓDI GO POSTAL: DK-2880 (iv) COMPUTER LEGIBLE FORM: (A) TYPE OF MEDIUM: Diskette (B) COMPUTER: IBM compatible PC (C) OPERATING SYSTEM: PC-DOS / MS-DOS (D) SOFTWARE: Patentln Relay # 1.0 , Version # 1.25 (2) INFORMATION FOR SEQ ID NO: 1: (i) CHARACTERISTICS OF THE SEQUENCE: (A) LENGTH: 305 amino acids. (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) TYPE OF MOLECULE: protein (vi) ORIGINAL SOURCE: (A) ORGANISM: Humi cola Insol ens (B) STRING: DSM 1800 (xi) DESCRIPTION OF THE SEQUENCE: SEQ ID NO. 1: Met Arg Ser Ser Pro Leu Pro Pro? Val Val? La? Pro Leu -21 -20 -15 -10 Val Leu? The Leu? The? La? Sp Gly? Rg Ser Thr? Rg Tyr Trp? Sp Cys -5 1 5 10 Cys Lys Pro Ser Cys Gly Trp? Lys Lys? Pro Val? Sn Gln Pro 15 20 25 Val Phß Ser Cys? Sn? Asn Ph? Gln? Rg lie Thr? Sp Ph? Sp? La 30 35 40 Lys Ser Gly Cys Glu Pro Gly Gly Val? Tyr Ser Cys? La? Sp G n 45 50 55 Thr Pro Trp? Val? Sn Aßp? Sp Ph? Ala Leu Gly Phe Ala Wing Thr 60 65 70 75 Ser lie Ala Gly Ser? Sn Glu? The Gly Trp Cys Cys Ala Cys Tyr Glu 80 85 90 Leu Thr Phß Thr Ser Gly Pro Val? The Gly Lys Lys Met Val Val Gln 95 100 105 Ser Thr Ser Thr Gly Gly? Sp L? U Gly Ser? Sn His Ph? Asp Leu Asn 110 115 120 lie Pro Gly Gly Gly Val Gly lie Phß? sp Gly Cys Thr Pro Gln Phe 125 130 135 Gly Gly Lßu Pro Gly Gln? Rg Tyr Gly Gly He Ser Ser? Rg? Sn Glu 140 145 150 155 Cys? Sp? Rg Ph? Pro? Sp? La Lys Pro Gly Cys Tyr Trp? Rg Ph? 160 165 170 Asp Trp Phe Lys Asn Wing Asp? Sn Pro Ser Ph? Ser Ph?? Gg Gln Val 175 180 185 Gln Cys Pro? Glu Leu Val? La? Rg Thr Gly Cys? Rg? Rg? Sn? Sp 190 195 200 Sp Gly Asn Phß Pro? Val Gln Lie Pro Ser Ser Ser Thr Ser Ser 205 210 2X5 Pro Val Asn Gln Pro Thr Ser Thr Be Thr Thr Ser Thr Ser Thr Thr 220 225 230 235 Be Ser Pro Pro Val Gln Pro Thr Pro Pro Ser Gly Cys Thr Ala Glu 240 245 250 Arg Trp Wing Gln Cys Gly Gly Aßn Gly Trp Ser Gly Cyß Thr Thr Cyß 255 260 265 Val Ala Gly Ser Thr Cys Thr Lys He? ßn? Sp Trp Tyr His Gln Cy? 270 275 280 Leu It is noted that in relation to this date, the best method known to the applicant to carry out the aforementioned invention, is that which is clear from the present description of the invention. Having described the invention as above, property is claimed as contained in the following:

Claims (18)

1. A method for obtaining a cellulosic textile fabric having a strongly reduced tendency to form frising, the method is characterized in that it comprises the treatment of a textile fabric containing cellulose fiber, with a cellulase (cellulolytic enzyme) capable of making a partial hydrolysis of the surface of the fiber, corresponding to a weight loss of less than 2% w / w, based on the untreated cellulose fabric.

2. A method according to claim 1, characterized in that the formation of frising corresponds to a frising rating or rating of at least 4, more preferably of at least 4.5.

3. A method according to claim 1 or 2, characterized in that the textile fabric contains cellulose fibers selected from the group consisting of cotton, viscose (rayon), lyocell; all viscose, cotton or lyocell blends with other fibers such as polyester; viscose / cotton blends, lyocell / cotton blends, viscose / wool blends, lyocell / wool blends, cotton / wool blends; flax (flax), ramie and other fabrics based on cellulose fibers, including all blends of cellulosic fiber, with other fibers such as wool, polyamide, acrylic and polyester fibers, for example, viscose / cotton / polyester blends, blends wool / cotton / polyester, and flax / cotton blends.

4. A method according to any of claims 1-3, characterized in that the cellulase is a single component cellulase, preferably an endoglucanase (EC 3.2.1.4).

5. A method according to claim 3 or 4, characterized in that the cellulase is a microbial cellulase, preferably a bacterial or fungal cellulase, more preferably a fungal cellulase.

6. The method according to claim 5, characterized in that the cellulase is an acid cellulase, preferably a fungal acid cellulase, more preferably a fungal acid cellulase with substantial cellulolytic activity at acidic conditions, which is derived from or producible by fungi from the group of consistent genera of Trichoderma, Actinomyces, Trichoderma, Myrothecium, Aspergillus, and Botrytis.

7. The method according to claim 6, characterized in that the cellulase is derived from or producible by fungi from the group of species consisting of Trichoderma viride, Trichoderma longibrachiatum, Myrothecium verrucaria, Aspergillus niger, Aspergillus oryzae, and Botrytis cinerea.

8. The method according to claim 5, characterized in that the cellulase is a neutral or alkaline cellulase, preferably a fungal, neutral or alkaline cellulase, more preferably an alkaline fungal cellulase with substantial cellulolytic activity at alkaline conditions, which is derived from or producible by fungi of the group of genera consisting of Aspergillus, Penicillium, Myceliphthora, Humicola, Irpex, Fusarium, Stachybotrys, Scopulariopsis, Chaetomium, Mycogone, Verticillium, Myrothecium, Papulospora, Gliocladium Cephalosporium and Acremonium.

9. The method according to claim 8, characterized in that the alkaline cellulase is derived from or producible by fungi from the group of species consisting of Humicola insolens, Fusarium oxisporum, Myceliopthora thermophila, or Cephalosporium sp.

10. The method according to claim 9, characterized in that the cellulase is derived from or producible by fungi from the group of species consisting of Humicola insolens, DSM 1800, Fusarium oxisporum, DSM 2672, Myceliopthora thermophila, CBS 117.65, or Cephalosporium sp. , RYM-202.

11. The method according to any of claims 8-10, characterized in that the treatment is carried out at a pH below 9, preferably at a pH below 6, more preferably at a pH from about 4.5 to about 5.5, especially at a pH of about 5.0.

12. The method according to any of claims 10 or 11, characterized in that the cellulase is a 43 kD endoglucanase derived or produced by Humi col a insol ens, DSM 1800, SEQ ID No: 1, or a functional analogue of said enzyme which i) comprises an amino acid sequence that is at least 60% homologous with the amino acid sequence of the progenitor cellulase, ii) reacts with an antibody produced against the progenitor cellulase, and / or iii) is encoded by a DNA sequence that hybridizes with the same probe as a DNA sequence that codifies for the progenitor cellulase.

13. The method according to claim 12, characterized in that the cellulase is a variant of the 43 kD glucanase derived or producible from Humi col a insol ens, DSM 1800, SEQ ID No: 1, modified by substitution of one or more residues of amino acids in one or more positions at positions 8, 55, 58, 62, 67, 132, 147, 162, 221, 222, 223, 280; or modified by truncation, preferably genetic truncation, in a position from position 213.

14. The method according to claim 12, characterized in that one or more of the amino acid residues are substituted as follows Y8F S55E / D D58A / S / N W62E D67R / N F132A / D / E / G Y147S A162P V221S N222S Q223T Y280F

15. The method according to claim 5, characterized in that the bacterial cellulose is derived from or producible by bacteria from the group of genera consisting of Pseudomonas or Bacillus' lautus.

16. The method according to any of the preceding claims, characterized in that the treatment is carried out in any stage of processing a textile fabric manufacturing process, conventional.

17. The method according to claim 16, characterized in that the treatment is carried out in circular systems at a high speed such as the machines of dyeing by overflow to jet (jet dye), hoists and boats.

18. The method according to claim 16, characterized in that the treatment is carried out in a J-chamber, on a pad-roll or in a pad bath during a two-step biopolishing process.