TR201909896T4 - Changing color in textiles. - Google Patents

Abstract

The invention discloses the use of a peroxidase, a hydrogen peroxide source, and a vehicle for producing a color change in textile.

Description

DESCRIPTION COLOR CHANGE IN TEXTILE Assigned to Series List This reference contains a Sequence List in computer readable form.

Field of Invention The present invention is used in textiles, especially in dyed cellulosic fabric such as denim, a peroxidase a process to provide a modified color with a source of hydrogen peroxide and a vehicle It is related to.

BACKGROUND OF THE INVENTION The use of enzymes to process textiles is now well known. Amylases are produced is used for stripping and cellulases are used for etching. Laccases or Enzymes such as perhydrolase are also used in the processing of textiles by harsh chemical bleaching. It is applied instead for color changing.

In WC 96/ 12852, a bleached appearance of the dyed fabric surface in color intensity A phenol oxidizing enzyme system, in an aqueous medium of a dyed fabric, to provide e.g. contacting a lactase and an enhancing agent (mediator) together with oxygen A transaction is described.

WO 99/34054 describes a method comprising at least one peroxidase, an oxidase agent, and at least one vehicle. rinse water, For example, a peroxidase, hydrogen peroxide and a substance such as 1-hydroxy-benzotriazole A process for removing excess dye from fabric dyed with a liquid containing the agent is explained. Compositions and methods for color changing are described.

In WO 01/48304, excess disperse dye from printed or dyed textile material enzyme that exhibits at least one peroxidase activity or laccase activity for removal, a rinse containing an oxidizing agent and at least one vehicle a transaction is described.

In DE 19821263 an oxidation catalyst, an oxidizer, for the treatment of textile fabrics and an enzymatic bleach with enzyme-enhancing compounds containing a designated vehicle system is explained.

DESCRIPTION COLOR CHANGE IN TEXTILE Assigned to Series List This reference contains a Sequence List in computer readable form.

Field of Invention The present invention is used in textiles, especially in dyed cellulosic fabric such as denim, a peroxidase a process to provide a modified color with a source of hydrogen peroxide and a vehicle It is related to.

BACKGROUND OF THE INVENTION The use of enzymes to process textiles is now well known. Amylases are produced is used for stripping and cellulases are used for etching. Laccases or Enzymes such as perhydrolase are also used in the processing of textiles by harsh chemical bleaching. It is applied instead for color changing.

In WC 96/ 12852, a bleached appearance of the dyed fabric surface in color intensity A phenol oxidizing enzyme system, in an aqueous medium of a dyed fabric, to provide e.g. contacting a lactase and an enhancing agent (mediator) together with oxygen A transaction is described.

WO 99/34054 describes a method comprising at least one peroxidase, an oxidase agent, and at least one vehicle. rinse water, For example, a peroxidase, hydrogen peroxide and a substance such as 1-hydroxy-benzotriazole A process for removing excess dye from fabric dyed with a liquid containing the agent is explained. Compositions and methods for color changing are described.

In WO 01/48304, excess disperse dye from printed or dyed textile material enzyme that exhibits at least one peroxidase activity or laccase activity for removal, a rinse containing an oxidizing agent and at least one vehicle a transaction is described.

In DE 19821263 an oxidation catalyst, an oxidizer, for the treatment of textile fabrics and an enzymatic bleach with enzyme-enhancing compounds containing a designated vehicle system is explained.

DESCRIPTION COLOR CHANGE IN TEXTILE Assigned to Series List This reference contains a Sequence List in computer readable form.

Field of Invention The present invention is used in textiles, especially in dyed cellulosic fabric such as denim, a peroxidase a process to provide a modified color with a source of hydrogen peroxide and a vehicle It is related to.

BACKGROUND OF THE INVENTION The use of enzymes to process textiles is now well known. Amylases are produced is used for stripping and cellulases are used for etching. Laccases or Enzymes such as perhydrolase are also used in the processing of textiles by harsh chemical bleaching. It is applied instead for color changing.

In WC 96/ 12852, a bleached appearance of the dyed fabric surface in color intensity A phenol oxidizing enzyme system, in an aqueous medium of a dyed fabric, to provide e.g. contacting a lactase and an enhancing agent (mediator) together with oxygen A transaction is described.

WO 99/34054 describes a method comprising at least one peroxidase, an oxidase agent, and at least one vehicle. rinse water, For example, a peroxidase, hydrogen peroxide and a substance such as 1-hydroxy-benzotriazole A process for removing excess dye from fabric dyed with a liquid containing the agent is explained. Compositions and methods for color changing are described.

In WO 01/48304, excess disperse dye from printed or dyed textile material enzyme that exhibits at least one peroxidase activity or laccase activity for removal, a rinse containing an oxidizing agent and at least one vehicle a transaction is described.

In DE 19821263 an oxidation catalyst, an oxidizer, for the treatment of textile fabrics and an enzymatic bleach with enzyme-enhancing compounds containing a designated vehicle system is explained. laccase containing 4-carboxamido and 4-cyanO derivatives of 2,6-dimethoxyphenol, which can be used agents are described.

In DE 19723912, dyed cellulosic fiber products such as textiles a process for bleaching using oxidoreductase, a suitable oxidizing agent and a vehicle is described, wherein the intermediate is aliphatic, cycloaliphatic, heterocyclic or aromatic NO or NOH selected from the compounds.

Summary of the Invention The present invention is the use of a textile product to change the color of dyed textiles. exhibiting peroxidase activity covered by enzyme classification class EC 1.11.1.7 a peroxidase, a source of hydrogen peroxide, and violuric acid or a salt or hydrate thereof relates to a method comprising contacting a vehicle with

The method according to the present invention causes a color change in the textile product. color change selected from at least one of the following effects: lightening color, changing color, color change in dominance, reduction of rebonding/back-staining, and bleaching.

In some embodiments, methods for treating the textile product in an aqueous solution are provided. includes: (a) contacting the textile product with cellulase to acidify the textile product; (b) To change the color of the textile product, a peroxidase, a hydrogen peroxide contacting the source and a vehicle. In some embodiments, there is a gap between step (a) and (b). There is a washing phase. In some embodiments, (a) and (b) a single wash without intermediate wash stages. performed in the bathroom. In some embodiments, (a) and (b) take turns in the same bathroom or is performed simultaneously. In some embodiments, (a) and (b) alternate in a single bath. is performed, where (a) is performed before (b).

In some embodiments, step (a) is followed by an enzymatic generation step. Some In embodiments, the enzymatic descaling step is in the same bath as step (a). realizable. In some embodiments, the enzymatic descaling step is combined with steps (a) and (b). performed sequentially or simultaneously in the same bath. In some regulations, The enzymatic degeneration step is carried out in the same bath as steps (a) and (b), sequentially, wherein the sequence of the steps is enzymatic removal, steps (a) and (b). Some In embodiments, the enzymatic descaling step is performed in a bath, followed by a bath stage and stages (a) and (b) are performed in the same bathroom. laccase containing 4-carboxamido and 4-cyanO derivatives of 2,6-dimethoxyphenol, which can be used agents are described.

In DE 19723912, dyed cellulosic fiber products such as textiles a process for bleaching using oxidoreductase, a suitable oxidizing agent and a vehicle is described, wherein the intermediate is aliphatic, cycloaliphatic, heterocyclic or aromatic NO or NOH selected from the compounds.

Summary of the Invention The present invention is the use of a textile product to change the color of dyed textiles. exhibiting peroxidase activity covered by enzyme classification class EC 1.11.1.7 a peroxidase, a source of hydrogen peroxide, and violuric acid or a salt or hydrate thereof relates to a method comprising contacting a vehicle with

The method according to the present invention causes a color change in the textile product. color change selected from at least one of the following effects: lightening color, changing color, color change in dominance, reduction of rebonding/back-staining, and bleaching.

In some embodiments, methods for treating the textile product in an aqueous solution are provided. includes: (a) contacting the textile product with cellulase to acidify the textile product; (b) To change the color of the textile product, a peroxidase, a hydrogen peroxide contacting the source and a vehicle. In some embodiments, there is a gap between step (a) and (b). There is a washing phase. In some embodiments, (a) and (b) a single wash without intermediate wash stages. performed in the bathroom. In some embodiments, (a) and (b) take turns in the same bathroom or is performed simultaneously. In some embodiments, (a) and (b) alternate in a single bath. is performed, where (a) is performed before (b).

In some embodiments, step (a) is followed by an enzymatic generation step. Some In embodiments, the enzymatic descaling step is in the same bath as step (a). realizable. In some embodiments, the enzymatic descaling step is combined with steps (a) and (b). performed sequentially or simultaneously in the same bath. In some regulations, The enzymatic degeneration step is carried out in the same bath as steps (a) and (b), sequentially, wherein the sequence of the steps is enzymatic removal, steps (a) and (b). Some In embodiments, the enzymatic descaling step is performed in a bath, followed by a bath stage and stages (a) and (b) are performed in the same bathroom. laccase containing 4-carboxamido and 4-cyanO derivatives of 2,6-dimethoxyphenol, which can be used agents are described.

In DE 19723912, dyed cellulosic fiber products such as textiles a process for bleaching using oxidoreductase, a suitable oxidizing agent and a vehicle is described, wherein the intermediate is aliphatic, cycloaliphatic, heterocyclic or aromatic NO or NOH selected from the compounds.

Summary of the Invention The present invention is the use of a textile product to change the color of dyed textiles. exhibiting peroxidase activity covered by enzyme classification class EC 1.11.1.7 a peroxidase, a source of hydrogen peroxide, and violuric acid or a salt or hydrate thereof relates to a method comprising contacting a vehicle with

The method according to the present invention causes a color change in the textile product. color change selected from at least one of the following effects: lightening color, changing color, color change in dominance, reduction of rebonding/back-staining, and bleaching.

In some embodiments, methods for treating the textile product in an aqueous solution are provided. includes: (a) contacting the textile product with cellulase to acidify the textile product; (b) To change the color of the textile product, a peroxidase, a hydrogen peroxide contacting the source and a vehicle. In some embodiments, there is a gap between step (a) and (b). There is a washing phase. In some embodiments, (a) and (b) a single wash without intermediate wash stages. performed in the bathroom. In some embodiments, (a) and (b) take turns in the same bathroom or is performed simultaneously. In some embodiments, (a) and (b) alternate in a single bath. is performed, where (a) is performed before (b).

In some embodiments, step (a) is followed by an enzymatic generation step. Some In embodiments, the enzymatic descaling step is in the same bath as step (a). realizable. In some embodiments, the enzymatic descaling step is combined with steps (a) and (b). performed sequentially or simultaneously in the same bath. In some regulations, The enzymatic degeneration step is carried out in the same bath as steps (a) and (b), sequentially, wherein the sequence of the steps is enzymatic removal, steps (a) and (b). Some In embodiments, the enzymatic descaling step is performed in a bath, followed by a bath stage and stages (a) and (b) are performed in the same bathroom.

In some embodiments, the peroxidase enzyme is a Coprinus cinereus peroxidase or a soybean bean peroxidasia.

In some embodiments, the textile product is a dyed textile product. In some regulations, dyed textile product is dyed fabric. In some embodiments, the dyed textile product it is denim. In some embodiments, the dye is an indigo dye. In some embodiments, the dye is sulfur is paint.

In some embodiments, the textile product processing method is the textile product production method.

In some embodiments, the method or compound according to the present invention is on the front of the textile product. provides color change.

DETAILED DESCRIPTION OF THE INVENTION The expression "one" in the singular form used here is clearly the opposite in the context in which it is used. includes plural forms, unless specified. Thus, for example, references to "a peroxidase" are or more peroxidase use. "One step" of a procedure is at least one step means and there may be one, two, three, four, five or even more procedural stages.

The term "in order" as used herein in reference to more than one enzymatic process in a textile product, after a specified second enzymatic treatment has been performed then it means it's done. Sequential processes can be separated by intermediate washing stages.

As used herein, the phrase that sequential enzymatic processes can be performed in the "same bath", intermediate means largely in the same liquid medium without washing steps. one-bath sequential process pH adjustments, temperature adjustment and/or salts, activators, agent may include the addition of substances and the like, but should not include washing or rinsing.

The term "simultaneous" refers to more than one enzymatic process in a textile product. The term means that a second enzymatic treatment specified is the same as a first specified enzymatic treatment. It means that it takes place over time (that is, in at least partially overlapping ways).

Simultaneous enzymatic processes are not necessarily "in the same bath" without intermediate washing steps. is performed.

Peroxidase Enzymes EC-numbers can be used to classify enzymes. Recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology, Reference is made to Academic Press Inc., 1992.

In some embodiments, the peroxidase enzyme is a Coprinus cinereus peroxidase or a soybean bean peroxidasia.

In some embodiments, the textile product is a dyed textile product. In some regulations, dyed textile product is dyed fabric. In some embodiments, the dyed textile product it is denim. In some embodiments, the dye is an indigo dye. In some embodiments, the dye is sulfur is paint.

In some embodiments, the textile product processing method is the textile product production method.

In some embodiments, the method or compound according to the present invention is on the front of the textile product. provides color change.

DETAILED DESCRIPTION OF THE INVENTION The expression "one" in the singular form used here is clearly the opposite in the context in which it is used. includes plural forms, unless specified. Thus, for example, references to "a peroxidase" are or more peroxidase use. "One step" of a procedure is at least one step means and there may be one, two, three, four, five or even more procedural stages.

The term "in order" as used herein in reference to more than one enzymatic process in a textile product, after a specified second enzymatic treatment has been performed then it means it's done. Sequential processes can be separated by intermediate washing stages.

As used herein, the phrase that sequential enzymatic processes can be performed in the "same bath", intermediate means largely in the same liquid medium without washing steps. one-bath sequential process pH adjustments, temperature adjustment and/or salts, activators, agent may include the addition of substances and the like, but should not include washing or rinsing.

The term "simultaneous" refers to more than one enzymatic process in a textile product. The term means that a second enzymatic treatment specified is the same as a first specified enzymatic treatment. It means that it takes place over time (that is, in at least partially overlapping ways).

Simultaneous enzymatic processes are not necessarily "in the same bath" without intermediate washing steps. is performed.

Peroxidase Enzymes EC-numbers can be used to classify enzymes. Recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology, Reference is made to Academic Press Inc., 1992.

In some embodiments, the peroxidase enzyme is a Coprinus cinereus peroxidase or a soybean bean peroxidasia.

In some embodiments, the textile product is a dyed textile product. In some regulations, dyed textile product is dyed fabric. In some embodiments, the dyed textile product it is denim. In some embodiments, the dye is an indigo dye. In some embodiments, the dye is sulfur is paint.

In some embodiments, the textile product processing method is the textile product production method.

In some embodiments, the method or compound according to the present invention is on the front of the textile product. provides color change.

DETAILED DESCRIPTION OF THE INVENTION The expression "one" in the singular form used here is clearly the opposite in the context in which it is used. includes plural forms, unless specified. Thus, for example, references to "a peroxidase" are or more peroxidase use. "One step" of a procedure is at least one step means and there may be one, two, three, four, five or even more procedural stages.

The term "in order" as used herein in reference to more than one enzymatic process in a textile product, after a specified second enzymatic treatment has been performed then it means it's done. Sequential processes can be separated by intermediate washing stages.

As used herein, the phrase that sequential enzymatic processes can be performed in the "same bath", intermediate means largely in the same liquid medium without washing steps. one-bath sequential process pH adjustments, temperature adjustment and/or salts, activators, agent may include the addition of substances and the like, but should not include washing or rinsing.

The term "simultaneous" refers to more than one enzymatic process in a textile product. The term means that a second enzymatic treatment specified is the same as a first specified enzymatic treatment. It means that it takes place over time (that is, in at least partially overlapping ways).

Simultaneous enzymatic processes are not necessarily "in the same bath" without intermediate washing steps. is performed.

Peroxidase Enzymes EC-numbers can be used to classify enzymes. Recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology, Reference is made to Academic Press Inc., 1992.

As will be understood, besides the term enzyme, the various enzymes and enzymes mentioned herein classes of natural-type enzymes, as well as any type thereof that preserves the activity in question. covers the variant. Such variants can be produced by recombinant techniques. Natural type enzymes also by recombinant techniques or by isolation and purification from natural source. can be produced. In a particular embodiment, the enzyme in question is well defined, ie only one major enzyme component available. This can for example be understood by separating on a suitable size separation column. this type well-defined or purified or highly pure enzyme as known in the art and/or as described in publications related to the particular enzyme in question.

A peroxidase enzyme classification according to the invention is one covered by EC 1.11.1.7. peroxidase enzyme or any derivative thereof that exhibits peroxidase activity is the fragment.

Preferably, the peroxidase of the invention is a plant peroxidase, eg soybean peroxidase. (see SEQ ID No: 2) or a fungal or bacterial peroxidase.

Some preferred fungi include strains belonging to: subsection Deuteromycotina, class Hyphomycetes, eg, Fusarium, Humicola, Tricoderma, Myrothecium, Verticillum, Arthromyces, Caldariomyces, UIocIadium, Embellisia, Cladosporium or Dreschlera, especially Fusarium oxysporum (DSM 2672), Humicola insolens, Trichoderma reesei, Myrothecium verrucaria (IFO 6113), Verticillum alboatrum, Verticillum dahlie, Arthromyces ramosus (FERM P-7754), Caldariomyces fumago, Ulocladium chartarum, Embellisia aIli or Dreschlera halodes.

Other preferred fungi include strains belonging to: subsection Basidiomycotina, class Basidiomycetes, eg Coprinus, Phanerochaete, Coriolus or Trametes, especially Coprinus cinereus f. microsporus (IFO 8371), Coprinus macrorhizus, Phanerochaete chrysosporium (eg NA-12) or Trametes (formerly Polyporus), eg T. versicolor (eg PR4 28-A).

Other preferred fungi include strains belonging to: subsection Zygomycotina, class Mycoraceae, eg, Rhizopus or Mucor, especially Mucor hiemalis.

Some preferred bacteria include strains of: order Actinomycetales, e.g.

Streptomyces spheroides (ATTC or Streptoverticillium verticillium subspecies verticillium.

As will be understood, besides the term enzyme, the various enzymes and enzymes mentioned herein classes of natural-type enzymes, as well as any type thereof that preserves the activity in question. covers the variant. Such variants can be produced by recombinant techniques. Natural type enzymes also by recombinant techniques or by isolation and purification from natural source. can be produced. In a particular embodiment, the enzyme in question is well defined, ie only one major enzyme component available. This can for example be understood by separating on a suitable size separation column. this type well-defined or purified or highly pure enzyme as known in the art and/or as described in publications related to the particular enzyme in question.

A peroxidase enzyme classification according to the invention is one covered by EC 1.11.1.7. peroxidase enzyme or any derivative thereof that exhibits peroxidase activity is the fragment.

Preferably, the peroxidase of the invention is a plant peroxidase, eg soybean peroxidase. (see SEQ ID No: 2) or a fungal or bacterial peroxidase.

Some preferred fungi include strains belonging to: subsection Deuteromycotina, class Hyphomycetes, eg, Fusarium, Humicola, Tricoderma, Myrothecium, Verticillum, Arthromyces, Caldariomyces, UIocIadium, Embellisia, Cladosporium or Dreschlera, especially Fusarium oxysporum (DSM 2672), Humicola insolens, Trichoderma reesei, Myrothecium verrucaria (IFO 6113), Verticillum alboatrum, Verticillum dahlie, Arthromyces ramosus (FERM P-7754), Caldariomyces fumago, Ulocladium chartarum, Embellisia aIli or Dreschlera halodes.

Other preferred fungi include strains belonging to: subsection Basidiomycotina, class Basidiomycetes, eg Coprinus, Phanerochaete, Coriolus or Trametes, especially Coprinus cinereus f. microsporus (IFO 8371), Coprinus macrorhizus, Phanerochaete chrysosporium (eg NA-12) or Trametes (formerly Polyporus), eg T. versicolor (eg PR4 28-A).

Other preferred fungi include strains belonging to: subsection Zygomycotina, class Mycoraceae, eg, Rhizopus or Mucor, especially Mucor hiemalis.

Some preferred bacteria include strains of: order Actinomycetales, e.g.

Streptomyces spheroides (ATTC or Streptoverticillium verticillium subspecies verticillium.

As will be understood, besides the term enzyme, the various enzymes and enzymes mentioned herein classes of natural-type enzymes, as well as any type thereof that preserves the activity in question. covers the variant. Such variants can be produced by recombinant techniques. Natural type enzymes also by recombinant techniques or by isolation and purification from natural source. can be produced. In a particular embodiment, the enzyme in question is well defined, ie only one major enzyme component available. This can for example be understood by separating on a suitable size separation column. this type well-defined or purified or highly pure enzyme as known in the art and/or as described in publications related to the particular enzyme in question.

A peroxidase enzyme classification according to the invention is one covered by EC 1.11.1.7. peroxidase enzyme or any derivative thereof that exhibits peroxidase activity is the fragment.

Preferably, the peroxidase of the invention is a plant peroxidase, eg soybean peroxidase. (see SEQ ID No: 2) or a fungal or bacterial peroxidase.

Some preferred fungi include strains belonging to: subsection Deuteromycotina, class Hyphomycetes, eg, Fusarium, Humicola, Tricoderma, Myrothecium, Verticillum, Arthromyces, Caldariomyces, UIocIadium, Embellisia, Cladosporium or Dreschlera, especially Fusarium oxysporum (DSM 2672), Humicola insolens, Trichoderma reesei, Myrothecium verrucaria (IFO 6113), Verticillum alboatrum, Verticillum dahlie, Arthromyces ramosus (FERM P-7754), Caldariomyces fumago, Ulocladium chartarum, Embellisia aIli or Dreschlera halodes.

Other preferred fungi include strains belonging to: subsection Basidiomycotina, class Basidiomycetes, eg Coprinus, Phanerochaete, Coriolus or Trametes, especially Coprinus cinereus f. microsporus (IFO 8371), Coprinus macrorhizus, Phanerochaete chrysosporium (eg NA-12) or Trametes (formerly Polyporus), eg T. versicolor (eg PR4 28-A).

Other preferred fungi include strains belonging to: subsection Zygomycotina, class Mycoraceae, eg, Rhizopus or Mucor, especially Mucor hiemalis.

Some preferred bacteria include strains of: order Actinomycetales, e.g.

Streptomyces spheroides (ATTC or Streptoverticillium verticillium subspecies verticillium.

Other preferred bacteria include: Rhodobacter sphaeroides, Rhodomonas palustri, Streptococcus Iactis, Pseudomonas purrocinia (ATCC 15958), Pseudomonas stearothermophilus

Other preferred bacteria are strains of Myxococcus, eg M. virescens. are included.

Peroxidase also contains a DNA sequence encoding said peroxidase, as well as peroxidase. DNA sequences that encode functions that enable expression of the encoding DNA sequence of a host cell transformed with a recombinant DNA vector carrying peroxidazine. cultured in a culture medium under conditions enabling its expression and a peroxidase produced by a method comprising harvesting the peroxidase from culture. In particular, a peroxidase according to the present invention is a species of Coprinus (as Coprinopsis species). also mentioned) is a peroxidase derived specifically from C. macrorhizus or C. cinereus (see Ex. SEQ 1D NO: 1).

In a preferred embodiment, the peroxidase in the methods and compositions of the invention One or more of the polypeptide of SEQ 1D NO:1 or 2 or a homologous sequence thereof an amino acid containing a substitution, deletion and/or addition in (or more) of its amino acids sequence contains or consists of such an amino acid sequence. Preferably, the homologous sequence SEQ ID N02] or at least 80% identical to SEQ ID NO:2, ie at least 85% identical, at least 90% identical or at least 95% identical.

For the purposes of the present invention, sequence identity between two amino acid sequences degree EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Needleman-Wunsch algorithm implemented with the Needle program (Needleman and Wunsch, gap open penalty 10 and gap extension penalty 0.5 and EBLOSUM62 (EMBOSS version BLOSUM62) is the substitution matrix. Needle output labeled "longest identity" (-n0brief option) is used as a percent identity and is calculated as: (Identical Remains x 100)/(Length of Alignment - Total Number of Spaces in Alignment) For the purposes of the present invention, the sequence between two deoxyribonucleotide sequences degree of identity EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, supra), preferably Needle version 3.0.0 or later Needleman-Wunsch algorithm implemented with the program (Needleman and Wunsch, 1970, Other preferred bacteria include: Rhodobacter sphaeroides, Rhodomonas palustri, Streptococcus Iactis, Pseudomonas purrocinia (ATCC 15958), Pseudomonas stearothermophilus

Other preferred bacteria are strains of Myxococcus, eg M. virescens. are included.

Peroxidase also contains a DNA sequence encoding said peroxidase, as well as peroxidase. DNA sequences that encode functions that enable expression of the encoding DNA sequence of a host cell transformed with a recombinant DNA vector carrying peroxidazine. cultured in a culture medium under conditions enabling its expression and a peroxidase produced by a method comprising harvesting the peroxidase from culture. In particular, a peroxidase according to the present invention is a species of Coprinus (as Coprinopsis species). also mentioned) is a peroxidase derived specifically from C. macrorhizus or C. cinereus (see Ex. SEQ 1D NO: 1).

In a preferred embodiment, the peroxidase in the methods and compositions of the invention One or more of the polypeptide of SEQ 1D NO:1 or 2 or a homologous sequence thereof an amino acid containing a substitution, deletion and/or addition in (or more) of its amino acids sequence contains or consists of such an amino acid sequence. Preferably, the homologous sequence SEQ ID N02] or at least 80% identical to SEQ ID NO:2, ie at least 85% identical, at least 90% identical or at least 95% identical.

For the purposes of the present invention, sequence identity between two amino acid sequences degree EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Needleman-Wunsch algorithm implemented with the Needle program (Needleman and Wunsch, gap open penalty 10 and gap extension penalty 0.5 and EBLOSUM62 (EMBOSS version BLOSUM62) is the substitution matrix. Needle output labeled "longest identity" (-n0brief option) is used as a percent identity and is calculated as: (Identical Remains x 100)/(Length of Alignment - Total Number of Spaces in Alignment) For the purposes of the present invention, the sequence between two deoxyribonucleotide sequences degree of identity EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, supra), preferably Needle version 3.0.0 or later Needleman-Wunsch algorithm implemented with the program (Needleman and Wunsch, 1970, Other preferred bacteria include: Rhodobacter sphaeroides, Rhodomonas palustri, Streptococcus Iactis, Pseudomonas purrocinia (ATCC 15958), Pseudomonas stearothermophilus

Other preferred bacteria are strains of Myxococcus, eg M. virescens. are included.

Peroxidase also contains a DNA sequence encoding said peroxidase, as well as peroxidase. DNA sequences that encode functions that enable expression of the encoding DNA sequence of a host cell transformed with a recombinant DNA vector carrying peroxidazine. cultured in a culture medium under conditions enabling its expression and a peroxidase produced by a method comprising harvesting the peroxidase from culture. In particular, a peroxidase according to the present invention is a species of Coprinus (as Coprinopsis species). also mentioned) is a peroxidase derived specifically from C. macrorhizus or C. cinereus (see Ex. SEQ 1D NO: 1).

In a preferred embodiment, the peroxidase in the methods and compositions of the invention One or more of the polypeptide of SEQ 1D NO:1 or 2 or a homologous sequence thereof an amino acid containing a substitution, deletion and/or addition in (or more) of its amino acids sequence contains or consists of such an amino acid sequence. Preferably, the homologous sequence SEQ ID N02] or at least 80% identical to SEQ ID NO:2, ie at least 85% identical, at least 90% identical or at least 95% identical.

For the purposes of the present invention, sequence identity between two amino acid sequences degree EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Needleman-Wunsch algorithm implemented with the Needle program (Needleman and Wunsch, gap open penalty 10 and gap extension penalty 0.5 and EBLOSUM62 (EMBOSS version BLOSUM62) is the substitution matrix. Needle output labeled "longest identity" (-n0brief option) is used as a percent identity and is calculated as: (Identical Remains x 100)/(Length of Alignment - Total Number of Spaces in Alignment) For the purposes of the present invention, the sequence between two deoxyribonucleotide sequences degree of identity EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, supra), preferably Needle version 3.0.0 or later Needleman-Wunsch algorithm implemented with the program (Needleman and Wunsch, 1970, above). Optional parameters used are gap open penalty 10 and space extension penal substitution is the matrix. Needle output labeled "longest identity" (obtained with the -nobrief option) It is used as a percent identity and is calculated as: (Identical Deoxyribonucleotides x 100)/(Length of Alignment - Total Number of Gaps in Alignment) In the present invention, the polypeptide in the peroxidase polypeptide sequence SEQ ID NO:1 or 2 or one or more (or more) amino acids of a homologous sequence thereof There may be variants with substitutions, deletions and/or additions. Preferably, the amino acid changes (i.e. substitution, deletion of one or more (or more) amino acids) and splicing) in the small type, i.e. significantly affecting the folding and/or activity of the protein. conservative amino acid substitutions or additions that do not affect; typically one to about small deletions of amino acids; small amino- or carboxy-terminal extensions; a small binding peptide of up to about 20-25 residues; or its net charge, such as a poly-histidine system, an antigenic epitope, or a binding domain, or is a small extension that makes purification easier by modifying another function.

Examples of conservative substitutions are basic amino acids (arginine, Iizine and histidine), acidic amino acids (glutamic acid and aspartic acid), polar amino acids (glutamine and asparagine), hydrophobic amino acids (leucine, isoleucine and valine), aromatic amino acids (phenylalanine, tryptophan and tyrosine) and small amino acids (glycine, alanine, serine, threonine and methionine) group is in it. Amino acid substitutions that do not generally alter the original activity are still available in the art. known and, for example, H. Neurath and R.L. Hill, 1979, The Proteins, Academic Press, New Described in York. The most common changes are: Ala/Ser, Val/Ile, Asp/Glu, Thr/Ser, Ala/Gly, Ala/Thr, Ser/Asu, Ala/Val, Ser/Gly, Tyr/Phe, Ala/Pro, Lys/Arg, Asp/Asn, Leu/Ile, Leu/Val, Ala/Glu and Asp/Gly.

Essential amino acids in a parent polypeptide site-directed inutagenesis or alanine-scan can be determined according to procedures known in the art, such as mutagenesis (Cunningham and Wells, mutations are applied and the endoglucanase activity of the resulting mutant molecules is tested. The amino acid residues that are important for the activity of the molecule are determined. See. Also, Hilton et al., also nuclear magnetic with mutation in the putative contact site amino acids by techniques such as resonance, crystallography, electron diffraction or photoaffinity marking. above). Optional parameters used are gap open penalty 10 and space extension penal substitution is the matrix. Needle output labeled "longest identity" (obtained with the -nobrief option) It is used as a percent identity and is calculated as: (Identical Deoxyribonucleotides x 100)/(Length of Alignment - Total Number of Gaps in Alignment) In the present invention, the polypeptide in the peroxidase polypeptide sequence SEQ ID NO:1 or 2 or one or more (or more) amino acids of a homologous sequence thereof There may be variants with substitutions, deletions and/or additions. Preferably, the amino acid changes (i.e. substitution, deletion of one or more (or more) amino acids) and splicing) in the small type, i.e. significantly affecting the folding and/or activity of the protein. conservative amino acid substitutions or additions that do not affect; typically one to about small deletions of amino acids; small amino- or carboxy-terminal extensions; a small binding peptide of up to about 20-25 residues; or its net charge, such as a poly-histidine system, an antigenic epitope, or a binding domain, or is a small extension that makes purification easier by modifying another function.

Examples of conservative substitutions are basic amino acids (arginine, Iizine and histidine), acidic amino acids (glutamic acid and aspartic acid), polar amino acids (glutamine and asparagine), hydrophobic amino acids (leucine, isoleucine and valine), aromatic amino acids (phenylalanine, tryptophan and tyrosine) and small amino acids (glycine, alanine, serine, threonine and methionine) group is in it. Amino acid substitutions that do not generally alter the original activity are still available in the art. known and, for example, H. Neurath and R.L. Hill, 1979, The Proteins, Academic Press, New Described in York. The most common changes are: Ala/Ser, Val/Ile, Asp/Glu, Thr/Ser, Ala/Gly, Ala/Thr, Ser/Asu, Ala/Val, Ser/Gly, Tyr/Phe, Ala/Pro, Lys/Arg, Asp/Asn, Leu/Ile, Leu/Val, Ala/Glu and Asp/Gly.

Essential amino acids in a parent polypeptide site-directed inutagenesis or alanine-scan can be determined according to procedures known in the art, such as mutagenesis (Cunningham and Wells, mutations are applied and the endoglucanase activity of the resulting mutant molecules is tested. The amino acid residues that are important for the activity of the molecule are determined. See. Also, Hilton et al., also nuclear magnetic with mutation in the putative contact site amino acids by techniques such as resonance, crystallography, electron diffraction or photoaffinity marking. above). Optional parameters used are gap open penalty 10 and space extension penal substitution is the matrix. Needle output labeled "longest identity" (obtained with the -nobrief option) It is used as a percent identity and is calculated as: (Identical Deoxyribonucleotides x 100)/(Length of Alignment - Total Number of Gaps in Alignment) In the present invention, the polypeptide in the peroxidase polypeptide sequence SEQ ID NO:1 or 2 or one or more (or more) amino acids of a homologous sequence thereof There may be variants with substitutions, deletions and/or additions. Preferably, the amino acid changes (i.e. substitution, deletion of one or more (or more) amino acids) and splicing) in the small type, i.e. significantly affecting the folding and/or activity of the protein. conservative amino acid substitutions or additions that do not affect; typically one to about small deletions of amino acids; small amino- or carboxy-terminal extensions; a small binding peptide of up to about 20-25 residues; or its net charge, such as a poly-histidine system, an antigenic epitope, or a binding domain, or is a small extension that makes purification easier by modifying another function.

Examples of conservative substitutions are basic amino acids (arginine, Iizine and histidine), acidic amino acids (glutamic acid and aspartic acid), polar amino acids (glutamine and asparagine), hydrophobic amino acids (leucine, isoleucine and valine), aromatic amino acids (phenylalanine, tryptophan and tyrosine) and small amino acids (glycine, alanine, serine, threonine and methionine) group is in it. Amino acid substitutions that do not generally alter the original activity are still available in the art. known and, for example, H. Neurath and R.L. Hill, 1979, The Proteins, Academic Press, New Described in York. The most common changes are: Ala/Ser, Val/Ile, Asp/Glu, Thr/Ser, Ala/Gly, Ala/Thr, Ser/Asu, Ala/Val, Ser/Gly, Tyr/Phe, Ala/Pro, Lys/Arg, Asp/Asn, Leu/Ile, Leu/Val, Ala/Glu and Asp/Gly.

Essential amino acids in a parent polypeptide site-directed inutagenesis or alanine-scan can be determined according to procedures known in the art, such as mutagenesis (Cunningham and Wells, mutations are applied and the endoglucanase activity of the resulting mutant molecules is tested. The amino acid residues that are important for the activity of the molecule are determined. See. Also, Hilton et al., also nuclear magnetic with mutation in the putative contact site amino acids by techniques such as resonance, crystallography, electron diffraction or photoaffinity marking. It can also be determined by the physical structure analysis determined. See, for example, de Vos et al., 1992, Science 309259-64. The identities of important amino acids are also associated with the parent polypeptide. It can also be deduced from analysis of identities with polypeptides.

Known methods of inutagenesis, recombination and/or mixing followed by Reidhaar-Olson Single or multiple amino acid substitutions, deletions and/or additions using can be made and tested. Other available methods include error-prone PCR, phage display DNA 7:127).

Cloned, mutagenized polypeptides expressed by host cells high-throughput, automated screening of mutagenesis/shuffling methods to detect activity mutagenized DNA molecules encoding polypeptides can be harvested from host cells and Sequence determination can be made quickly using standard techniques in the art. These methods are a to quickly determine the importance of individual amino acid residues in the polypeptide. Allows.

Preferably, amino acid substitutions, deletions in the polypeptide of SEQ ID NO: 1 or 2. Polypeptide is the N-terminus of a portion of one polypeptide and a portion of another polypeptide. or a hybrid polypeptide attached to the C-terminus.

The polypeptide may also be attached to the N-terminus or C-terminus of another polypeptide of the invention. It may also be a fused polypeptide to which it is fused or a cleavable fusion polypeptide.

A fused polypeptide is a polypeptide of another polypeptide in a polynucleotide of the present invention. It is produced by joining a coding polynucleotide. Generating fusion polypeptides techniques are known in the art and include coding sequences encoding polypeptides. as in-frame and the same promoter(s) of expression of the combined polypeptide and connecting the finisher so that it is under its control. Fusion proteins also using intein technology, where fusions are created post-translationally It can also be determined by the physical structure analysis determined. See, for example, de Vos et al., 1992, Science 309259-64. The identities of important amino acids are also associated with the parent polypeptide. It can also be deduced from analysis of identities with polypeptides.

Known methods of inutagenesis, recombination and/or mixing followed by Reidhaar-Olson Single or multiple amino acid substitutions, deletions and/or additions using can be made and tested. Other available methods include error-prone PCR, phage display DNA 7:127).

Cloned, mutagenized polypeptides expressed by host cells high-throughput, automated screening of mutagenesis/shuffling methods to detect activity mutagenized DNA molecules encoding polypeptides can be harvested from host cells and Sequence determination can be made quickly using standard techniques in the art. These methods are a to quickly determine the importance of individual amino acid residues in the polypeptide. Allows.

Preferably, amino acid substitutions, deletions in the polypeptide of SEQ ID NO: 1 or 2. Polypeptide is the N-terminus of a portion of one polypeptide and a portion of another polypeptide. or a hybrid polypeptide attached to the C-terminus.

The polypeptide may also be attached to the N-terminus or C-terminus of another polypeptide of the invention. It may also be a fused polypeptide to which it is fused or a cleavable fusion polypeptide.

A fused polypeptide is a polypeptide of another polypeptide in a polynucleotide of the present invention. It is produced by joining a coding polynucleotide. Generating fusion polypeptides techniques are known in the art and include coding sequences encoding polypeptides. as in-frame and the same promoter(s) of expression of the combined polypeptide and connecting the finisher so that it is under its control. Fusion proteins also using intein technology, where fusions are created post-translationally It can also be determined by the physical structure analysis determined. See, for example, de Vos et al., 1992, Science 309259-64. The identities of important amino acids are also associated with the parent polypeptide. It can also be deduced from analysis of identities with polypeptides.

Known methods of inutagenesis, recombination and/or mixing followed by Reidhaar-Olson Single or multiple amino acid substitutions, deletions and/or additions using can be made and tested. Other available methods include error-prone PCR, phage display DNA 7:127).

Cloned, mutagenized polypeptides expressed by host cells high-throughput, automated screening of mutagenesis/shuffling methods to detect activity mutagenized DNA molecules encoding polypeptides can be harvested from host cells and Sequence determination can be made quickly using standard techniques in the art. These methods are a to quickly determine the importance of individual amino acid residues in the polypeptide. Allows.

Preferably, amino acid substitutions, deletions in the polypeptide of SEQ ID NO: 1 or 2. Polypeptide is the N-terminus of a portion of one polypeptide and a portion of another polypeptide. or a hybrid polypeptide attached to the C-terminus.

The polypeptide may also be attached to the N-terminus or C-terminus of another polypeptide of the invention. It may also be a fused polypeptide to which it is fused or a cleavable fusion polypeptide.

A fused polypeptide is a polypeptide of another polypeptide in a polynucleotide of the present invention. It is produced by joining a coding polynucleotide. Generating fusion polypeptides techniques are known in the art and include coding sequences encoding polypeptides. as in-frame and the same promoter(s) of expression of the combined polypeptide and connecting the finisher so that it is under its control. Fusion proteins also using intein technology, where fusions are created post-translationally 776-779).

A fusion polypeptide may also include a cleavage site between the two polypeptides. Fusion After the protein is secreted, the region is cleaved to reveal the two polypeptides. Fragmentation Examples of regions are, without limitation, Martin Vd., 2003, J. 1nd. microbiol. The regions described in 48 are included.

Hydrogen Peroxide Source Hydrogen peroxide required for compounds exhibiting peroxidase or peroxidase activity an aqueous hydrogen peroxide or hydrogen peroxide for the production of hydrogen peroxide at the source It can be supplied as a peroxide precursor solution. that can be used by peroxidase Any solids released by the dissolution of peroxide are a source of hydrogen peroxide. can serve as Hydrogen when dissolved in water or a suitable water-based medium metal peroxides, percarbonates, persulfates, perphosphates, peroxyacids, alkylperoxides, acylperoxides, peroxyesters, urea peroxide, ozone, perborates and peroxycarboxylic acids or salts thereof.

Another source of hydrogen peroxide is a hydrogen peroxide-forming enzyme system, for example It is an oxidase with a substrate for the oxidase. Oxidase and substrate combinations examples include, but are not limited to: amino acid oxidase (see eg US oxidase and lactate, galactose oxidase (see eg WO 00/50606) and galactose and aldose oxidase (see eg WO 99/31990) and a suitable aldose.

Under the Biochemistry Association), other such combinations of oxidases and substrates examples will be readily understood by those skilled in the art.

Intermediate Substance The mediators according to the invention serve as electron donors for the peroxidase. middleman The compounds according to the invention increase the electron transfer between the peroxidase and the textile product. 776-779).

A fusion polypeptide may also include a cleavage site between the two polypeptides. Fusion After the protein is secreted, the region is cleaved to reveal the two polypeptides. Fragmentation Examples of regions are, without limitation, Martin Vd., 2003, J. 1nd. microbiol. The regions described in 48 are included.

Hydrogen Peroxide Source Hydrogen peroxide required for compounds exhibiting peroxidase or peroxidase activity an aqueous hydrogen peroxide or hydrogen peroxide for the production of hydrogen peroxide at the source It can be supplied as a peroxide precursor solution. that can be used by peroxidase Any solids released by the dissolution of peroxide are a source of hydrogen peroxide. can serve as Hydrogen when dissolved in water or a suitable water-based medium metal peroxides, percarbonates, persulfates, perphosphates, peroxyacids, alkylperoxides, acylperoxides, peroxyesters, urea peroxide, ozone, perborates and peroxycarboxylic acids or salts thereof.

Another source of hydrogen peroxide is a hydrogen peroxide-forming enzyme system, for example It is an oxidase with a substrate for the oxidase. Oxidase and substrate combinations examples include, but are not limited to: amino acid oxidase (see eg US oxidase and lactate, galactose oxidase (see eg WO 00/50606) and galactose and aldose oxidase (see eg WO 99/31990) and a suitable aldose.

Under the Biochemistry Association), other such combinations of oxidases and substrates examples will be readily understood by those skilled in the art.

Intermediate Substance The mediators according to the invention serve as electron donors for the peroxidase. middleman The compounds according to the invention increase the electron transfer between the peroxidase and the textile product. 776-779).

A fusion polypeptide may also include a cleavage site between the two polypeptides. Fusion After the protein is secreted, the region is cleaved to reveal the two polypeptides. Fragmentation Examples of regions are, without limitation, Martin Vd., 2003, J. 1nd. microbiol. The regions described in 48 are included.

Hydrogen Peroxide Source Hydrogen peroxide required for compounds exhibiting peroxidase or peroxidase activity an aqueous hydrogen peroxide or hydrogen peroxide for the production of hydrogen peroxide at the source It can be supplied as a peroxide precursor solution. that can be used by peroxidase Any solids released by the dissolution of peroxide are a source of hydrogen peroxide. can serve as Hydrogen when dissolved in water or a suitable water-based medium metal peroxides, percarbonates, persulfates, perphosphates, peroxyacids, alkylperoxides, acylperoxides, peroxyesters, urea peroxide, ozone, perborates and peroxycarboxylic acids or salts thereof.

Another source of hydrogen peroxide is a hydrogen peroxide-forming enzyme system, for example It is an oxidase with a substrate for the oxidase. Oxidase and substrate combinations examples include, but are not limited to: amino acid oxidase (see eg US oxidase and lactate, galactose oxidase (see eg WO 00/50606) and galactose and aldose oxidase (see eg WO 99/31990) and a suitable aldose.

Under the Biochemistry Association), other such combinations of oxidases and substrates examples will be readily understood by those skilled in the art.

Intermediate Substance The mediators according to the invention serve as electron donors for the peroxidase. middleman The compounds according to the invention increase the electron transfer between the peroxidase and the textile product. increases the bleaching effects of the methods. A particularly preferred intermediate is alloxan-S-oxime (violuric acid) and/or salts thereof or hydrates.

Textile Product As used herein, the term "textile product" includes fibers, yarns, fabrics, garments and non-wovens. indicates products. The term is natural, synthetic (eg, manufactured) and various natural and synthetic It covers textile products made from blends. Textile products, unprocessed or processed fiber, yarn, woven or knitted fabric, non-woven products and clothing; and some can be made using the various materials mentioned here.

The process according to the invention is most suitable for fabrics containing cellulose, for example cotton, viscose, rayon, ramie, linen, Tencel or blends thereof, or any of these fibers blends of any of these fibers, such as cotton and spandex (stretch-denim) blends. It is applied to blends with synthetic fibers. In particular, the fabric is dyed fabric, preferably it is denim. Denim fabric indigo or indigo-related dyes, such as thioindigo It may be dyed with paints.

In the most preferred embodiment of the process according to the invention, the fabric is indigo-dyed denim. and clothing items made of them.

The process of producing textile products A fabric, for example a cellulosic material as ready-made material for the manufacture of clothing its processing involves several steps: spinning the fiber into a yarn; weaving or knitting from yarn making the fabric; and subsequent preparation, dyeing/printing and finishing operations.

The preparation processes are the removal of natural and man-made impurities from the fiber and For example, increasing their aesthetic appearance and workability before dyeing/printing and finishing required for Common preparation processes produce a fabric suitable for dyeing or finishing. Includes stripping (for woven products), rubbing and bleaching.

Woven fabric, warp threads stretched in the longitudinal direction of the loom It is made by weaving "filling" or "weft" yarns between warp threads lubrication and when filling yarns are placed at high speed during weaving They must be sized before weaving to protect them from abrasion. Common release agents starches (or starch derivatives and modified starches), poly(vinyl alcohol), starches predominantly carboxyl methyl cellulose (ie, CMC). Usually paraffin in the hash mixture, increases the bleaching effects of the methods. A particularly preferred intermediate is alloxan-S-oxime (violuric acid) and/or salts thereof or hydrates.

Textile Product As used herein, the term "textile product" includes fibers, yarns, fabrics, garments and non-wovens. indicates products. The term is natural, synthetic (eg, manufactured) and various natural and synthetic It covers textile products made from blends. Textile products, unprocessed or processed fiber, yarn, woven or knitted fabric, non-woven products and clothing; and some can be made using the various materials mentioned here.

The process according to the invention is most suitable for fabrics containing cellulose, for example cotton, viscose, rayon, ramie, linen, Tencel or blends thereof, or any of these fibers blends of any of these fibers, such as cotton and spandex (stretch-denim) blends. It is applied to blends with synthetic fibers. In particular, the fabric is dyed fabric, preferably it is denim. Denim fabric indigo or indigo-related dyes, such as thioindigo It may be dyed with paints.

In the most preferred embodiment of the process according to the invention, the fabric is indigo-dyed denim. and clothing items made of them.

The process of producing textile products A fabric, for example a cellulosic material as ready-made material for the manufacture of clothing its processing involves several steps: spinning the fiber into a yarn; weaving or knitting from yarn making the fabric; and subsequent preparation, dyeing/printing and finishing operations.

The preparation processes are the removal of natural and man-made impurities from the fiber and For example, increasing their aesthetic appearance and workability before dyeing/printing and finishing required for Common preparation processes produce a fabric suitable for dyeing or finishing. Includes stripping (for woven products), rubbing and bleaching.

Woven fabric, warp threads stretched in the longitudinal direction of the loom It is made by weaving "filling" or "weft" yarns between warp threads lubrication and when filling yarns are placed at high speed during weaving They must be sized before weaving to protect them from abrasion. Common release agents starches (or starch derivatives and modified starches), poly(vinyl alcohol), starches predominantly carboxyl methyl cellulose (ie, CMC). Usually paraffin in the hash mixture, increases the bleaching effects of the methods. A particularly preferred intermediate is alloxan-S-oxime (violuric acid) and/or salts thereof or hydrates.

Textile Product As used herein, the term "textile product" includes fibers, yarns, fabrics, garments and non-wovens. indicates products. The term is natural, synthetic (eg, manufactured) and various natural and synthetic It covers textile products made from blends. Textile products unprocessed or processed fiber, yarn, woven or knitted fabric, non-woven products and clothing; and some can be made using the various materials mentioned here.

The process according to the invention is most suitable for fabrics containing cellulose, for example cotton, viscose, rayon, ramie, linen, Tencel or blends thereof, or any of these fibers blends of any of these fibers, such as cotton and spandex (stretch-denim) blends. It is applied to blends with synthetic fibers. In particular, the fabric is dyed fabric, preferably it is denim. Denim fabric indigo or indigo-related dyes, such as thioindigo It may be dyed with paints.

In the most preferred embodiment of the process according to the invention, the fabric is indigo-dyed denim. and clothing items made of them.

The process of producing textile products A fabric, for example a cellulosic material as ready-made material for the manufacture of clothing its processing involves several steps: spinning the fiber into a yarn; weaving or knitting from yarn making the fabric; and subsequent preparation, dyeing/printing and finishing operations.

The preparation processes are the removal of natural and man-made impurities from the fiber and For example, increasing their aesthetic appearance and workability before dyeing/printing and finishing required for Common preparation processes produce a fabric suitable for dyeing or finishing. Includes stripping (for woven products), rubbing and bleaching.

Woven fabric, warp threads stretched in the longitudinal direction of the loom It is made by weaving "filling" or "weft" yarns between warp threads lubrication and when filling yarns are placed at high speed during weaving They must be sized before weaving to protect them from abrasion. Common release agents starches (or starch derivatives and modified starches), poly(vinyl alcohol), starches predominantly carboxyl methyl cellulose (ie, CMC). Usually paraffin in the hash mixture, acrylic binders and various lubricants are added. Filler thread along the warp threads or any of the countless other permutations. Generally, dresses shirts, trousers, sheets, towels, curtains Etc. It is produced from woven fabric. Material Once done, the husk on the fabric must be removed again (ie ribbing). By knitting, a fabric is formed by interlocking loops of yarn. of two types of yarn Knitted fabric is a single continuous thread produced from wire. As with weaving, there are many different ways to loop yarn together. and the final fabric properties depend on both the yarn and the type of knitting. underwear, sweaters, socks, sports shirts, tracksuits Etc. It is made of woven fabrics.

Dismantling Separation of sizing compounds from warp yarns in a woven quina and/or removal. Starch is usually treated with an enzymatic descaling procedure. is removed. In addition, sometimes oxidative descaling and descaling with acids or bases used.

In some embodiments, the descaling enzyme is an amylolytic enzyme, such as an alpha-amylase, a beta-amylase is a mannanase, a glucoamylase, or a combination thereof.

Suitable alpha or beta-amylases are of this type, as well as those of bacterial or fungal origin. chemically or genetically modified mutants and variants of amylases are included. Suitable alpha-amylases include alpha-amylases obtainable from Bacillus species. to suitable commercially available amylases, without limiting, OPTISIZE® NEXT, OPTISIZE® FLEX and OPTISIZE® COOL (all from Genencor International Inc.) and DURAMYLTM, ERMAMYLTM, FUNGAMYLTM THERMAMYLTM, AQUAZYMETM and BANTM (all available from Novozyines A/S, Bagsvaerd, Denmark) is included.

CGTases (cyclodextrin glucanotransferases, EC) to other suitable amylolytic enzymes 2.4.1.19), eg from Bacillus, Thermoanaerobactor or Thermoanaero-bacterium species are included.

Scrubbing to remove impurities from the fiber, swelling the fiber and removing the pod using for. It is one of the most important steps. The main purposes of rubbing are: a) fabric cleaning uniformly, b) softening particles and other garbage, c) fabric acrylic binders and various lubricants are added. Filler thread along the warp threads or any of the countless other permutations. Generally, dresses shirts, trousers, sheets, towels, curtains Etc. It is produced from woven fabric. Material Once done, the husk on the fabric must be removed again (ie ribbing). By knitting, a fabric is formed by interlocking loops of yarn. of two types of yarn Knitted fabric is a single continuous thread produced from wire. As with weaving, there are many different ways to loop yarn together. and the final fabric properties depend on both the yarn and the type of knitting. underwear, sweaters, socks, sports shirts, tracksuits Etc. It is made of woven fabrics.

Dismantling Separation of sizing compounds from warp yarns in a woven quina and/or removal. Starch is usually treated with an enzymatic descaling procedure. is removed. In addition, sometimes oxidative descaling and descaling with acids or bases used.

In some embodiments, the descaling enzyme is an amylolytic enzyme, such as an alpha-amylase, a beta-amylase is a mannanase, a glucoamylase, or a combination thereof.

Suitable alpha or beta-amylases are of this type, as well as those of bacterial or fungal origin. chemically or genetically modified mutants and variants of amylases are included. Suitable alpha-amylases include alpha-amylases obtainable from Bacillus species. to suitable commercially available amylases, without limiting, OPTISIZE® NEXT, OPTISIZE® FLEX and OPTISIZE® COOL (all from Genencor International Inc.) and DURAMYLTM, ERMAMYLTM, FUNGAMYLTM THERMAMYLTM, AQUAZYMETM and BANTM (all available from Novozyines A/S, Bagsvaerd, Denmark) is included.

CGTases (cyclodextrin glucanotransferases, EC) to other suitable amylolytic enzymes 2.4.1.19), eg from Bacillus, Thermoanaerobactor or Thermoanaero-bacterium species are included.

Scrubbing to remove impurities from the fiber, swelling the fiber and removing the pod using for. It is one of the most important steps. The main purposes of rubbing are: a) fabric cleaning uniformly, b) softening particles and other garbage, c) fabric acrylic binders and various lubricants are added. Filler thread along the warp threads or any of the countless other permutations. Generally, dresses shirts, trousers, sheets, towels, curtains Etc. It is produced from woven fabric. Material Once done, the husk on the fabric must be removed again (ie ribbing). By knitting, a fabric is formed by interlocking loops of yarn. of two types of yarn Knitted fabric is a single continuous thread produced from wire. As with weaving, there are many different ways to loop yarn together. and the final fabric properties depend on both the yarn and the type of knitting. underwear, sweaters, socks, sports shirts, tracksuits Etc. It is made of woven fabrics.

Dismantling Separation of sizing compounds from warp yarns in a woven quina and/or removal. Starch is usually treated with an enzymatic descaling procedure. is removed. In addition, sometimes oxidative descaling and descaling with acids or bases used.

In some embodiments, the descaling enzyme is an amylolytic enzyme, such as an alpha-amylase, a beta-amylase is a mannanase, a glucoamylase, or a combination thereof.

Suitable alpha or beta-amylases are of this type, as well as those of bacterial or fungal origin. chemically or genetically modified mutants and variants of amylases are included. Suitable alpha-amylases include alpha-amylases obtainable from Bacillus species. to suitable commercially available amylases, without limiting, OPTISIZE® NEXT, OPTISIZE® FLEX and OPTISIZE® COOL (all from Genencor International Inc.) and DURAMYLTM, ERMAMYLTM, FUNGAMYLTM THERMAMYLTM, AQUAZYMETM and BANTM (all available from Novozyines A/S, Bagsvaerd, Denmark) is included.

CGTases (cyclodextrin glucanotransferases, EC) to other suitable amylolytic enzymes 2.4.1.19), eg from Bacillus, Thermoanaerobactor or Thermoanaero-bacterium species are included.

Scrubbing to remove impurities from the fiber, swelling the fiber and removing the pod using for. It is one of the most important steps. The main purposes of rubbing are: a) fabric cleaning uniformly, b) softening particles and other garbage, c) fabric increasing absorbency, (1) saponification of fats, oils and waxes, and thawing and e) minimizing immature cotton. At the approximate boiling point Scrubbing with sodium hydroxide is an acceptable process for 100% cotton, while calcium hydroxide and sodium carbonate is used less frequently. Synthetic fiber is used in much softer conditions. cleared. Surfactants and chelating agents are important for alkaline scrubbing.

Enzymatic scrub application has started, where cellulase, hemicellulase, pectinase, lipase and All proteases are reported to have scrubbing effects.

Bleaching Bleaching, removal of pigmented color and/or colored impurities as well as seed coat removal of parts. It is the most important chemical treatment, because without damaging the fiber. A balance must be maintained between the degrees of whiteness. bleaching oxidizing or reducing performed using chemistry. Oxidizing agents also include a) hypochlorite (OCl'), b) chloride dioxide (using or generating can be divided as The reducing agents are typically sulfur dioxide, hydrosulfite salts Etc.

Enzymatic bleaching using glucose oxidase has been reported. Traditionally, this hydrogen peroxide is used.

printing and dyeing Binding the printing and dyeing dyestuff in textile products to the fiber in textile products Any suitable method for applying dyes to the textile product is carried out. Textile dyeing products e.g. passing the fabric through a concentrated dye solution, wet by storing the fabric in a vapor-proof chamber, allowing the dye to adhere to the fabric substrate. by rinsing the unreacted dye after it has been allowed to diffuse and react. is performed. Alternatively, by steaming the dye textile product before rinsing. can be fixed. Dyes include synthetic and natural dyes. Typical dyes are anionic functional containing groups (eg, acid dyes, direct dyes, Mordant dyes and reactive dyes), those containing cationic groups (e.g. basic dyes), chemical reaction prior to application require (e.g., fixed dyes, sulfur dyes and azoic dyes), disperse dyes and solvent are dyes.

To ensure stability in dyed textile products and to ensure that textile products are protected by the consumer. To prevent unwanted dye transfer during washing, excess non-fibre-bound The soluble dyestuff must be removed after dyeing. Generally, A large amount of water is required to remove excess paint from the grain. a traditional increasing absorbency, (1) saponification of fats, oils and waxes, and thawing and e) minimizing immature cotton. At the approximate boiling point Scrubbing with sodium hydroxide is an acceptable process for 100% cotton, while calcium hydroxide and sodium carbonate is used less frequently. Synthetic fiber is used in much softer conditions. cleared. Surfactants and chelating agents are important for alkaline scrubbing.

Enzymatic scrub application has started, where cellulase, hemicellulase, pectinase, lipase and All proteases are reported to have scrubbing effects.

Bleaching Bleaching, removal of pigmented color and/or colored impurities as well as seed coat removal of parts. It is the most important chemical treatment, because without damaging the fiber. A balance must be maintained between the degrees of whiteness. bleaching oxidizing or reducing performed using chemistry. Oxidizing agents also include a) hypochlorite (OCl'), b) chloride dioxide (using or generating can be divided as The reducing agents are typically sulfur dioxide, hydrosulfite salts Etc.

Enzymatic bleaching using glucose oxidase has been reported. Traditionally, this hydrogen peroxide is used.

printing and dyeing Binding the printing and dyeing dyestuff in textile products to the fiber in textile products Any suitable method for applying dyes to the textile product is carried out. Textile dyeing products e.g. passing the fabric through a concentrated dye solution, wet by storing the fabric in a vapor-proof chamber, allowing the dye to adhere to the fabric substrate. by rinsing the unreacted dye after it has been allowed to diffuse and react. is performed. Alternatively, by steaming the dye textile product before rinsing. can be fixed. Dyes include synthetic and natural dyes. Typical dyes are anionic functional containing groups (eg, acid dyes, direct dyes, Mordant dyes and reactive dyes), those containing cationic groups (e.g. basic dyes), chemical reaction prior to application require (e.g., fixed dyes, sulfur dyes and azoic dyes), disperse dyes and solvent are dyes.

To ensure stability in dyed textile products and to ensure that textile products are protected by the consumer. To prevent unwanted dye transfer during washing, excess non-fibre-bound The soluble dyestuff must be removed after dyeing. Generally, A large amount of water is required to remove excess paint from the grain. a traditional increasing absorbency, (1) saponification of fats, oils and waxes, and thawing and e) minimizing immature cotton. At the approximate boiling point Scrubbing with sodium hydroxide is an acceptable process for 100% cotton, while calcium hydroxide and sodium carbonate is used less frequently. Synthetic fiber is used in much softer conditions. cleared. Surfactants and chelating agents are important for alkaline scrubbing.

Enzymatic scrub application has started, where cellulase, hemicellulase, pectinase, lipase and All proteases are reported to have scrubbing effects.

Bleaching Bleaching, removal of pigmented color and/or colored impurities as well as seed coat removal of parts. It is the most important chemical treatment, because without damaging the fiber. A balance must be maintained between the degrees of whiteness. bleaching oxidizing or reducing performed using chemistry. Oxidizing agents also include a) hypochlorite (OCl'), b) chloride dioxide (using or generating can be divided as The reducing agents are typically sulfur dioxide, hydrosulfite salts Etc.

Enzymatic bleaching using glucose oxidase has been reported. Traditionally, this hydrogen peroxide is used.

printing and dyeing Binding the printing and dyeing dyestuff in textile products to the fiber in textile products Any suitable method for applying dyes to the textile product is carried out. Textile dyeing products e.g. passing the fabric through a concentrated dye solution, wet by storing the fabric in a vapor-proof chamber, allowing the dye to adhere to the fabric substrate. by rinsing the unreacted dye after it has been allowed to diffuse and react. is performed. Alternatively, by steaming the dye textile product before rinsing. can be fixed. Dyes include synthetic and natural dyes. Typical dyes are anionic functional containing groups (eg, acid dyes, direct dyes, Mordant dyes and reactive dyes), those containing cationic groups (e.g. basic dyes), chemical reaction prior to application require (e.g., fixed dyes, sulfur dyes and azoic dyes), disperse dyes and solvent are dyes.

To ensure stability in dyed textile products and to ensure that textile products are protected by the consumer. To prevent unwanted dye transfer during washing, excess non-fibre-bound The soluble dyestuff must be removed after dyeing. Generally, A large amount of water is required to remove excess paint from the grain. a traditional In the process, the printed or dyed textile product is first rinsed with cold water. then back- a suitable additive to reduce staining, eg poly(vinylpyrrolidone) (PVP) added and washed at high temperature.

WO99/34054 describes a drug containing at least one peroxidase, an oxidase agent, and at least one vehicle. rinse water, such as a percoccidase, hydrogen peroxide and 1-hydroxy-benzotriazole an enzymatic agent for removing excess dye from fabric dyed with a liquid containing a vehicle the transaction is explained.

Biopolishing The terms "biopolishing", "hair removal" or "hair-removal" used here are synonymous.

Without the application of finishing components, most cotton fabrics and cotton blend fabrics are relatively It feels firm and firm to the touch. The fabric surface is also not smooth, because small pile microfibrils protrude. In addition, after a relatively short period of use, The fuzz seen on the fabric surface gives an unpleasant, aged appearance.

Biopolishing is to treat cellulosic fabrics with enzymes such as cellulases during their production, It is a method that increases the fabric quality in terms of "low pilling". Biopolishing most important effects are less lint and fuzz, higher gloss/foam, increased fabric characterized by tactile sensation, longer lasting softness and/or increased water absorbency can be done. Biopolishing is often used in the manufacture of knitted or woven fabrics or clothing. carried out by wet processing. Wet treatment, for example, removing, rubbing, bleaching, washing, It includes stages such as drying/pressing and finishing. Biopolishing soaking stages as a separate step after any of these or with any of these soaking steps. can be performed in combination.

Denim Fabric Production Some dyed fabrics, such as denim fabric, involve dyeing the yarns before they are woven.

For denim fabric, the warp threads are dyed and shaped, for example, with indigo, before being woven.

Preferably the dyeing of the denim yarn is a ring-dyeing. Invent a preferred the arrangement of the yarn is a fixed dye, eg indigo or an indigo-related dye, eg thioindigo or ring with a sulfur dye or a direct dye or a reactive dye or a naphthol is painting. The yarn can also be combined with more than one dye, e.g. first a sulfur dye and then a It can be painted with fixed paint or vice versa.

Preferably before the yarns are dyed in order to obtain a higher quality denim fabric. In the process, the printed or dyed textile product is first rinsed with cold water. then back- a suitable additive to reduce staining, eg poly(vinylpyrrolidone) (PVP) added and washed at high temperature.

WO99/34054 describes a drug containing at least one peroxidase, an oxidase agent, and at least one vehicle. rinse water, such as a percoccidase, hydrogen peroxide and 1-hydroxy-benzotriazole an enzymatic agent for removing excess dye from fabric dyed with a liquid containing a vehicle the transaction is explained.

Biopolishing The terms "biopolishing", "hair removal" or "hair-removal" used here are synonymous.

Without the application of finishing components, most cotton fabrics and cotton blend fabrics are relatively it feels hard and firm to the touch. The fabric surface is also not smooth, because small pile microfibrils protrude. In addition, after a relatively short period of use, The fuzz seen on the fabric surface gives an unpleasant, aged appearance.

Biopolishing is to treat cellulosic fabrics with enzymes such as cellulases during their production, It is a method that increases the fabric quality in terms of "low pilling". Biopolishing most important effects are less lint and fuzz, higher gloss/foam, increased fabric characterized by tactile sensation, longer lasting softness and/or increased water absorbency can be done. Biopolishing is often used in the manufacture of knitted or woven fabrics or clothing. carried out by wet processing. Wet treatment, for example, removing, rubbing, bleaching, washing, It includes stages such as drying/pressing and finishing. Biopolishing soaking stages as a separate step after any of these or with any of these soaking steps. can be performed in combination.

Denim Fabric Production Some dyed fabrics, such as denim fabric, involve dyeing the yarns before they are woven.

For denim fabric, the warp threads are dyed and shaped, for example, with indigo, before being woven.

Preferably the dyeing of the denim yarn is a ring-dyeing. Invent a preferred the arrangement of the yarn is a fixed dye, eg indigo or an indigo-related dye, eg thioindigo or ring with a sulfur dye or a direct dye or a reactive dye or a naphthol is painting. The yarn can also be combined with more than one dye, e.g. first a sulfur dye and then a It can be painted with fixed paint or vice versa.

Preferably before the yarns are dyed in order to obtain a higher quality denim fabric. In the process, the printed or dyed textile product is first rinsed with cold water. then back- a suitable additive to reduce staining, eg poly(vinylpyrrolidone) (PVP) added and washed at high temperature.

WO99/34054 describes a drug containing at least one peroxidase, an oxidase agent, and at least one vehicle. rinse water, such as a percoccidase, hydrogen peroxide and 1-hydroxy-benzotriazole an enzymatic agent for removing excess dye from fabric dyed with a liquid containing a vehicle the transaction is explained.

Biopolishing The terms "biopolishing", "hair removal" or "hair-removal" used here are synonymous.

Without the application of finishing components, most cotton fabrics and cotton blend fabrics are relatively it feels hard and firm to the touch. The fabric surface is also not smooth, because small pile microfibrils protrude. In addition, after a relatively short period of use, The fuzz seen on the fabric surface gives an unpleasant, aged appearance.

Biopolishing is to treat cellulosic fabrics with enzymes such as cellulases during their production, It is a method that increases the fabric quality in terms of "low pilling". Biopolishing most important effects are less lint and fuzz, higher gloss/foam, increased fabric characterized by tactile sensation, longer lasting softness and/or increased water absorbency can be done. Biopolishing is often used in the manufacture of knitted or woven fabrics or clothing. carried out by wet processing. Wet treatment, for example, removing, rubbing, bleaching, washing, It includes stages such as drying/pressing and finishing. Biopolishing soaking stages as a separate step after any of these or with any of these soaking steps. can be performed in combination.

Denim Fabric Production Some dyed fabrics, such as denim fabric, involve dyeing the yarns before they are woven.

For denim fabric, the warp threads are dyed and shaped, for example, with indigo, before being woven.

Preferably the dyeing of the denim yarn is a ring-dyeing. Invent a preferred the arrangement of the yarn is a fixed dye, eg indigo or an indigo-related dye, eg thioindigo or ring with a sulfur dye or a direct dye or a reactive dye or a naphthol is painting. The yarn can also be combined with more than one dye, e.g. first a sulfur dye and then a It can be painted with fixed paint or vice versa.

Preferably before the yarns are dyed in order to obtain a higher quality denim fabric. rubbed and/or agartihr. Generally, woven into dyed fabric such as denim. The dyed fabric or garment then undergoes a resoldering stage, preferably followed by a bio- enters the grinding phase and/or a color changing phase.

The disassembly process used here is the same as the one mentioned above in the text.

After descaling, the dyed fabric enters a bio-grinding stage. Bio-grinding stage can be accomplished with enzymes or pumice stones or both. used here in an aqueous medium containing an abrasive cellulase or a combination thereof means providing a "stone-washed" appearance with agitation. In every situation, mechanical action is required to remove paint and the process is usually washing machines, for example drum washers, are performed in core washers.

As a result of uneven removal of paint, painted areas and Contrasts occur between areas where the dye has been removed. Treatment with cellulase completely replaces the process with the sponge stone. However, more highly digested where a finish is desired, the cellulase treatment can be combined with the pumice stone treatment.

Preferably, the etching is followed by a color changing step. "color changing" used here or the terms "color adjusting" are equally the absence of a dyestuff associated with the textile product. any equivalent of the textile product as a result of the removal, alteration or removal of indicates any color change. Without wanting to get angry with a theory, color the change is due to the alteration of the chromophores associated with the textile material, it is claimed that it thus changes its visual appearance. Choromophores are a textile product. may be inherently related to the material used to produce it (front, white color of cotton) or it may be associated with special finishes such as dyeing or printing. Color changing in a chromophore chemical change as well as chemical change in the material to which a chromophore is attached Samples of color change include, but are not limited to, bleaching, rebonding/back-staining. reduce, fade, add a gray tone, change hue, saturation, and brightness. replacement and the like. The amount and type of color change is a peroxidase enzyme. enzymatic treatment of the color (ie residual color) of a textile product spectrophotometric or known by the color (i.e. original) of the textile product before processing can be determined by comparison with visual inspection methods.

In the present invention, a method for changing the color of a textile product rubbed and/or agartihr. Generally, woven into dyed fabric such as denim. The dyed fabric or garment then undergoes a resoldering stage, preferably followed by a bio- enters the grinding phase and/or a color changing phase.

The disassembly process used here is the same as the one mentioned above in the text.

After descaling, the dyed fabric enters a bio-grinding stage. Bio-grinding stage can be accomplished with enzymes or pumice stones or both. used here in an aqueous medium containing an abrasive cellulase or a combination thereof means providing a "stone-washed" appearance with agitation. In every situation, mechanical action is required to remove paint and the process is usually washing machines, for example drum washers, are performed in core washers.

As a result of uneven removal of paint, painted areas and Contrasts occur between areas where the dye has been removed. Treatment with cellulase completely replaces the process with the sponge stone. However, more highly digested where a finish is desired, the cellulase treatment can be combined with the pumice stone treatment.

Preferably, the etching is followed by a color changing step. "color changing" used here or the terms "color adjusting" are equally the absence of a dyestuff associated with the textile product. any equivalent of the textile product as a result of the removal, alteration or removal of indicates any color change. Without wanting to get angry with a theory, color the change is due to the alteration of the chromophores associated with the textile material, it is claimed that it thus changes its visual appearance. Choromophores are a textile product. may be inherently related to the material used to produce it (front, white color of cotton) or it may be associated with special finishes such as dyeing or printing. Color changing in a chromophore chemical change as well as chemical change in the material to which a chromophore is attached Samples of color change include, but are not limited to, bleaching, rebonding/back-staining. reduce, fade, add a gray tone, change hue, saturation, and brightness. replacement and the like. The amount and type of color change is a peroxidase enzyme. enzymatic treatment of the color (ie residual color) of a textile product spectrophotometric or known by the color (i.e. original) of the textile product before processing can be determined by comparison with visual inspection methods.

In the present invention, a method for changing the color of a textile product rubbed and/or agartihr. Generally, woven into dyed fabric such as denim. The dyed fabric or garment then undergoes a resoldering stage, preferably followed by a bio- enters the grinding phase and/or a color changing phase.

The disassembly process used here is the same as the one mentioned above in the text.

After descaling, the dyed fabric enters a bio-grinding stage. Bio-grinding stage can be accomplished with enzymes or pumice stones or both. used here in an aqueous medium containing an abrasive cellulase or a combination thereof means providing a "stone-washed" appearance with agitation. In every situation, mechanical action is required to remove paint and the process is usually washing machines, for example drum washers, are performed in core washers.

As a result of uneven removal of paint, painted areas and Contrasts occur between areas where the dye has been removed. Treatment with cellulase completely replaces the process with the sponge stone. However, more highly digested where a finish is desired, the cellulase treatment can be combined with the pumice stone treatment.

Preferably, the etching is followed by a color changing step. "color changing" used here or the terms "color adjusting" are equally the absence of a dyestuff associated with the textile product. any equivalent of the textile product as a result of the removal, alteration or removal of indicates any color change. Without wanting to get angry with a theory, color the change is due to the alteration of the chromophores associated with the textile material, it is claimed that it thus changes its visual appearance. Choromophores are a textile product. may be inherently related to the material used to produce it (front, white color of cotton) or it may be associated with special finishes such as dyeing or printing. Color changing in a chromophore chemical change as well as chemical change in the material to which a chromophore is attached Samples of color change include, but are not limited to, bleaching, rebonding/back-staining. reduce, fade, add a gray tone, change hue, saturation, and brightness. replacement and the like. The amount and type of color change is a peroxidase enzyme. enzymatic treatment of the color (ie residual color) of a textile product spectrophotometric or known by the color (i.e. original) of the textile product before processing can be determined by comparison with visual inspection methods.

In the present invention, a method for changing the color of a textile product contact of the product with a peroxidase, a hydrogen peroxide source and an intermediate includes transfer. In some embodiments, the textile product is a peroxidase, a hydrogen peroxide It is contacted in an aqueous solution with the source and a vehicle.

In the textile product, especially in denim, a faded or agarmis appearance can be obtained in certain areas. It is an important part of textile production. This is normally from the etching stage. then applying KMnO4 (or KMnO4/H3PO4) solution on the dried denim. (via brushing, rubbing or spraying). stained areas It becomes agarmis after drying and washing with Na28205 solution. This transaction During oxidation, the indigo/sulfur dyes are destroyed by KMnO4 and combined with Nazszos. The brown color caused by oxidation products is removed by washing. This type of a local color change on the denim to meet the needs of the process consumers, that is, it creates a special agarina pattern.

The composition according to the present invention can also be applied on denim by means of a simple 'scrub-wash'. can create a custom bleached pattern, i.e. on dry denim, as described in the present invention. a mixture of peroxidase and a medium is applied, treated after washing with H2O2 bath fields become agarrnis.

For the purpose of the present invention, the "color changing" is on the front of the textile product. measured by the agartina level. This bleaching level is for example a textile processing application. in the context of the production of a brighter and/or whiter product, as well as, for example, a Indicates lightening of a stain in the context of the cleaning application.

In some embodiments, the bleaching level on the front of the textile product is given in Example 1. protein/g fabric peroxidase dosage, 0.5 mM/L vehicle dosage and 0.05 g/L hydrogen by treatment with a peroxidase, a hydrogen peroxide source, and a vehicle with peroxide dosage is measured. The hydrogen peroxide dosage used here is the hydrogen peroxide added during the process. hydrogen peroxide added in an amount constituting the dosage or 0.05 g/L level of hydrogen peroxide indicates the peroxide source. In a preferred embodiment, the test specified in Example 1 Under the conditions, the method or composition according to the present invention has the highest bleaching level in the front. at least 1.5 Delta L* units, more preferably at least 1.6, more preferably at least 1.7, more preferably at least 1.8, more preferably at least 1.9, more preferably at least 2, more preferably at least 2.1, more preferably at least 2.2, more preferably at least 2.3, more preferably at least 2.4, more preferably at least 2.5, more preferably at least at least 2.6, still more preferably at least 2.7, still more preferably at least 2.8, still more preferably at least 2.9, contact of the product with a peroxidase, a hydrogen peroxide source and an intermediate includes transfer. In some embodiments, the textile product is a peroxidase, a hydrogen peroxide It is contacted in an aqueous solution with the source and a vehicle.

In the textile product, especially in denim, a faded or agarmis appearance can be obtained in certain areas. It is an important part of textile production. This is normally from the etching stage. then applying KMnO4 (or KMnO4/H3PO4) solution on the dried denim. (via brushing, rubbing or spraying). stained areas It becomes agarmis after drying and washing with Na28205 solution. This transaction During oxidation, the indigo/sulfur dyes are destroyed by KMnO4 and combined with Nazszos. The brown color caused by oxidation products is removed by washing. This type of a local color change on the denim to meet the needs of the process consumers, that is, it creates a special agarina pattern.

The composition according to the present invention can also be applied on denim by means of a simple 'scrub-wash'. can create a custom bleached pattern, i.e. on dry denim, as described in the present invention. a mixture of peroxidase and a medium is applied, treated after washing with H2O2 bath fields become agarrnis.

For the purpose of the present invention, the "color changing" is on the front of the textile product. measured by the agartina level. This bleaching level is for example a textile processing application. in the context of the production of a brighter and/or whiter product, as well as, for example, a Indicates lightening of a stain in the context of the cleaning application.

In some embodiments, the bleaching level on the front of the textile product is given in Example 1. protein/g fabric peroxidase dosage, 0.5 mM/L vehicle dosage and 0.05 g/L hydrogen by treatment with a peroxidase, a hydrogen peroxide source, and a vehicle with peroxide dosage is measured. The hydrogen peroxide dosage used here is the hydrogen peroxide added during the process. hydrogen peroxide added in an amount constituting the dosage or 0.05 g/L level of hydrogen peroxide indicates the peroxide source. In a preferred embodiment, the test specified in Example 1 Under the conditions, the method or composition according to the present invention has the highest bleaching level in the front. at least 1.5 Delta L* units, more preferably at least 1.6, more preferably at least 1.7, more preferably at least 1.8, more preferably at least 1.9, more preferably at least 2, more preferably at least 2.1, more preferably at least 2.2, more preferably at least 2.3, more preferably at least 2.4, more preferably at least 2.5, more preferably at least at least 2.6, still more preferably at least 2.7, still more preferably at least 2.8, still more preferably at least 2.9, contact of the product with a peroxidase, a hydrogen peroxide source and an intermediate includes transfer. In some embodiments, the textile product is a peroxidase, a hydrogen peroxide It is contacted in an aqueous solution with the source and a vehicle.

In the textile product, especially in denim, a faded or agarmis appearance can be obtained in certain areas. It is an important part of textile production. This is normally from the etching stage. then applying KMnO4 (or KMnO4/H3PO4) solution on the dried denim. (via brushing, rubbing or spraying). stained areas It becomes agarmis after drying and washing with Na28205 solution. This transaction During oxidation, the indigo/sulfur dyes are destroyed by KMnO4 and combined with Nazszos. The brown color caused by oxidation products is removed by washing. This type of a local color change on the denim to meet the needs of the process consumers, that is, it creates a special agarina pattern.

The composition according to the present invention can also be applied on denim by means of a simple 'scrub-wash'. can create a custom bleached pattern, i.e. on dry denim, as described in the present invention. a mixture of peroxidase and a medium is applied, treated after washing with H2O2 bath fields become agarrnis.

For the purpose of the present invention, the "color changing" is on the front of the textile product. measured by the agartina level. This bleaching level is for example a textile processing application. in the context of the production of a brighter and/or whiter product, as well as, for example, a Indicates lightening of a stain in the context of the cleaning application.

In some embodiments, the bleaching level on the front of the textile product is given in Example 1. protein/g fabric peroxidase dosage, 0.5 mM/L vehicle dosage and 0.05 g/L hydrogen by treatment with a peroxidase, a hydrogen peroxide source, and a vehicle with peroxide dosage is measured. The hydrogen peroxide dosage used here is the hydrogen peroxide added during the process. hydrogen peroxide added in an amount constituting the dosage or 0.05 g/L level of hydrogen peroxide indicates the peroxide source. In a preferred embodiment, the test specified in Example 1 Under the conditions, the method or composition according to the present invention has the highest bleaching level in the front. at least 1.5 Delta L* units, more preferably at least 1.6, more preferably at least 1.7, more preferably at least 1.8, more preferably at least 1.9, more preferably at least 2, more preferably at least 2.1, more preferably at least 2.2, more preferably at least 2.3, more preferably at least 2.4, more preferably at least 2.5, more preferably at least at least 2.6, still more preferably at least 2.7, still more preferably at least 2.8, still more preferably at least 2.9, it even exhibits a color change that is most preferably at least 3 Delta L* units. Delta L* unit It is described in the material and method section under color adjustment.

According to the present invention, color change on the back of the textile product Delta b* unit bleaching known as the level. The dyestuff on the back of the textile product is usually low. The color change of the dried textile product cannot be detected easily.

In some embodiments, the bleaching level on the back of the textile product is given in Example 1. protein/g fabric peroxidase dosage, 0.5 mM/L vehicle dosage and 0.05 g/L hydrogen by treatment with a peroxidase, a hydrogen peroxide source, and a vehicle with peroxide dosage is measured, where preferably the method or composition according to the present invention is >0 Delta b* on the reverse unit exhibits a color change with the level of bleaching. Delta b* unit under color adjustment described in the material and method section.

Additional Enzymes It will be appreciated that one or more of cellulase, perhydrolase, laccase, amylase, lipase, mannanase, amylase, protease, oxidase, catalase or other enzymes mentioned herein are present It can be used as an additional enzyme in compositions and methods. In addition, from the essence of the specification any number of additional enzymes (or enzymes) by existing compositions and methods without system) can be combined.

The protease is for example a metalloprotease (EC 3.4.17 or EC 3.4.24) or a serine protease (EC 3.4.21), preferably an alkaline microbial protease or a trypsin-like protease.

Examples of proteases are subtilisins (EC 3.4.21.62), especially those derived from Bacillus, e.g. subtilisin Novo, subtilisin Carlsberg, subtilisin 309, subtilisin 147 and subtilisin 168 (WO 89/06279). Examples of trypsin-like proteases are trypsin (pre-, porcine or protease. denotes an enzyme that catalyzes its degradation. Cellulases are often, for example, including those identified as cellobiohydrolases, endoglucanases and beta-glucosidases.

Commercially available cellulase enzyme useful in the method of the present invention Examples of products are: Cellusoft®, Celluclast®, Denimax® Acid, Denimax® Ultra (all Novozymes A/S, Bagsvaerd, Denmark); IndiageTM, PrimafastTM (both Genencor International Inc., USA); PowerstoneTM (logen, Canada) and EcostoneTM, it even exhibits color change, most preferably at least 3 Delta L* units. Delta L* unit It is described in the material and method section under color adjustment.

According to the present invention, color change on the back of the textile product Delta b* unit bleaching known as the level. The dyestuff on the back of the textile product is usually low. The color change of the dried textile product cannot be detected easily.

In some embodiments, the bleaching level on the back of the textile product is given in Example 1. protein/g fabric peroxidase dosage, 0.5 mM/L vehicle dosage and 0.05 g/L hydrogen by treatment with a peroxidase, a hydrogen peroxide source, and a vehicle with peroxide dosage is measured, where preferably the method or composition according to the present invention is >0 Delta b* on the reverse unit exhibits a color change with the level of bleaching. Delta b* unit under color adjustment described in the material and method section.

Additional Enzymes It will be appreciated that one or more of cellulase, perhydrolase, laccase, amylase, lipase, mannanase, amylase, protease, oxidase, catalase or other enzymes mentioned herein are present It can be used as an additional enzyme in compositions and methods. In addition, from the essence of the specification any number of additional enzymes (or enzymes) by existing compositions and methods without system) can be combined.

The protease is for example a metalloprotease (EC 3.4.17 or EC 3.4.24) or a serine protease (EC 3.4.21), preferably an alkaline microbial protease or a trypsin-like protease.

Examples of proteases are subtilisins (EC 3.4.21.62), especially those derived from Bacillus, e.g. subtilisin Novo, subtilisin Carlsberg, subtilisin 309, subtilisin 147 and subtilisin 168 (WO 89/06279). Examples of trypsin-like proteases are trypsin (pre-, porcine or protease. denotes an enzyme that catalyzes its degradation. Cellulases are often, for example, including those identified as cellobiohydrolases, endoglucanases and beta-glucosidases.

Commercially available cellulase enzyme useful in the method of the present invention Examples of products are: Cellusoft®, Celluclast®, Denimax® Acid, Denimax® Ultra (all Novozymes A/S, Bagsvaerd, Denmark); IndiageTM, PrimafastTM (both Genencor International Inc., USA); PowerstoneTM (logen, Canada) and EcostoneTM, it even exhibits color change, most preferably at least 3 Delta L* units. Delta L* unit It is described in the material and method section under color adjustment.

According to the present invention, color change on the back of the textile product Delta b* unit bleaching known as the level. The dyestuff on the back of the textile product is usually low. The color change of the dried textile product cannot be detected easily.

In some embodiments, the bleaching level on the back of the textile product is given in Example 1. protein/g fabric peroxidase dosage, 0.5 mM/L vehicle dosage and 0.05 g/L hydrogen by treatment with a peroxidase, a hydrogen peroxide source, and a vehicle with peroxide dosage is measured, where preferably the method or composition according to the present invention is >0 Delta b* on the reverse unit exhibits a color change with the level of bleaching. Delta b* unit under color adjustment described in the material and method section.

Additional Enzymes It will be appreciated that one or more of cellulase, perhydrolase, laccase, amylase, lipase, mannanase, amylase, protease, oxidase, catalase or other enzymes mentioned herein are present It can be used as an additional enzyme in compositions and methods. In addition, from the essence of the specification any number of additional enzymes (or enzymes) by existing compositions and methods without system) can be combined.

The protease is for example a metalloprotease (EC 3.4.17 or EC 3.4.24) or a serine protease (EC 3.4.21), preferably an alkaline microbial protease or a trypsin-like protease.

Examples of proteases are subtilisins (EC 3.4.21.62), especially those derived from Bacillus, e.g. subtilisin Novo, subtilisin Carlsberg, subtilisin 309, subtilisin 147 and subtilisin 168 (WO 89/06279). Examples of trypsin-like proteases are trypsin (pre-, porcine or protease. denotes an enzyme that catalyzes its degradation. Cellulases are often, for example, including those identified as cellobiohydrolases, endoglucanases and beta-glucosidases.

Commercially available cellulase enzyme useful in the method of the present invention Examples of products are: Cellusoft®, Celluclast®, Denimax® Acid, Denimax® Ultra (all Novozymes A/S, Bagsvaerd, Denmark); IndiageTM, PrimafastTM (both Genencor International Inc., USA); PowerstoneTM (logen, Canada) and EcostoneTM, BiotouchTM (both AB Enzymes, Finland).

A "perhydrolase" as described for use in an oxidizing paint decolorization process catalyzes a perhydrolysis reaction that produces a sufficiently high amount of peracid It is an enzyme that can In general, the perhydrolase enzyme has a high perhydrolysis/hydrolysis ratio. exhibits. In some embodiments, the perhydrolase enzyme is a naturally occurring Mycobacterium smegmatis perhydrolase enzyme or a variant thereof. This enzyme, its enzymatic properties, structure and various variants and homologues International Patent Application Publication A "laccase" is simultaneous with the reduction of oxygen to water in a four-electron transfer process. Oxidation of phenols, polyphenols and anilines by single-electron removal It is a poly-virgin containing oxidase (EC 1.10.32) that catalyzes it. In the method according to the present invention Examples of commercially available laccase enzyme products that are useful are: EcoFade Procedure According to the Invention In the present invention, a textile product has a peroxidase, a hydrogen peroxide source and a vehicle. The method for the processing of the textile product is provided by contacting it with the substance.

A wash water/textile product suitable for use in the present method is approximately 20:1 to It is suggested that it can be between 521 (volume/weight).

The reaction time is usually from about 1 minute to about 5 hours. Preferably the reaction time is from about 3 minutes to about 180 minutes, more preferably reaction time about 5 minutes to about 60 minutes, still more preferably 5 to 30 minutes, and most preferably It is between 30 minutes.

The process according to the present invention is at a pH of between about 2 and about 8, preferably about about 8 at a pH of 3 to about 7, more preferably at a pH of about 4 to about 7, still more preferably at a pH of from about 4 to about 6 and most preferably about 4 carried out at a pH of from 5 to about 5.

The process according to the present invention is below 90°C, preferably below 75°C, more preferably Below 65°C, more preferably below 60°C, more preferably below 55°C, more preferably It can take place at a temperature below 45°C, still more preferably below 35°C.

BiotouchTM (both AB Enzymes, Finland).

A "perhydrolase" as described for use in an oxidizing paint decolorization process catalyzes a perhydrolysis reaction that produces a sufficiently high amount of peracid It is an enzyme that can In general, the perhydrolase enzyme has a high perhydrolysis/hydrolysis ratio. exhibits. In some embodiments, the perhydrolase enzyme is a naturally occurring Mycobacterium smegmatis perhydrolase enzyme or a variant thereof. This enzyme, its enzymatic properties, structure and various variants and homologues International Patent Application Publication A "laccase" is simultaneous with the reduction of oxygen to water in a four-electron transfer process. Oxidation of phenols, polyphenols and anilines by single-electron removal It is a poly-virgin containing oxidase (EC 1.10.32) that catalyzes it. In the method according to the present invention Examples of commercially available laccase enzyme products that are useful are: EcoFade Procedure According to the Invention In the present invention, a textile product has a peroxidase, a hydrogen peroxide source and a vehicle. The method for the processing of the textile product is provided by contacting it with the substance.

A wash water/textile product suitable for use in the present method is approximately 20:1 to It is suggested that it can be between 521 (volume/weight).

The reaction time is usually from about 1 minute to about 5 hours. Preferably the reaction time is from about 3 minutes to about 180 minutes, more preferably reaction time about 5 minutes to about 60 minutes, still more preferably 5 to 30 minutes, and most preferably It is between 30 minutes.

The process according to the present invention is at a pH of between about 2 and about 8, preferably about about 8 at a pH of 3 to about 7, more preferably at a pH of about 4 to about 7, still more preferably at a pH of from about 4 to about 6 and most preferably about 4 carried out at a pH of from 5 to about 5.

The process according to the present invention is below 90°C, preferably below 75°C, more preferably Below 65°C, more preferably below 60°C, more preferably below 55°C, more preferably It can take place at a temperature below 45°C, still more preferably below 35°C.

BiotouchTM (both AB Enzymes, Finland).

A "perhydrolase" as described for use in an oxidizing paint decolorization process catalyzes a perhydrolysis reaction that produces a sufficiently high amount of peracid It is an enzyme that can In general, the perhydrolase enzyme has a high perhydrolysis/hydrolysis ratio. exhibits. In some embodiments, the perhydrolase enzyme is a naturally occurring Mycobacterium smegmatis perhydrolase enzyme or a variant thereof. This enzyme, its enzymatic properties, structure and various variants and homologues International Patent Application Publication A "laccase" is simultaneous with the reduction of oxygen to water in a four-electron transfer process. Oxidation of phenols, polyphenols and anilines by single-electron removal It is a poly-virgin containing oxidase (EC 1.10.32) that catalyzes it. In the method according to the present invention Examples of commercially available laccase enzyme products that are useful are: EcoFade Procedure According to the Invention In the present invention, a textile product has a peroxidase, a hydrogen peroxide source and a vehicle. The method for the processing of the textile product is provided by contacting it with the substance.

A wash water/textile product suitable for use in the present method is approximately 20:1 to It is suggested that it can be between 521 (volume/weight).

The reaction time is usually from about 1 minute to about 5 hours. Preferably the reaction time is from about 3 minutes to about 180 minutes, more preferably reaction time about 5 minutes to about 60 minutes, still more preferably 5 to 30 minutes, and most preferably It is between 30 minutes.

The process according to the present invention is at a pH of between about 2 and about 8, preferably about about 8 at a pH of 3 to about 7, more preferably at a pH of about 4 to about 7, still more preferably at a pH of from about 4 to about 6 and most preferably about 4 carried out at a pH of from 5 to about 5.

The process according to the present invention is below 90°C, preferably below 75°C, more preferably Below 65°C, more preferably below 60°C, more preferably below 55°C, more preferably It can take place at a temperature below 45°C, still more preferably below 35°C.

In some embodiments, the process according to the present invention is 10-90°C, preferably 15-80°C, more It is carried out in a temperature range of 50°C.

Enzyme dosage is highly dependent on enzyme reaction time and activity, i.e. relatively a relatively high enzyme with a short enzymatic reaction time or low enzymatic activity requires dosage and vice versa. In general, enzyme dosage is present in the reaction can be adjusted according to the duration. In a particular embodiment, the dosage of peroxidase and, if present, additional enzymes is applied to the fabric. approximately 0.0001 milligrams (mg) of enzyme protein per gram of enzyme protein to approximately 10 mg of enzyme protein (of each enzyme), preferably 0.0005 mg of enzyme protein to 5 mg of enzyme per gram of fabric protein, more preferably 0.0008 mg enzyme protein to 3 mg enzyme protein per gram of fabric, more preferably 0.001 mg of enzyme protein to 2 mg of enzyme protein per gram of fabric, more preferably 0.001 mg of enzyme protein to 1 mg of enzyme protein per gram of fabric, more preferably 0.001 mg of enzyme protein to 0.5 mg of enzyme protein per gram of fabric, still more preferably 0.001 mg of enzyme protein to 0.1 mg of enzyme protein per gram of fabric. These amounts are also indicates the amount of each enzyme. between 0.05 mM to 10 mM and still more preferably 0.05 mM to 5 mM and still more preferably 0.1 mM to 1 mM and most preferably 0.1 mM to It may be present at a concentration of 0.5 mM.

The hydrogen peroxide source is at the start of the process or during the process, e.g. typically to lmM hydrogen peroxide levels, and in particular 001 to 0.5 mM hydrogen peroxide may be added in an amount corresponding to the levels. The hydrogen peroxide used here source of hydrogen peroxide or hydrogen peroxide dosed within the specified ranges indicates the amount of hydrogen peroxide source added in a peroxide-forming amount.

When needed, oxygen in the atmosphere will usually be available in sufficient quantity. Therefore, The reaction can suitably be carried out in an open reactor, ie in the atmosphere.

In addition to peroxidase and additional enzymes, various additives, if present, are included in the invention. can be used in the corresponding transaction. Surfactants and/or dispersants in a textile product available and/or added. Therefore, the process and use of textiles according to the present invention An anionic, non-ionic, cationic10 traditionally used product in processing In some embodiments, the process according to the present invention is 10-90°C, preferably 15-80°C, more It is carried out in a temperature range of 50°C.

Enzyme dosage is highly dependent on enzyme reaction time and activity, i.e. relatively a relatively high enzyme with a short enzymatic reaction time or low enzymatic activity requires dosage and vice versa. In general, enzyme dosage is present in the reaction can be adjusted according to the duration. In a particular embodiment, the dosage of peroxidase and, if present, additional enzymes is applied to the fabric. approximately 0.0001 milligrams (mg) of enzyme protein per gram of enzyme protein to approximately 10 mg of enzyme protein (of each enzyme), preferably 0.0005 mg of enzyme protein to 5 mg of enzyme per gram of fabric protein, more preferably 0.0008 mg enzyme protein to 3 mg enzyme protein per gram of fabric, more preferably 0.001 mg of enzyme protein to 2 mg of enzyme protein per gram of fabric, more preferably 0.001 mg of enzyme protein to 1 mg of enzyme protein per gram of fabric, more preferably 0.001 mg of enzyme protein to 0.5 mg of enzyme protein per gram of fabric, still more preferably 0.001 mg of enzyme protein to 0.1 mg of enzyme protein per gram of fabric. These amounts are also indicates the amount of each enzyme. between 0.05 mM to 10 mM and still more preferably 0.05 mM to 5 mM and still more preferably 0.1 mM to 1 mM and most preferably 0.1 mM to It may be present at a concentration of 0.5 mM.

The hydrogen peroxide source is at the start of the process or during the process, e.g. typically to lmM hydrogen peroxide levels, and in particular 001 to 0.5 mM hydrogen peroxide may be added in an amount corresponding to the levels. The hydrogen peroxide used here source of hydrogen peroxide or hydrogen peroxide dosed within the specified ranges indicates the amount of hydrogen peroxide source added in a peroxide-forming amount.

When needed, oxygen in the atmosphere will usually be available in sufficient quantity. Therefore, The reaction can suitably be carried out in an open reactor, ie in the atmosphere.

In addition to peroxidase and additional enzymes, various additives, if present, are included in the invention. can be used in the corresponding transaction. Surfactants and/or dispersants in a textile product available and/or added. Therefore, the process and use of textiles according to the present invention An anionic, non-ionic, cationic10 traditionally used product in processing In some embodiments, the process according to the present invention is 10-90°C, preferably 15-80°C, more It is carried out in a temperature range of 50°C.

Enzyme dosage is highly dependent on enzyme reaction time and activity, i.e. relatively a relatively high enzyme with a short enzymatic reaction time or low enzymatic activity requires dosage and vice versa. In general, enzyme dosage is present in the reaction can be adjusted according to the duration. In a particular embodiment, the dosage of peroxidase and, if present, additional enzymes is applied to the fabric. approximately 0.0001 milligrams (mg) of enzyme protein per gram of enzyme protein to approximately 10 mg of enzyme protein (of each enzyme), preferably 0.0005 mg of enzyme protein to 5 mg of enzyme per gram of fabric protein, more preferably 0.0008 mg enzyme protein to 3 mg enzyme protein per gram of fabric, more preferably 0.001 mg of enzyme protein to 2 mg of enzyme protein per gram of fabric, more preferably 0.001 mg of enzyme protein to 1 mg of enzyme protein per gram of fabric, more preferably 0.001 mg of enzyme protein to 0.5 mg of enzyme protein per gram of fabric, still more preferably 0.001 mg of enzyme protein to 0.1 mg of enzyme protein per gram of fabric. These amounts are also indicates the amount of each enzyme. between 0.05 mM to 10 mM and still more preferably 0.05 mM to 5 mM and still more preferably 0.1 mM to 1 mM and most preferably 0.1 mM to It may be present at a concentration of 0.5 mM.

The hydrogen peroxide source is at the start of the process or during the process, e.g. typically to lmM hydrogen peroxide levels, and in particular 001 to 0.5 mM hydrogen peroxide may be added in an amount corresponding to the levels. The hydrogen peroxide used here source of hydrogen peroxide or hydrogen peroxide dosed within the specified ranges indicates the amount of hydrogen peroxide source added in a peroxide-forming amount.

When needed, oxygen in the atmosphere will usually be available in sufficient quantity. Therefore, The reaction can suitably be carried out in an open reactor, ie in the atmosphere.

In addition to peroxidase and additional enzymes, various additives, if present, are included in the invention. can be used in the corresponding transaction. Surfactants and/or dispersants in a textile product available and/or added. Therefore, the process and use of textiles according to the present invention An anionic, non-ionic, cationic10 traditionally used product in processing and/or in the presence of zwitterionic surfactant and/or dispersant.

Examples of anionic surfactants are carboxylates, sulfates, sulfonates or alkyl, substituted alkyl or aryl phosphates. Examples of nonionic surfactants polyoxyethylene compounds, for example alcohol ethoxylates, propoxylates or mixed ethoxy- /propoxylates are poly-glycerols and other polyols as well as certain block-copolymers.

Examples of cationic surfactants are water-soluble cationic polymers, e.g. quaternary ammonium sulfates and certain amines, e.g. epichlorohydrin/dimethylamine polymers (EPI-DMA) and their crosslinked solutions, polydiallyl dimethyl ammonium chloride (DADMAC), DADMAC/Acrylamide co-polymers and ionene polymers, eg US patent examples of substances are betaines, glycinates, amino propionates, imino propionates and various imidazoline derivatives. Also, US patent no. The polymers described in 5,256,252 are also can be used.

In the process according to the invention, peroxidase can be administered alone or in combination with an additional enzyme. "An addition The term "enzyme" means at least one additional enzyme, eg, one, two, three, four, five, six, seven, eight, nine, ten or it means even more additional enzymes. means applicable at the same or at another stage. Other processing stage textile production Compared to the stage in the process where the textile is treated with a peroxidase, earlier or earlier maybe later.

In certain embodiments, additional enzyme protease, lipase, xylanase, cutinase, Oxidoreductase, cellulase, is an enzyme with endoglucanase, amylase and/or nannanase activity. oxidoreductase Examples of enzymes that have laccase, perhydrolase and/or peroxidase activity are enzymes. In a preferred embodiment, the additional enzyme is laccase.

In some embodiments, the method of processing the textile product includes: (a) textile contacting the product with cellulase; (b) a peroxidase of the textile product, a hydrogen peroxide source and contact with an intermediate. In some embodiments, steps (a) and (b) There is a washing stage between them. In some embodiments, the intermediate wash stages (a) and (b) performed in a single bath without In some embodiments, (a) and (b) the same bathroom performed sequentially or simultaneously. In some embodiments, (a) and (b) a single It is performed sequentially in the bath, where (a) is performed before (b).

In some embodiments, step (a) is followed by an enzymatic degradation step. Some and/or in the presence of zwitterionic surfactant and/or dispersant.

Examples of anionic surfactants are carboxylates, sulfates, sulfonates or alkyl, substituted alkyl or aryl phosphates. Examples of nonionic surfactants polyoxyethylene compounds, for example alcohol ethoxylates, propoxylates or mixed ethoxy- /propoxylates are poly-glycerols and other polyols as well as certain block-copolymers.

Examples of cationic surfactants are water-soluble cationic polymers, e.g. quaternary ammonium sulfates and certain amines, e.g. epichlorohydrin/dimethylamine polymers (EPI-DMA) and their crosslinked solutions, polydiallyl dimethyl ammonium chloride (DADMAC), DADMAC/Acrylamide co-polymers and ionene polymers, eg US patent examples of substances are betaines, glycinates, amino propionates, imino propionates and various imidazoline derivatives. Also, US patent no. The polymers described in 5,256,252 are also can be used.

In the process according to the invention, peroxidase can be administered alone or in combination with an additional enzyme. "An addition The term "enzyme" means at least one additional enzyme, eg, one, two, three, four, five, six, seven, eight, nine, ten or it means even more additional enzymes. means applicable at the same or at another stage. Other processing stage textile production Compared to the stage in the process where the textile is treated with a peroxidase, earlier or earlier maybe later.

In certain embodiments, additional enzyme protease, lipase, xylanase, cutinase, Oxidoreductase, cellulase, is an enzyme with endoglucanase, amylase and/or nannanase activity. oxidoreductase Examples of enzymes that have laccase, perhydrolase and/or peroxidase activity are enzymes. In a preferred embodiment, the additional enzyme is laccase.

In some embodiments, the method of processing the textile product includes: (a) textile contacting the product with cellulase; (b) a peroxidase of the textile product, a hydrogen peroxide source and contact with an intermediate. In some embodiments, steps (a) and (b) There is a washing stage between them. In some embodiments, the intermediate wash stages (a) and (b) performed in a single bath without In some embodiments, (a) and (b) the same bathroom performed sequentially or simultaneously. In some embodiments, (a) and (b) a single It is performed sequentially in the bath, where (a) is performed before (b).

In some embodiments, step (a) is followed by an enzymatic degradation step. Some and/or in the presence of zwitterionic surfactant and/or dispersant.

Examples of anionic surfactants are carboxylates, sulfates, sulfonates or alkyl, substituted alkyl or aryl phosphates. Examples of nonionic surfactants polyoxyethylene compounds, for example alcohol ethoxylates, propoxylates or mixed ethoxy- /propoxylates are poly-glycerols and other polyols as well as certain block-copolymers.

Examples of cationic surfactants are water-soluble cationic polymers, e.g. quaternary ammonium sulfates and certain amines, e.g. epichlorohydrin/dimethylamine polymers (EPI-DMA) and their crosslinked solutions, polydiallyl dimethyl ammonium chloride (DADMAC), DADMAC/Acrylamide co-polymers and ionene polymers, eg US patent examples of substances are betaines, glycinates, amino propionates, imino propionates and various imidazoline derivatives. Also, US patent no. The polymers described in 5,256,252 are also can be used.

In the process according to the invention, peroxidase can be administered alone or in combination with an additional enzyme. "An addition The term "enzyme" means at least one additional enzyme, eg, one, two, three, four, five, six, seven, eight, nine, ten or it means even more additional enzymes. means applicable at the same or at another stage. Other processing stage textile production Compared to the stage in the process where the textile is treated with a peroxidase, earlier or earlier maybe later.

In certain embodiments, additional enzyme protease, lipase, xylanase, cutinase, Oxidoreductase, cellulase, is an enzyme with endoglucanase, amylase and/or nannanase activity. oxidoreductase Examples of enzymes that have laccase, perhydrolase and/or peroxidase activity are enzymes. In a preferred embodiment, the additional enzyme is laccase.

In some embodiments, the method of processing the textile product includes: (a) textile contacting the product with cellulase; (b) a peroxidase of the textile product, a hydrogen peroxide source and contact with an intermediate. In some embodiments, steps (a) and (b) There is a washing stage between them. In some embodiments, the intermediate wash stages (a) and (b) performed in a single bath without In some embodiments, (a) and (b) the same bathroom performed sequentially or simultaneously. In some embodiments, (a) and (b) a single It is performed sequentially in the bath, where (a) is performed before (b).

In some embodiments, step (a) is followed by an enzymatic degradation step. Some In embodiments, the enzymatic degeneration step is in the same bath as step (a). realizable. In some embodiments, the enzymatic descaling step is combined with steps (a) and (b). performed sequentially or simultaneously in the same bath. In some regulations, enzymatic descaling step is performed in the same bath as steps (a) and (b), sequentially, wherein the sequence of the steps is enzymatic removal, steps (a) and (b). Some In embodiments, the enzymatic descaling step is performed in a bath, followed by a bath stage and stages (a) and (b) are performed in the same bathroom.

Peroxidases are also generally used for processing, processing, finishing, polishing, fiber production or similar It can also be used in other directions in textile production, including aspects. The color of your denim In addition to changing dyed waste), fabric dyeing, textile bleaching, fiber modification, obtaining improved fiber or fabric properties, and can be used similarly.

The present composition or process also includes the pigmented color and/or colored dye in the cotton fabric. It can be applied to bleach the textile product to remove impurities. In some regulations, a peroxidase to remove pigmented color and/or colored impurities in cotton fabric hydrogen peroxide source and a vehicle application phase after the scrubbing phase is performed.

In some embodiments, the present compositions also provide a means of changing the color of the wool. can also be used in the method.

Existing compositions also allow the removal of excess ink after the dyeing/printing phase. It can also be used in a directed method. To provide stability in dyed textile products and to To prevent unwanted dye transfer during consumer washing of products, Highly soluble dyestuff that does not bind to the fiber can be removed by application.

Existing compositions can also be used in wastewater treatment. For example, peroxidases It can be used to decolorize colored compounds.

Although mainly indigo and sulphur-dyed textiles have been described, existing The methods can be applied to change the color of a textile product dyed with a large number of dyes.

Examples of dyes include, without limitation, azo, monoazo, disazo, nitro, xanthene, quinoline, anthraquinone, triarylmethane, paraazoaniline, azinoxazine, stilbene, aniline and phthalocyanine dyes or mixtures thereof. In one embodiment, the dye is an azo dye (eg, Reactive Black10). In embodiments, the enzymatic degeneration step is in the same bath as step (a). realizable. In some embodiments, the enzymatic descaling step is combined with steps (a) and (b). performed sequentially or simultaneously in the same bath. In some regulations, enzymatic descaling step is performed in the same bath as steps (a) and (b), sequentially, wherein the sequence of the steps is enzymatic removal, steps (a) and (b). Some In embodiments, the enzymatic descaling step is performed in a bath, followed by a bath stage and stages (a) and (b) are performed in the same bathroom.

Peroxidases are also generally used for processing, processing, finishing, polishing, fiber production or similar It can also be used in other directions in textile production, including aspects. The color of your denim In addition to changing dyed waste), fabric dyeing, textile bleaching, fiber modification, obtaining improved fiber or fabric properties, and can be used similarly.

The present composition or process also includes the pigmented color and/or colored dye in the cotton fabric. It can be applied to bleach the textile product to remove impurities. In some regulations, a peroxidase to remove pigmented color and/or colored impurities in cotton fabric hydrogen peroxide source and a vehicle application phase after the scrubbing phase is performed.

In some embodiments, the present compositions also provide a means of changing the color of the wool. can also be used in the method.

Existing compositions also allow the removal of excess ink after the dyeing/printing phase. It can also be used in a directed method. To provide stability in dyed textile products and to To prevent unwanted dye transfer during consumer washing of products, Highly soluble dyestuff that does not bind to the fiber can be removed by application.

Existing compositions can also be used in wastewater treatment. For example, peroxidases It can be used to decolorize colored compounds.

Although mainly indigo and sulphur-dyed textiles have been described, existing The methods can be applied to change the color of a textile product dyed with a large number of dyes.

Examples of dyes include, without limitation, azo, monoazo, disazo, nitro, xanthene, quinoline, anthraquinone, triarylmethane, paraazoaniline, azinoxazine, stilbene, aniline and phthalocyanine dyes or mixtures thereof. In one embodiment, the dye is an azo dye (eg, Reactive Black10). In embodiments, the enzymatic degeneration step is in the same bath as step (a). realizable. In some embodiments, the enzymatic descaling step is combined with steps (a) and (b). performed sequentially or simultaneously in the same bath. In some regulations, enzymatic descaling step is performed in the same bath as steps (a) and (b), sequentially, wherein the sequence of the steps is enzymatic removal, steps (a) and (b). Some In embodiments, the enzymatic descaling step is performed in a bath, followed by a bath stage and stages (a) and (b) are performed in the same bathroom.

Peroxidases are also generally used for processing, processing, finishing, polishing, fiber production or similar It can also be used in other directions in textile production, including aspects. The color of your denim In addition to changing dyed waste), fabric dyeing, textile bleaching, fiber modification, obtaining improved fiber or fabric properties, and can be used similarly.

The present composition or process also includes the pigmented color and/or colored dye in the cotton fabric. It can be applied to bleach the textile product to remove impurities. In some regulations, a peroxidase to remove pigmented color and/or colored impurities in cotton fabric hydrogen peroxide source and a vehicle application phase after the scrubbing phase is performed.

In some embodiments, the present compositions also provide a means of changing the color of the wool. can also be used in the method.

Existing compositions also allow the removal of excess ink after the dyeing/printing phase. It can also be used in a directed method. To provide stability in dyed textile products and to To prevent unwanted dye transfer during consumer washing of products, Highly soluble dyestuff that does not bind to the fiber can be removed by application.

Existing compositions can also be used in wastewater treatment. For example, peroxidases It can be used to decolorize colored compounds.

Although mainly indigo and sulphur-dyed textiles have been described, existing The methods can be applied to change the color of a textile product dyed with a large number of dyes.

Examples of dyes include, without limitation, azo, monoazo, disazo, nitro, xanthene, quinoline, anthraquinone, triarylmethane, paraazoaniline, azinoxazine, stilbene, aniline and phthalocyanine dyes or mixtures thereof. In one embodiment, the dye is an azo dye (eg, Reactive Black10). (sulfooxy)ethyl1)sulfonyl)phenyl)azo)-tetrasodium salt), Reactive Violet 5, inethyl yellow, Congo red). In some embodiments, the dye is an anthraquinone dye (eg, reinazole blue), indigo (indigo). carmine), a triarylmethane/paraazoaniline dye (pre-crystal violet, malachite green) or a sulfur-based paint. In various embodiments, the dye is a reactive, direct, disperse or pigment. is paint. In some embodiments, the dye is a component of an ink.

compositions As explained above, the present compounds are a peroxidase, a source of hydrogen peroxide, and contains an intermediate.

Such compositions also contain a peroxidase, a source of hydrogen peroxide, and an intermediate. A "off-the-shelf" (RTU) that includes, consists of, or consists primarily of may also be provided in composition form. In some embodiments, the vehicle is 1-methylvioluric acid, 1,3-dimethylvioluric acid, thioviolic acid, Violuric acid and their esters, ethers, salts] or hydrates. In some embodiments, the source of hydrogen peroxide is percarbonates, persulfates, perphosphates, peroxyacids, alkylperoxides, acylperoxides, peroxyesters, urea the peroxide is selected from perborates and peroxycarboxylic acids or salts thereof. RTU The composition may also use one or more of the following to provide a pH buffer when the composition is in solution. may contain compounds. For example, in some embodiments, the composition is phosphate buffer or adipic acid. Includes buffering system. Preferably, the adipic acid buffering system is acetic acid buffering system. system. The RTU compound is in a solid, granular form for ease of storage and transportation. it could be. The composition then obtains, for example, an aqueous solution for use as described. to be diluted with water. RTU compositions can also be used for any number of additional reactions. agent, such as dispersants, surfactants, blockers, polyiners, preservatives and may contain similar.

Determination of Peroxidase Activity (POXU) One peroxidase unit (POXU) per minute at 30°C in a mixture containing pmol is the amount of enzyme that catalyzes the conversion of hydrogen peroxide: 0.88 mM hydrogen peroxide; and The reaction is continued for 60 seconds (without stirring10) while measuring the absorbance at 418 nm. (sulfooxy)ethyl1)sulfonyl)phenyl)azo)-tetrasodium salt), Reactive Violet 5, inethyl yellow, Congo red). In some embodiments, the dye is an anthraquinone dye (eg, reinazole blue), indigo (indigo). carmine), a triarylmethane/paraazoaniline dye (pre-crystal violet, malachite green) or a sulfur-based paint. In various embodiments, the dye is a reactive, direct, disperse or pigment. is paint. In some embodiments, the dye is a component of an ink.

compositions As explained above, the present compounds are a peroxidase, a source of hydrogen peroxide, and contains an intermediate.

Such compositions also contain a peroxidase, a source of hydrogen peroxide, and an intermediate. A "off-the-shelf" (RTU) that includes, consists of, or consists primarily of may also be provided in composition form. In some embodiments, the vehicle is 1-methylvioluric acid, 1,3-dimethylvioluric acid, thioviolic acid, Violuric acid and their esters, ethers, salts] or hydrates. In some embodiments, the source of hydrogen peroxide is percarbonates, persulfates, perphosphates, peroxyacids, alkylperoxides, acylperoxides, peroxyesters, urea the peroxide is selected from perborates and peroxycarboxylic acids or salts thereof. RTU The composition may also use one or more of the following to provide a pH buffer when the composition is in solution. may contain compounds. For example, in some embodiments, the composition is phosphate buffer or adipic acid. Includes buffering system. Preferably, the adipic acid buffering system is acetic acid buffering system. system. The RTU compound is in a solid, granular form for ease of storage and transportation. it could be. The composition then obtains, for example, an aqueous solution for use as described. to be diluted with water. RTU compositions can also be used for any number of additional reactions. agent, such as dispersants, surfactants, blockers, polyiners, preservatives and may contain similar.

Determination of Peroxidase Activity (POXU) One peroxidase unit (POXU) per minute at 30°C in a mixture containing pmol is the amount of enzyme that catalyzes the conversion of hydrogen peroxide: 0.88 mM hydrogen peroxide; and The reaction is continued for 60 seconds (without stirring10) while measuring the absorbance at 418 nm. (sulfooxy)ethyl1)sulfonyl)phenyl)azo)-tetrasodium salt), Reactive Violet 5, inethyl yellow, Congo red). In some embodiments, the dye is an anthraquinone dye (eg, reinazole blue), indigo (indigo). carmine), a triarylmethane/paraazoaniline dye (pre-crystal violet, malachite green) or a sulfur-based paint. In various embodiments, the dye is a reactive, direct, disperse or pigment. is paint. In some embodiments, the dye is a component of an ink.

compositions As explained above, the present compounds are a peroxidase, a source of hydrogen peroxide, and contains an intermediate.

Such compositions also contain a peroxidase, a source of hydrogen peroxide, and an intermediate. A "off-the-shelf" (RTU) that includes, consists of, or consists primarily of may also be provided in composition form. In some embodiments, the vehicle is 1-methylvioluric acid, 1,3-dimethylvioluric acid, thioviolic acid, Violuric acid and their esters, ethers, salts] or hydrates. In some embodiments, the source of hydrogen peroxide is percarbonates, persulfates, perphosphates, peroxyacids, alkylperoxides, acylperoxides, peroxyesters, urea the peroxide is selected from perborates and peroxycarboxylic acids or salts thereof. RTU The composition may also use one or more of the following to provide a pH buffer when the composition is in solution. may contain compounds. For example, in some embodiments, the composition is phosphate buffer or adipic acid. Includes buffering system. Preferably, the adipic acid buffering system is acetic acid buffering system. system. The RTU compound is in a solid, granular form for ease of storage and transportation. it could be. The composition then obtains, for example, an aqueous solution for use as described. to be diluted with water. RTU compositions can also be used for any number of additional reactions. agent, such as dispersants, surfactants, blockers, polyiners, preservatives and may contain similar.

Determination of Peroxidase Activity (POXU) One peroxidase unit (POXU) per minute at 30°C in a mixture containing pmol is the amount of enzyme that catalyzes the conversion of hydrogen peroxide: 0.88 mM hydrogen peroxide; and The reaction is continued for 60 seconds (without stirring10) while measuring the absorbance at 418 nm. An absorption coefficient of oxidized ABTS of cm'1 and two µmol of oxidized ABTS per It is calculated using a converted amo] 11202 stoichiometry. EXAMPLES Materials and Methods Amino acid sequence of Coprinus cinereus peroxidazine (CiP) as SEQ ID No:1 is shown.

The amino acid sequence of soybean peroxidazine (SBP) is shown as SEQ ID NO:2.

The amino acid sequence of Myceliophthora thermophila laccase (MtL) is in WO95/33536, sequence number 2 is shown as.

Cellusoft L® (a Trichoderma reesei multi-component cellulase product, available from Novozymes A/S possible) Denimax® Core 1380 S (an enzyme product containing cellulase and alpha-amylase, from Novozymes A/S available) VA: violuric acid HOBT: 1-hydroxy-benzotriazole MS: Methylsyringate Color Measurement The bleaching level in denim samples is pre-calibrated with the DataColor SF450X. determined by measuring reflectivity, alternatively an equivalent tool can be used. Each Four readings were taken for the sample and the average of the readings was used. agartina level CIE L* index on the blue side (front side) of the sample and CIE b* on the back side of the sample evaluated with the index.

L* indicates color change in white/black on a scale of 0 to 100 and a decrease in L* means an increase in black (decrease in white), while an increase in L* indicates an increase in white. means an increase (decrease in black). Delta L* unit = treated with a specific enzyme sample fabric L* value - sample fabric L* value before enzyme treatment. Delta L* the larger the unit, the brighter and/or whiter the denim is, hence the bleaching level. as high as 0 (front a Delta L* unit with 6 is higher than a Delta L* unit with 4 has a bleaching level).10 An absorption coefficient of oxidized ABTS of cm'1 and two µmol of oxidized ABTS per It is calculated using a converted amo] 11202 stoichiometry. EXAMPLES Materials and Methods Amino acid sequence of Coprinus cinereus peroxidazine (CiP) as SEQ ID No:1 is shown.

The amino acid sequence of soybean peroxidazine (SBP) is shown as SEQ ID NO:2.

The amino acid sequence of Myceliophthora thermophila laccase (MtL) is in WO95/33536, sequence number 2 is shown as.

Cellusoft L® (a Trichoderma reesei multi-component cellulase product, available from Novozymes A/S possible) Denimax® Core 1380 S (an enzyme product containing cellulase and alpha-amylase, from Novozymes A/S available) VA: violuric acid HOBT: 1-hydroxy-benzotriazole MS: Methylsyringate Color Measurement The bleaching level in denim samples is pre-calibrated with the DataColor SF450X. determined by measuring reflectivity, alternatively an equivalent tool can be used. Each Four readings were taken for the sample and the average of the readings was used. agartina level CIE L* index on the blue side (front side) of the sample and CIE b* on the back side of the sample evaluated with the index.

L* indicates color change in white/black on a scale of 0 to 100 and a decrease in L* means an increase in black (decrease in white), while an increase in L* indicates an increase in white. means an increase (decrease in black). Delta L* unit = treated with a specific enzyme sample fabric L* value - sample fabric L* value before enzyme treatment. Delta L* the larger the unit, the brighter and/or whiter the denim is, hence the bleaching level. as high as 0 (front a Delta L* unit with 6 is higher than a Delta L* unit with 4 has a bleaching level).10 An absorption coefficient of oxidized ABTS of cm'1 and two µmol of oxidized ABTS per It is calculated using a converted amo] 11202 stoichiometry. EXAMPLES Materials and Methods Amino acid sequence of Coprinus cinereus peroxidazine (CiP) as SEQ ID No:1 is shown.

The amino acid sequence of soybean peroxidazine (SBP) is shown as SEQ ID NO:2.

The amino acid sequence of Myceliophthora thermophila laccase (MtL) is in WO95/33536, sequence number 2 is shown as.

Cellusoft L® (a Trichoderma reesei multi-component cellulase product, available from Novozymes A/S possible) Denimax® Core 1380 S (an enzyme product containing cellulase and alpha-amylase, from Novozymes A/S available) VA: violuric acid HOBT: 1-hydroxy-benzotriazole MS: Methylsyringate Color Measurement The bleaching level in denim samples is pre-calibrated with the DataColor SF450X. determined by measuring reflectivity, alternatively an equivalent tool can be used. Each Four readings were taken for the sample and the average of the readings was used. agartina level CIE L* index on the blue side (front side) of the sample and CIE b* on the back side of the sample evaluated with the index.

L* indicates color change in white/black on a scale of 0 to 100 and a decrease in L* means an increase in black (decrease in white), while an increase in L* indicates an increase in white. means an increase (decrease in black). Delta L* unit = treated with a specific enzyme sample fabric L* value - sample fabric L* value before enzyme treatment. Delta L* the larger the unit, the brighter and/or whiter the denim is, hence the bleaching level. as high as 0 (front a Delta L* unit with 6 is higher than a Delta L* unit with 4 has a bleaching level).10 The b* value indicates the color change in blue/yellow, and a decrease in the b* value shows the blue An increase in b* means an increase in color (decrease in yellow), while an increase in b* means increase (decrease in blue). Delta b* unit : treated with a specific enzyme sample fabric b* value - sample fabric b* value before enzyme treatment. delta b* the larger the unit, the brighter and/or whiter the back of the denim is, so the back The bleaching level on the side is as high as 0 (eg, a Delta b* unit of 3 is a Delta b* unit of 1) unit has a higher bleaching level).

Protein Content BCATM Protein Analysis Kit according to the enzyme protein product guide in an enzyme product (product no 23225, available from Therrno Fisher Scientific Inc.). Example 1: Color change with CiP/VA in Launder-O-meter at different dosages Coprinus cinereus peroxidase / violuric acid, including agartina level at different dosages (CiP/VA) effects on denim were tested in the Launder-O-Meter (SDL-Atlas LP2).

After etching, the denim was cut 16 cm wide and 27 cm long. Denim A pipe with a height of 12.5 cm and a weight of approximately 22 g was formed by suturing.

After placing the pipes in a conditioned environment (65% RH, 20°C) for 24 hours numbered, weighed with analytical balance and recorded. Each conditioned pipe It was placed in a 200 ml beaker with the blue side facing east. For each beaker, 30 large hazelnuts (MIO M-SR-A4-80, acid resistant), 10 small hazelnuts (M6 M-SR-A4-80, acid resistant) Mechanical supports were provided using Cowie, Schweiz, Bie & Bemtsen).

Then buffer (50 mM sodium acetate) according to the calculation of actual fabric weights. buffer, pH=5.0) and peroxidase and vehicle added according to Table 1, liquid/fabric The total volume was brought to around 176 m1 so that the ratio was 8:1 (v/W ml/g). reaction H2O2 was added to the solution according to Table 1 to start the solution.

Meanwhile, the Launder-O-Meter (LOM) machine was started after the required program was selected. and stopped when the temperature reached 55°C. With 2 neoprene seals per beaker A coated cover is fitted and tightly closed with a metal clamping tool. beakers loaded into the preheated LOM. 6 in horizontal position at each of the 4 drum positions Metal racks are used to store and fix the beaker. LOM cover closed and the washing program was continued and the time was started.10 The b* value indicates the color change in blue/yellow, and a decrease in the b* value shows the blue An increase in b* means an increase in color (decrease in yellow), while an increase in b* means increase (decrease in blue). Delta b* unit : treated with a specific enzyme sample fabric b* value - sample fabric b* value before enzyme treatment. delta b* the larger the unit, the brighter and/or whiter the back of the denim is, so the back The bleaching level on the side is as high as 0 (eg, a Delta b* unit of 3 is a Delta b* unit of 1) unit has a higher bleaching level).

Protein Content BCATM Protein Analysis Kit according to the enzyme protein product guide in an enzyme product (product no 23225, available from Therrno Fisher Scientific Inc.). Example 1: Color change with CiP/VA in Launder-O-meter at different dosages Coprinus cinereus peroxidase / violuric acid, including agartina level at different dosages (CiP/VA) effects on denim were tested in the Launder-O-Meter (SDL-Atlas LP2).

After etching, the denim was cut 16 cm wide and 27 cm long. Denim A pipe with a height of 12.5 cm and a weight of approximately 22 g was formed by suturing.

After placing the pipes in a conditioned environment (65% RH, 20°C) for 24 hours numbered, weighed with analytical balance and recorded. Each conditioned pipe It was placed in a 200 ml beaker with the blue side facing east. For each beaker, 30 large hazelnuts (MIO M-SR-A4-80, acid resistant), 10 small hazelnuts (M6 M-SR-A4-80, acid resistant) Mechanical supports were provided using Cowie, Schweiz, Bie & Bemtsen).

Then buffer (50 mM sodium acetate) according to the calculation of actual fabric weights. buffer, pH=5.0) and peroxidase and vehicle added according to Table 1, liquid/fabric The total volume was brought to around 176 m1 so that the ratio was 8:1 (v/W ml/g). reaction H2O2 was added to the solution according to Table 1 to start the solution.

Meanwhile, the Launder-O-Meter (LOM) machine was started after the required program was selected. and stopped when the temperature reached 55°C. With 2 neoprene seals per beaker A coated cover is fitted and tightly closed with a metal clamping tool. beakers loaded into the preheated LOM. 6 in horizontal position at each of the 4 drum positions Metal racks are used to store and fix the beaker. LOM cover closed and the washing program was continued and the time was started.10 The b* value indicates the color change in blue/yellow, and a decrease in the b* value shows the blue An increase in b* means an increase in color (decrease in yellow), while an increase in b* means increase (decrease in blue). Delta b* unit : treated with a specific enzyme sample fabric b* value - sample fabric b* value before enzyme treatment. delta b* the larger the unit, the brighter and/or whiter the back of the denim is, so the back The bleaching level on the side is as high as 0 (eg, a Delta b* unit of 3 is a Delta b* unit of 1) unit has a higher bleaching level).

Protein Content BCATM Protein Analysis Kit according to the enzyme protein product guide in an enzyme product (product no 23225, available from Therrno Fisher Scientific Inc.). Example 1: Color change with CiP/VA in Launder-O-meter at different dosages Coprinus cinereus peroxidase / violuric acid, including agartina level at different dosages (CiP/VA) effects on denim were tested in the Launder-O-Meter (SDL-Atlas LP2).

After etching, the denim was cut 16 cm wide and 27 cm long. Denim A pipe with a height of 12.5 cm and a weight of approximately 22 g was formed by suturing.

After placing the pipes in a conditioned environment (65% RH, 20°C) for 24 hours numbered, weighed with analytical balance and recorded. Each conditioned pipe It was placed in a 200 ml beaker with the blue side facing east. For each beaker, 30 large hazelnuts (MIO M-SR-A4-80, acid resistant), 10 small hazelnuts (M6 M-SR-A4-80, acid resistant) Mechanical supports were provided using Cowie, Schweiz, Bie & Bemtsen).

Then buffer (50 mM sodium acetate) according to the calculation of actual fabric weights. buffer, pH=5.0) and peroxidase and vehicle added according to Table 1, liquid/fabric The total volume was brought to around 176 m1 so that the ratio was 8:1 (v/W ml/g). reaction H2O2 was added to the solution according to Table 1 to start the solution.

Meanwhile, the Launder-O-Meter (LOM) machine was started after the required program was selected. and stopped when the temperature reached 55°C. With 2 neoprene seals per beaker A coated cover is fitted and tightly closed with a metal clamping tool. beakers loaded into the preheated LOM. 6 in horizontal position at each of the 4 drum positions Metal racks are used to store and fix the beaker. LOM cover closed and the washing program was continued and the time was started.10 minutes (min), all beakers were removed and the denim samples were sampled for 10 minutes at 85°C. time, it was transferred to the passivation solution (2 g/L sodium carbonate). then sample fabrics (ie denim) were rinsed 2 times in hot water and 2 times in cold water. Denim samples were dried in the drum (machine AEG, L-AVATHERM 37700, Germany) and After the samples were conditioned for 24 hours at 20°C, 65% relative humidity, they were evaluated. has been taken.

The bleaching level in denim samples is pre-calibrated with the DataColor SF450X. The reflectivity was determined by measuring. Four readings were taken for each sample. Dawning level is CIE L* index on the blue side of the sample and CIE b* on the back side of the sample evaluated with the index. 4 readings per fabric, for both L* and b* performed and the average of four readings was used.

Cip/VA system untreated group (without added CiP, VA and H202) and control group (H202 a surprisingly high increase in bleaching level (higher Delta L*) compared to and Delta b* units). As shown in Table 1, the optimum for CiP, VA and 11202 dosages are 0.015 mg enzyme protein/g fabric, 0.5 mM/L and 0.05 g/L, respectively. coprinus The cinereus peroxidase and violuric acid (CiP/VA) system did not increase the level of agar on both sides. It works well over a wide dosage range by increasing

Table 1. Bleach level results with CiP/VA system at different dosages (55°C, pH 5.0, minute) denim fabrics CiP (mg enzyme protein/g denim) VA (mM/L) 11202 (g/L) Delta L* Delta 1)* 0.25 0.1 0.10 4.33 1.79 minutes (min), all beakers were removed and the denim samples were sampled for 10 minutes at 85°C. time, it was transferred to the passivation solution (2 g/L sodium carbonate). then sample fabrics (ie denim) were rinsed 2 times in hot water and 2 times in cold water. Denim samples were dried in the drum (machine AEG, L-AVATHERM 37700, Germany) and After the samples were conditioned for 24 hours at 20°C, 65% relative humidity, they were evaluated. has been taken.

The bleaching level in denim samples is pre-calibrated with the DataColor SF450X. The reflectivity was determined by measuring. Four readings were taken for each sample. Dawning level is CIE L* index on the blue side of the sample and CIE b* on the back side of the sample evaluated with the index. 4 readings per fabric, for both L* and b* performed and the average of four readings was used.

Cip/VA system untreated group (without added CiP, VA and H202) and control group (H202 a surprisingly high increase in bleaching level (higher Delta L*) compared to and Delta b* units). As shown in Table 1, the optimum for CiP, VA and 11202 dosages are 0.015 mg enzyme protein/g fabric, 0.5 mM/L and 0.05 g/L, respectively. coprinus The cinereus peroxidase and violuric acid (CiP/VA) system did not increase the level of agar on both sides. It works well over a wide dosage range by increasing

Table 1. Bleach level results with CiP/VA system at different dosages (55°C, pH 5.0, minute) denim fabrics CiP (mg enzyme protein/g denim) VA (mM/L) 11202 (g/L) Delta L* Delta 1)* 0.25 0.1 0.10 4.33 1.79 minutes (min), all beakers were removed and the denim samples were sampled for 10 minutes at 85°C. time, it was transferred to the passivation solution (2 g/L sodium carbonate). then sample fabrics (ie denim) were rinsed 2 times in hot water and 2 times in cold water. Denim samples were dried in the drum (machine AEG, L-AVATHERM 37700, Germany) and After the samples were conditioned for 24 hours at 20°C, 65% relative humidity, they were evaluated. has been taken.

The bleaching level in denim samples is pre-calibrated with the DataColor SF450X. The reflectivity was determined by measuring. Four readings were taken for each sample. Dawning level is CIE L* index on the blue side of the sample and CIE b* on the back side of the sample evaluated with the index. 4 readings per fabric, for both L* and b* performed and the average of four readings was used.

Cip/VA system untreated group (without added CiP, VA and H202) and control group (H202 a surprisingly high increase in bleaching level (higher Delta L*) compared to and Delta b* units). As shown in Table 1, the optimum for CiP, VA and 11202 dosages are 0.015 mg enzyme protein/g fabric, 0.5 mM/L and 0.05 g/L, respectively. coprinus The cinereus peroxidase and violuric acid (CiP/VA) system did not increase the level of agar on both sides. It works well over a wide dosage range by increasing

Table 1. Bleach level results with CiP/VA system at different dosages (55°C, pH 5.0, minute) denim fabrics CiP (mg enzyme protein/g denim) VA (mM/L) 11202 (g/L) Delta L* Delta 1)* 0.25 0.1 0.10 4.33 1.79 CiP (mg enzyme protein/g denim) VA (mM/L) Note: average of two samples for each dosage.

H2O2 (g/L) denim fabrics Delta L* Delta b* 12.90 Example 2: Color change with CiP/VA in LOM under different reaction conditions Effects of CiP/VA on denim with the same protocol as in Example 1 shown in Table 2 tested under reaction conditions. CiP dosage 0.015 mg enzyme protein/g fabric, VA 0.5 mM/L and HZOZ 0.05 g/L. 50 mM as pH=4 and pH=5 buffers 50 mM phosphate buffer was used as sodium acetate buffer, pH:6 and pH:7. untreated group (CiP, VA and H2O2 not added) and control group (0.] g/l H2O2 added) pH was carried out at 55°C for 30 minutes.

As shown in Table 2, the CiP/VA system has a wide temperature range (25 to 65°C) and 4 to 65°C. It can be concluded that it exhibits activity within the pH range of 7. as low as 25°C to 45°C It works better at temperatures. The reaction rate of CiP/VA is the main one that ends in the first 10 minutes. It is very fast with its bleaching effect.

Table 2. Bleaching level results with CiP/VA system at different pH, temperature and time pH Temperature (°C) Time (min) denim fabrics Delta L* delta b* CiP (mg enzyme protein/g denim) VA (mM/L) Note: average of two samples for each dosage.

H2O2 (g/L) denim fabrics Delta L* Delta b* 12.90 Example 2: Color change with CiP/VA in LOM under different reaction conditions Effects of CiP/VA on denim with the same protocol as in Example 1 shown in Table 2 tested under reaction conditions. CiP dosage 0.015 mg enzyme protein/g fabric, VA 0.5 mM/L and HZOZ 0.05 g/L. 50 mM as pH=4 and pH=5 buffers 50 mM phosphate buffer was used as sodium acetate buffer, pH:6 and pH:7. untreated group (CiP, VA and H2O2 not added) and control group (0.] g/l H2O2 added) pH was carried out at 55°C for 30 minutes.

As shown in Table 2, the CiP/VA system has a wide temperature range (25 to 65°C) and 4 to 65°C. It can be concluded that it exhibits activity within the pH range of 7. as low as 25°C to 45°C It works better at temperatures. The reaction rate of CiP/VA is the main one that ends in the first 10 minutes. It is very fast with its bleaching effect.

Table 2. Bleaching level results with CiP/VA system at different pH, temperature and time pH Temperature (°C) Time (min) denim fabrics Delta L* delta b* CiP (mg enzyme protein/g denim) VA (mM/L) Note: average of two samples for each dosage.

H2O2 (g/L) denim fabrics Delta L* Delta b* 12.90 Example 2: Color change with CiP/VA in LOM under different reaction conditions Effects of CiP/VA on denim with the same protocol as in Example 1 shown in Table 2 tested under reaction conditions. CiP dosage 0.015 mg enzyme protein/g fabric, VA 0.5 mM/L and HZOZ 0.05 g/L. 50 mM as pH=4 and pH=5 buffers 50 mM phosphate buffer was used as sodium acetate buffer, pH:6 and pH:7. untreated group (CiP, VA and H2O2 not added) and control group (0.] g/l H2O2 added) pH was carried out at 55°C for 30 minutes.

As shown in Table 2, the CiP/VA system has a wide temperature range (25 to 65°C) and 4 to 65°C. It can be concluded that it exhibits activity within the pH range of 7. as low as 25°C to 45°C It works better at temperatures. The reaction rate of CiP/VA is the main one that ends in the first 10 minutes. It is very fast with its bleaching effect.

Table 2. Bleaching level results with CiP/VA system at different pH, temperature and time pH Temperature (°C) Time (min) denim fabrics Delta L* delta b* denim fabrics pH Temperature (OC) Time (min) Delta L* Delta b* 4 11:00 3.32 10.75 3.77 6 5.79 1.01 7 2.54 0.68 11.05 1.17 1 1.13 2.89 55 9.24 3.42 65 7.09 3.66 8.59 2.91 8.79 2.74 9.31 2.44 60 9.98 1.72 Unprocessed Group 0.55 0.02 Control Group 0.58 0.09 Note: average of two samples for each condition. Example 3: When changing the color of denim in LOM, it is necessary to first combine CiP/VA with products. comparison data The performances of CIP/VA, CiP/HOBT, SBP/VA and MtL/MeS are the same as in Example 1. tested under the reaction conditions shown in Table 3 with the protocol. Processing time in this example is set to minutes. 50 mM sodium acetate buffer and pH=6.5 as pH=5 buffer 50 mM phosphate buffer was used.

denim fabrics pH Temperature (OC) Time (min) Delta L* Delta b* 4 11:00 3.32 10.75 3.77 6 5.79 1.01 7 2.54 0.68 11.05 1.17 1 1.13 2.89 55 9.24 3.42 65 7.09 3.66 8.59 2.91 8.79 2.74 9.31 2.44 60 9.98 1.72 Unprocessed Group 0.55 0.02 Control Group 0.58 0.09 Note: average of two samples for each condition. Example 3: When changing the color of denim in LOM, it is necessary to first combine CiP/VA with products. comparison data The performances of CIP/VA, CiP/HOBT, SBP/VA and MtL/MeS are the same as in Example 1. tested under the reaction conditions shown in Table 3 with the protocol. Processing time in this example is set to minutes. 50 mM sodium acetate buffer and pH=6.5 as pH=5 buffer 50 mM phosphate buffer was used.

denim fabrics pH Temperature (OC) Time (min) Delta L* Delta b* 4 11:00 3.32 10.75 3.77 6 5.79 1.01 7 2.54 0.68 11.05 1.17 1 1.13 2.89 55 9.24 3.42 65 7.09 3.66 8.59 2.91 8.79 2.74 9.31 2.44 60 9.98 1.72 Unprocessed Group 0.55 0.02 Control Group 0.58 0.09 Note: average of two samples for each condition. Example 3: When changing the color of denim in LOM, it is necessary to first combine CiP/VA with products. comparison data The performances of CIP/VA, CiP/HOBT, SBP/VA and MtL/MeS are the same as in Example 1. tested under the reaction conditions shown in Table 3 with the protocol. Processing time in this example is set to minutes. 50 mM sodium acetate buffer and pH=6.5 as pH=5 buffer 50 mM phosphate buffer was used.

As shown in Table 3, both hein CiP (SEQ ID No:1) and SBP (SEQ ID No:2) increases the bleaching effect. Compared to the product on the market (CiP/HOBT), CiP/VA or SBP/VA system higher bleach level (higher Delta L* unit and higher With a high Delta b*), it is more efficient than the CiP/HOBT system. For color changing VA is superior to HOBT in the peroxidase/mediator system.

As shown in Table 3, CiP/VA or SBP/VA systems are commercially available. In terms of bleaching level compared to the lakkaZ/intermediate system (MtL/MeS) system is performing well.

Table 3: CiP/V A and different enzyme/medium on denim bleaching in LOM results of systems Enzyme/vehicle Wash . . Tool inaddition H202 Enzyme dosage. . substance conditions dosage dosage CiP/VA 0.5 mM/L 6.71 2.27 CiP/HOBT 0.5 mM/L 1.86 0.3 55°C, pH=5.0, 0.015 mg/g min denim fabric SBPNA 0.5 mM/L 6.12 1.56 MtL/MeS 0.5 mM/L 5.32 1.45 Note: average of two samples for each condition. Example 4: Color with CiP/VA in combination with cellulase in a bath in LOM changing Normally, the etching and bleaching processes are carried out in two different treatment baths. Although it is a separate process, etching and bleaching process combined in one-bath denim The etching and bleaching phase is carried out in the same bath without straining and rinsing. indicates that it should be carried out in stages. In this example, after drying the denim normal abrasive rinsing, where the bleach is then carried out in another bath and bleaching treatments were used as control.

Denim etching stage: Denim fabric after desizing as described in Example 1 cut to the same size and tubular and placed in a LOM beaker with the same nuts As shown in Table 3, both hein CiP (SEQ ID No:1) and SBP (SEQ ID No:2) increases the bleaching effect. Compared to the product on the market (CiP/HOBT), CiP/VA or SBP/VA system higher bleach level (higher Delta L* unit and higher With a high Delta b*), it is more efficient than the CiP/HOBT system. For color changing VA is superior to HOBT in the peroxidase/mediator system.

As shown in Table 3, CiP/VA or SBP/VA systems are commercially available. In terms of bleaching level compared to the lakkaZ/intermediate system (MtL/MeS) system is performing well.

Table 3: CiP/V A and different enzyme/medium on denim bleaching in LOM results of systems Enzyme/vehicle Wash . . Tool inaddition H202 Enzyme dosage. . substance conditions dosage dosage CiP/VA 0.5 mM/L 6.71 2.27 CiP/HOBT 0.5 mM/L 1.86 0.3 55°C, pH=5.0, 0.015 mg/g min denim fabric SBPNA 0.5 mM/L 6.12 1.56 MtL/MeS 0.5 mM/L 5.32 1.45 Note: average of two samples for each condition. Example 4: Color with CiP/VA in combination with cellulase in a bath in LOM changing Normally, the etching and bleaching processes are carried out in two different treatment baths. Although it is a separate process, etching and bleaching process combined in one-bath denim The etching and bleaching phase is carried out in the same bath without straining and rinsing. indicates that it should be carried out in stages. In this example, after drying the denim normal abrasive rinsing, where the bleach is then carried out in another bath and bleaching treatments were used as control.

Denim etching stage: Denim fabric after desizing as described in Example 1 cut to the same size and tubular and placed in a LOM beaker with the same nuts As shown in Table 3, both hein CiP (SEQ ID No:1) and SBP (SEQ ID No:2) increases the bleaching effect. Compared to the product on the market (CiP/HOBT), CiP/VA or SBP/VA system higher bleach level (higher Delta L* unit and higher With a high Delta b*), it is more efficient than the CiP/HOBT system. For color changing VA is superior to HOBT in the peroxidase/mediator system.

As shown in Table 3, CiP/VA or SBP/VA systems are commercially available. In terms of bleaching level compared to the lakkaZ/intermediate system (MtL/MeS) system is performing well.

Table 3: CiP/V A and different enzyme/medium on denim bleaching in LOM results of systems Enzyme/vehicle Wash . . Tool inaddition H202 Enzyme dosage. . substance conditions dosage dosage CiP/VA 0.5 mM/L 6.71 2.27 CiP/HOBT 0.5 mM/L 1.86 0.3 55°C, pH=5.0, 0.015 mg/g min denim fabric SBPNA 0.5 mM/L 6.12 1.56 MtL/MeS 0.5 mM/L 5.32 1.45 Note: average of two samples for each condition. Example 4: Color with CiP/VA in combination with cellulase in a bath in LOM changing Normally, the etching and bleaching processes are carried out in two different treatment baths. Although it is a separate process, etching and bleaching process combined in one-bath denim The etching and bleaching phase is carried out in the same bath without straining and rinsing. indicates that it should be carried out in stages. In this example, after drying the denim normal abrasive rinsing, where the bleach is then carried out in another bath and bleaching treatments were used as control.

Denim etching stage: Denim fabric after desizing as described in Example 1 cut to the same size and tubular and placed in a LOM beaker with the same nuts has been placed. Then, according to the calculation of the actual fabric weights, the liquid/fabric buffer (50 mM sodium acetate buffer, pH=5.0), such that the ratio is 8:] (w/v ml/g). The cellulase product (Cellusoft® L) was added according to Table 4. beakers to preheated LOM is loaded. Etching was then started at 55°C in the LOM and in Example 1 at paragraph 3 performed as described. Forty minutes later, all beakers are in different baths or in the same removed from the LOM for the next bleaching step in the bath.

Control treatment (bleaching in a different bath than the etching bath): Control fabric sample For this, the etching bath was drained and the fabric sample was washed 2 times in hot water and 2 times in cold water. rinsed. The fabric sample was then reused in Example 1 as described in paragraph 2. It was placed in a beaker with hazelnuts. Next, buffer (50 mM sodium acetate buffer, pH=5.0) followed by peroxidase, vehicle and H2O2 Liquid/fabric ratio according to Table 4 821 (w/v, ml/g). Reload and wash program per LOM For the bleaching step, it was continued at 55°C for 30 minutes.

Combined process (etching and bleaching in the same bath): Combined process for sample fabrics, peroxidase, medium and H2O2 directly according to Table 4 beakers added to the etching bath containing The beakers were reloaded into the LOM and washed. The program was continued at 55°C for 30 minutes for the bleaching phase.

After the bleaching step in both the control process and the combined process, all beakers removed and the denim samples were placed in the passivation solution (2 g/L) for 10 minutes at 85°C. sodium carbonate) was transferred. Then, the sample fabrics were washed twice in hot water and cold. rinsed in water 2 times. Denim samples were drum-dried, conditioned and The bleaching level was evaluated in the same way as described in Example 1.

Table 4, two to three times the dosage used for the CiP/VA/H202 system dosage control process When between shows that it can be achieved. Example, combined etching of the CiP/VA/H202 system in a bath and shows that it is suitable for use in the bleaching process.

Table 4. Results of combined single-bath treatment with Cellusoft® L and CiP/V A in LOM Cellusoft® L, % CiP, mg enzyme V A, H2O2, umas ar L* 13* has been placed. Then, according to the calculation of the actual fabric weights, the liquid/fabric buffer (50 mM sodium acetate buffer, pH=5.0), such that the ratio is 8:] (w/v ml/g). The cellulase product (Cellusoft® L) was added according to Table 4. beakers to preheated LOM is loaded. Etching was then started at 55°C in the LOM and in Example 1 at paragraph 3 performed as described. Forty minutes later, all beakers are in different baths or in the same removed from the LOM for the next bleaching step in the bath.

Control treatment (bleaching in a different bath than the etching bath): Control fabric sample For this, the etching bath was drained and the fabric sample was washed 2 times in hot water and 2 times in cold water. rinsed. The fabric sample was then reused in Example 1 as described in paragraph 2. It was placed in a beaker with hazelnuts. Next, buffer (50 mM sodium acetate buffer, pH=5.0) followed by peroxidase, vehicle and H2O2 Liquid/fabric ratio according to Table 4 821 (w/v, ml/g). Reload and wash program per LOM For the bleaching step, it was continued at 55°C for 30 minutes.

Combined process (etching and bleaching in the same bath): Combined process for sample fabrics, peroxidase, medium and H2O2 directly according to Table 4 beakers added to the etching bath containing The beakers were reloaded into the LOM and washed. The program was continued at 55°C for 30 minutes for the bleaching phase.

After the bleaching step in both the control process and the combined process, all beakers removed and the denim samples were placed in the passivation solution (2 g/L) for 10 minutes at 85°C. sodium carbonate) was transferred. Then, the sample fabrics were washed twice in hot water and cold. rinsed in water 2 times. Denim samples were drum-dried, conditioned and The bleaching level was evaluated in the same way as described in Example 1.

Table 4, two to three times the dosage used for the CiP/VA/H202 system dosage control process When between shows that it can be achieved. Example, combined etching of the CiP/VA/H202 system in a bath and shows that it is suitable for use in the bleaching process.

Table 4. Results of combined single-bath treatment with Cellusoft® L and CiP/V A in LOM Cellusoft® L, % CiP, mg enzyme V A, H2O2, umas ar L* 13* has been placed. Then, according to the calculation of the actual fabric weights, the liquid/fabric buffer (50 mM sodium acetate buffer, pH=5.0), such that the ratio is 8:] (w/v ml/g). The cellulase product (Cellusoft® L) was added according to Table 4. beakers to preheated LOM is loaded. Etching was then started at 55°C in the LOM and in Example 1 at paragraph 3 performed as described. Forty minutes later, all beakers are in different baths or in the same removed from the LOM for the next bleaching step in the bath.

Control treatment (bleaching in a different bath than the etching bath): Control fabric sample For this, the etching bath was drained and the fabric sample was washed 2 times in hot water and 2 times in cold water. rinsed. The fabric sample was then reused in Example 1 as described in paragraph 2. It was placed in a beaker with hazelnuts. Next, buffer (50 mM sodium acetate buffer, pH=5.0) followed by peroxidase, vehicle and H2O2 Liquid/fabric ratio according to Table 4 821 (w/v, ml/g). Reload and wash program per LOM For the bleaching step, it was continued at 55°C for 30 minutes.

Combined process (etching and bleaching in the same bath): Combined process for sample fabrics, peroxidase, medium and H2O2 directly according to Table 4 beakers added to the etching bath containing The beakers were reloaded into the LOM and washed. The program was continued at 55°C for 30 minutes for the bleaching phase.

After the bleaching step in both the control process and the combined process, all beakers removed and the denim samples were placed in the passivation solution (2 g/L) for 10 minutes at 85°C. sodium carbonate) was transferred. Then, the sample fabrics were washed twice in hot water and cold. rinsed in water 2 times. Denim samples were drum-dried, conditioned and The bleaching level was evaluated in the same way as described in Example 1.

Table 4, two to three times the dosage used for the CiP/VA/H202 system dosage control process When between shows that it can be achieved. Example, combined etching of the CiP/VA/H202 system in a bath and shows that it is suitable for use in the bleaching process.

Table 4. Results of combined single-bath treatment with Cellusoft® L and CiP/V A in LOM Cellusoft® L, % CiP, mg enzyme V A, H2O2, umas ar L* 13* . . fabrics . Cellusoft® L, % CiP, mg enzyme VA, H2O2, denim weight protein/ g denim mM/L g/L Unified Note: the average of two samples for each combination. Example 5: With CiP/VA in combination with descaling and etching in a bath color change The single-bath combined process in this example is in the same bath without straining and rinsing. It refers to the realization of denim removal, abrasion and bleaching. In this example, In the control process, descaling and etching must be carried out simultaneously in the same bath. is performed, then the denim fabric sample is rinsed and the bleaching is then carried out in another The descaling and etching stage, in order to provide sufficient mechanical action for the process, It was carried out in WASCATOR (Electrolux, Switzerland). WASCATOR 7kg fabric capacity, controlled by a microprocessor-based program control unit, more than LOM it is a washer extractor that creates a high mechanical effect, hence denim enough that the sizing agent in the fabric can be easily removed with the aid of amylase. ready fabric is provided for the next bleaching stage with its stripping and abrasive effects. 1 kg The denim pipe is loaded into WASCATOR and the washing program is run as follows: Pre- 25°C, 5 min; liquid/fabric ratio is 1521 (v/w).

Main Enzyme product Denimax® Core 1380 S containing both alpha-amylase and cellulase washing is added according to Table 5; 50°C, 85 minutes; liquid/fabric ratio 10:] (v/w); bath pH 6.5 under test conditions. . . fabrics . Cellusoft® L, % CiP, mg enzyme VA, H2O2, denim weight protein/ g denim mM/L g/L Unified Note: the average of two samples for each combination. Example 5: With CiP/VA in combination with descaling and etching in a bath color change The single-bath combined process in this example is in the same bath without straining and rinsing. It refers to the realization of denim removal, abrasion and bleaching. In this example, In the control process, descaling and etching must be carried out simultaneously in the same bath. is performed, then the denim fabric sample is rinsed and the bleaching is then carried out in another The descaling and etching stage, in order to provide sufficient mechanical action for the process, It was carried out in WASCATOR (Electrolux, Switzerland). WASCATOR 7kg fabric capacity, controlled by a microprocessor-based program control unit, more than LOM it is a washer extractor that creates a high mechanical effect, hence denim enough that the sizing agent in the fabric can be easily removed with the aid of amylase. ready fabric is provided for the next bleaching stage with its stripping and abrasive effects. 1 kg The denim pipe is loaded into WASCATOR and the washing program is run as follows: Pre- 25°C, 5 min; liquid/fabric ratio is 1521 (v/w).

Main Enzyme product Denimax® Core 1380 S containing both alpha-amylase and cellulase washing is added according to Table 5; 50°C, 85 minutes; liquid/fabric ratio 10:] (v/w); bath pH 6.5 under test conditions. . . fabrics . Cellusoft® L, % CiP, mg enzyme VA, H2O2, denim weight protein/ g denim mM/L g/L Unified Note: the average of two samples for each combination. Example 5: With CiP/VA in combination with descaling and etching in a bath color change The single-bath combined process in this example is in the same bath without straining and rinsing. It refers to the realization of denim removal, abrasion and bleaching. In this example, In the control process, descaling and etching must be carried out simultaneously in the same bath. is performed, then the denim fabric sample is rinsed and the bleaching is then carried out in another The descaling and etching stage, in order to provide sufficient mechanical action for the process, It was carried out in WASCATOR (Electrolux, Switzerland). WASCATOR 7kg fabric capacity, controlled by a microprocessor-based program control unit, more than LOM it is a washer extractor that creates a high mechanical effect, hence denim enough that the sizing agent in the fabric can be easily removed with the aid of amylase. ready fabric is provided for the next bleaching stage with its stripping and abrasive effects. 1 kg The denim pipe is loaded into WASCATOR and the washing program is run as follows: Pre- 25°C, 5 min; liquid/fabric ratio is 1521 (v/w).

Main Enzyme product Denimax® Core 1380 S containing both alpha-amylase and cellulase washing is added according to Table 5; 50°C, 85 minutes; liquid/fabric ratio 10:] (v/w); bath pH 6.5 under test conditions.

Washing Denim pipes and treatment bath in a different bath or in the same bath for the next collected for the post-bleaching stage.

Control procedure: The fabric samples for the control were tested 2 times in hot water and 2 times in cold water. rinsed and then cut into small tubes and again as described in Example 1. were placed in beakers with hazelnuts. Next, buffer (50 mM sodium acetate buffer, (w/v, ml/g). Reloaded and washing program per LOM For the bleaching step, it was continued at 40°C for 30 minutes.

Combined process: Fabric samples for the composite process were cut into small tubes and As explained in Example 1, hazelnuts were placed in beakers. Collect from WASCATOR The bath was adjusted to pH 5 with acetic acid and added to the beakers. Peroxidase, intermediate and H2O2 was added at a liquid/fabric ratio of 10:1 (w/v, ml/g) according to Table 5. beakers Reloaded into LOM and wash program for 30 minutes at 40°C* for the bleaching phase period has been continued.

After the bleaching step in both the control process and the combined process, all beakers removed and the denim samples were placed in passivation solution (2 g/L) for 10 minutes at 85°C. sodium carbonate) was transferred. Then, the sample fabrics were washed twice in hot water and cold. rinsed twice in water. Denim samples were tumble dried, conditioned and The bleaching level was evaluated in the same way as described in Example 1.

Table 5, six to seven times the dosage used for the CiP/VA/HZOZ system dosage control process When between shows that it can be achieved. Example, combined CiP/VA/H202 system in one bath shows that it is suitable for use in stripping, etching and bleaching processes.

Table 5. Results of combined single-bath treatment with Denimax® Core 1380 S and CiP/VA . . , fabrics Islem Denimax® Core 1380 S, CiP (mg enzyme VA H202 Wd' 'l' t"/d' M/L /L 0 width weight pro blade width) m g Delta Delta Washing Denim pipes and treatment bath in a different bath or in the same bath for the next collected for the post-bleaching stage.

Control procedure: The fabric samples for the control were tested 2 times in hot water and 2 times in cold water. rinsed and then cut into small tubes and again as described in Example 1. were placed in beakers with hazelnuts. Next, buffer (50 mM sodium acetate buffer, (w/v, ml/g). Reloaded and washing program per LOM For the bleaching step, it was continued at 40°C for 30 minutes.

Combined process: Fabric samples for the composite process were cut into small tubes and As explained in Example 1, hazelnuts were placed in beakers. Collect from WASCATOR The bath was adjusted to pH 5 with acetic acid and added to the beakers. Peroxidase, intermediate and H2O2 was added at a liquid/fabric ratio of 10:1 (w/v, ml/g) according to Table 5. beakers Reloaded into LOM and wash program for 30 minutes at 40°C* for the bleaching phase period has been continued.

After the bleaching step in both the control process and the combined process, all beakers removed and the denim samples were placed in passivation solution (2 g/L) for 10 minutes at 85°C. sodium carbonate) was transferred. Then, the sample fabrics were washed twice in hot water and cold. rinsed twice in water. Denim samples were tumble dried, conditioned and The bleaching level was evaluated in the same way as described in Example 1.

Table 5, six to seven times the dosage used for the CiP/VA/HZOZ system dosage control process When between shows that it can be achieved. Example, combined CiP/VA/H202 system in one bath shows that it is suitable for use in stripping, etching and bleaching processes.

Table 5. Results of combined single-bath treatment with Denimax® Core 1380 S and CiP/VA . . , fabrics Islem Denimax® Core 1380 S, CiP (mg enzyme VA H202 Wd' 'l' t"/d' M/L /L 0 width weight pro blade width) m g Delta Delta Washing Denim pipes and treatment bath in a different bath or in the same bath for the next collected for the post-bleaching stage.

Control procedure: The fabric samples for the control were tested 2 times in hot water and 2 times in cold water. rinsed and then cut into small tubes and again as described in Example 1. were placed in beakers with hazelnuts. Next, buffer (50 mM sodium acetate buffer, (w/v, ml/g). Reloaded and washing program per LOM For the bleaching step, it was continued at 40°C for 30 minutes.

Combined process: Fabric samples for the composite process were cut into small tubes and As explained in Example 1, hazelnuts were placed in beakers. Collect from WASCATOR The bath was adjusted to pH 5 with acetic acid and added to the beakers. Peroxidase, intermediate and H2O2 was added at a liquid/fabric ratio of 10:1 (w/v, ml/g) according to Table 5. beakers Reloaded into LOM and wash program for 30 minutes at 40°C* for the bleaching phase period has been continued.

After the bleaching step in both the control process and the combined process, all beakers removed and the denim samples were placed in passivation solution (2 g/L) for 10 minutes at 85°C. sodium carbonate) was transferred. Then, the sample fabrics were washed twice in hot water and cold. rinsed twice in water. Denim samples were tumble dried, conditioned and The bleaching level was evaluated in the same way as described in Example 1.

Table 5, six to seven times the dosage used for the CiP/VA/HZOZ system dosage control process When between shows that it can be achieved. Example, combined CiP/VA/H202 system in one bath shows that it is suitable for use in stripping, etching and bleaching processes.

Table 5. Results of combined single-bath treatment with Denimax® Core 1380 S and CiP/VA . . , fabrics Islem Denimax® Core 1380 S, CiP (mg enzyme VA H202 Wd' 'l' t"/d' M/L /L 0 width weight pro blade width) m g Delta Delta . . . fabrics Islem Denimax® Core 1380 S, CiP (mg enzyme VA H202 0 width weight pro blade width) m g Delta Delta Unified Note: average of two samples for each enzyme combination. Example 6: Sodium peroxide or urea as a source of hydrogen peroxide in WASCATOR Color changing with CiP/VA using hydrogen peroxide Denim bleaching trials were carried out in Wascator (Electrolux, Switzerland). Each For trial, six pieces of large brewed pipes weighing approximately 1kg were put together. is loaded. 50 mM sodium acetate buffer to control the bath at pH 5 used. Peroxidase, intermediate and source of hydrogen peroxide (H2O2 or sodium percarbonate or urea hydrogen peroxide) were added according to Table 6. sodium percarbonate and At the dosages in 6, both sodium percarbonate and hydrogen peroxide amount to 0.06 g/L. releases up to H2O2. Trial conditions are as described below: Main wash Cip, VA and hydrogen peroxide source added according to Table 6; 40°C, 20 minutes; liquid/fabric ratio 10:1 (w/v); 50 mM sodium acetate pH 5 with buffer.

Rinse 25°C, 5 min; the liquid/fabric ratio is 15:1 (w/w).

Rinse 25°C, 5 min; the liquid/fabric ratio is 15:1 (w/w). removed and tumble dried . . . fabrics Islem Denimax® Core 1380 S, CiP (mg enzyme VA H202 0 width weight pro blade width) m g Delta Delta Unified Note: average of two samples for each enzyme combination. Example 6: Sodium peroxide or urea as a source of hydrogen peroxide in WASCATOR Color changing with CiP/VA using hydrogen peroxide Denim bleaching trials were carried out in Wascator (Electrolux, Switzerland). Each For trial, six pieces of large brewed pipes weighing approximately 1kg were put together. is loaded. 50 mM sodium acetate buffer to control the bath at pH 5 used. Peroxidase, intermediate and source of hydrogen peroxide (H2O2 or sodium percarbonate or urea hydrogen peroxide) were added according to Table 6. sodium percarbonate and At the dosages in 6, both sodium percarbonate and hydrogen peroxide amount to 0.06 g/L. releases up to H2O2. Trial conditions are as described below: Main wash Cip, VA and hydrogen peroxide source added according to Table 6; 40°C, 20 minutes; liquid/fabric ratio 10:1 (w/v); 50 mM sodium acetate pH 5 with buffer.

Rinse 25°C, 5 min; the liquid/fabric ratio is 15:1 (w/w).

Rinse 25°C, 5 min; the liquid/fabric ratio is 15:1 (w/w). removed and tumble dried . . . fabrics Islem Denimax® Core 1380 S, CiP (mg enzyme VA H202 0 width weight pro blade width) m g Delta Delta Unified Note: average of two samples for each enzyme combination. Example 6: Sodium peroxide or urea as a source of hydrogen peroxide in WASCATOR Color changing with CiP/VA using hydrogen peroxide Denim bleaching trials were carried out in Wascator (Electrolux, Switzerland). Each For trial, six pieces of large brewed pipes weighing approximately 1kg were put together. is loaded. 50 mM sodium acetate buffer to control the bath at pH 5 used. Peroxidase, intermediate and source of hydrogen peroxide (H2O2 or sodium percarbonate or urea hydrogen peroxide) were added according to Table 6. sodium percarbonate and At the dosages in 6, both sodium percarbonate and hydrogen peroxide amount to 0.06 g/L. releases up to H2O2. Trial conditions are as described below: Main wash Cip, VA and hydrogen peroxide source added according to Table 6; 40°C, 20 minutes; liquid/fabric ratio 10:1 (w/v); 50 mM sodium acetate pH 5 with buffer.

Rinse 25°C, 5 min; the liquid/fabric ratio is 15:1 (w/w).

Rinse 25°C, 5 min; the liquid/fabric ratio is 15:1 (w/w). removed and tumble dried The results in Table 6 are similar to that of sodium percarbonate or urea hydrogen peroxide H2O2. shows that it can reach the bleaching level.

Table 6. Different hydrogen peroxide sources for CiP/VA bleaching in Wascator results of use Hydrogen peroxide Denim fabrics CiP (mg enzyme protein/g VA Source g/ L enim) (m ) DEL/[a Dgita peroxide Example 7: Local color change with CiP/VA.

After etching, the denim was cut 16 cm wide and 27 cm long. Denim A rectangular fabric sample 12.5 cm high and approximately 22 g in weight was sewn on. has been created. The fabric sample is a 10 cm diameter cloth with the navi side up. The central part of the fabric sample was hung horizontally by placing it on the hoop. lml CiP/VA mix (CiP = 0.221 mg Enzyme Protein /g mix; VA = 0.028 mM/g mixture) was dropped into the center of the fabric sample and the penetration was automatically has come true. After 5 minutes, the fabric sample was given a tubular shape and in Example 1 As described, it was placed in a beaker with hazelnuts. Then buffer (50 mM sodium 1021 (w/h, m1/g) were made. Loaded into each LOM and the washing program is 20 minutes at 25°C* period has been continued. After 20 minutes, the wash bath was emptied and the liquid/cloth into the beaker. NaOH solution (1 g/L) was added at a rate of 1021 (v/a ml/g). Beaker back to LOM loaded and the washing program was continued at 25°C for 10 minutes.

Then, the sample fabrics were rinsed 2 times in hot water and 2 times in cold water.

Denim samples were tumble dried, conditioned, and for the agarthy level in Example 1 evaluated in the same way as described.

The results in Table 6 are similar to that of sodium percarbonate or urea hydrogen peroxide H2O2. shows that it can reach the bleaching level.

Table 6. Different hydrogen peroxide sources for CiP/VA bleaching in Wascator results of use Hydrogen peroxide Denim fabrics CiP (mg enzyme protein/g VA Source g/ L enim) (m ) DEL/[a Dgita peroxide Example 7: Local color change with CiP/VA.

After etching, the denim was cut 16 cm wide and 27 cm long. Denim A rectangular fabric sample 12.5 cm high and approximately 22 g in weight was sewn on. has been created. The fabric sample is a 10 cm diameter cloth with the navi side up. The central part of the fabric sample was hung horizontally by placing it on the hoop. lml CiP/VA mix (CiP = 0.221 mg Enzyme Protein /g mix; VA = 0.028 mM/g mixture) was dropped into the center of the fabric sample and the penetration was automatically has come true. After 5 minutes, the fabric sample was given a tubular shape and in Example 1 As described, it was placed in a beaker with hazelnuts. Then buffer (50 mM sodium 1021 (w/h, m1/g) were made. Loaded in each LOM and the washing program is 20 minutes at 25°C* period has been continued. After 20 minutes, the wash bath was emptied and the liquid/cloth into the beaker. NaOH solution (1 g/L) was added at a rate of 1021 (v/a ml/g). Beaker back to LOM loaded and the washing program was continued at 25°C for 10 minutes.

Then, the sample fabrics were rinsed 2 times in hot water and 2 times in cold water.

Denim samples were tumble dried, conditioned, and for the agarthy level in Example 1 evaluated in the same way as described.

The results in Table 6 are similar to that of sodium percarbonate or urea hydrogen peroxide H2O2. shows that it can reach the bleaching level.

Table 6. Different hydrogen peroxide sources for CiP/VA bleaching in Wascator results of use Hydrogen peroxide Denim fabrics CiP (mg enzyme protein/g VA Source g/ L enim) (m ) DEL/[a Dgita peroxide Example 7: Local color change with CiP/VA.

After etching, the denim was cut 16 cm wide and 27 cm long. Denim A rectangular fabric sample 12.5 cm high and approximately 22 g in weight was sewn on. has been created. The fabric sample is a 10 cm diameter cloth with the navi side up. The central part of the fabric sample was hung horizontally by placing it on the hoop. lml CiP/VA mix (CiP = 0.221 mg Enzyme Protein /g mix; VA = 0.028 mM/g mixture) was dropped into the center of the fabric sample and the penetration was automatically has come true. After 5 minutes, the fabric sample was given a tubular shape and in Example 1 As described, it was placed in a beaker with hazelnuts. Then buffer (50 mM sodium 1021 (w/h, m1/g) were made. Loaded into each LOM and the washing program is 20 minutes at 25°C* period has been continued. After 20 minutes, the wash bath was emptied and the liquid/cloth into the beaker. NaOH solution (1 g/L) was added at a rate of 1021 (v/a ml/g). Beaker back to LOM loaded and the washing program was continued at 25°C for 10 minutes.

Then, the sample fabrics were rinsed 2 times in hot water and 2 times in cold water.

Denim samples were tumble dried, conditioned, and for the agarthy level in Example 1 evaluated in the same way as described.

The Delta L* value of the central part of the fabric sample is 14.30 and the edge (central 5 cm away from the point) Delta L* value was 3.99. This result is the edge of the central area. bleaches much more than the area and thus a local bleaching pattern on the fabric. shows that it has been created.

Claims (1)

REQUESTS A method for changing the color of dyed textiles, which involves contacting a textile product with a peroxidase, a source of hydrogen peroxide and violuric acid or a salt or hydrate thereof, exhibiting peroxidase activity covered by enzyme classification class EC 1.11.1.7. The method of claim 1, wherein the textile product is called. The method of any one of claims 1-2, wherein the method is carried out in an aqueous solution having a pH of from about 2 to about 8, preferably from about 3 to about 7, more preferably from about 4 to about 7. The method of any one of claims 1-3, wherein the method is carried out at 10-90°C or below 45°C, and still more preferably in the temperature range of 30-50°C. The method of any one of claims 1-4, wherein the reaction time is from about 5 minutes to about 30 minutes. The method of any one of claims 1-5, wherein the peroxidase consists of the acid sequence SEQI ID NO:1 or SEQI. A method for changing the color of a textile product comprising (a) contacting the textile product with cellulase; (b) contacting the textile product according to any one of claims 1-6 with a peroxidase, a hydrogen peroxide source and a vehicle, wherein steps (a) and (b) are performed sequentially or simultaneously in the same bath. The method of claim 7 wherein step (a) is the method of claim 8 after an enzymatic debarking step, wherein the enzymatic debarking step is the method of claim 9 wherein the step of contacting the textile with an amylase is the step (a) and step (b) are carried out in the same bath sequentially or simultaneously. The method according to any preceding claim, wherein the textile product is processed in a textile manufacturing method. REQUESTS A method for changing the color of dyed textiles, which involves contacting a textile product with a peroxidase, a source of hydrogen peroxide and violuric acid or a salt or hydrate thereof, exhibiting peroxidase activity covered by enzyme classification class EC 1.11.1.7. The method of claim 1, wherein the textile product is called. The method of any one of claims 1-2, wherein the method is carried out in an aqueous solution having a pH of from about 2 to about 8, preferably from about 3 to about 7, more preferably from about 4 to about 7. The method of any one of claims 1-3, wherein the method is carried out at 10-90°C or below 45°C, and still more preferably in the temperature range of 30-50°C. The method of any one of claims 1-4, wherein the reaction time is from about 5 minutes to about 30 minutes. The method of any one of claims 1-5, wherein the peroxidase consists of the acid sequence SEQI ID NO:1 or SEQI. A method for changing the color of a textile product comprising (a) contacting the textile product with cellulase; (b) contacting the textile product according to any one of claims 1-6 with a peroxidase, a hydrogen peroxide source and a vehicle, wherein steps (a) and (b) are performed sequentially or simultaneously in the same bath. The method of claim 7 wherein step (a) is the method of claim 8 after an enzymatic debarking step, wherein the enzymatic debarking step is the method of claim 9 wherein the step of contacting the textile with an amylase is the step (a) and step (b) are carried out in the same bath sequentially or simultaneously. The method according to any preceding claim, wherein the textile product is processed in a textile manufacturing method. REQUESTS A method for changing the color of dyed textile products, enzyme classification of a textile product class EC 1.11. A peroxidase exhibiting peroxidase activity encompassed by 1.7 involves contacting a source of hydrogen peroxide and a vehicle, which is violuric acid or a salt or hydrate thereof. The method of claim 1, wherein the textile product is called. The method of any one of claims 1-2, wherein the method is carried out in an aqueous solution having a pH of from about 2 to about 8, preferably from about 3 to about 7, more preferably from about 4 to about 7. The method of any one of claims 1-3, wherein the method is carried out at 10-90°C or below 45°C, and still more preferably in the temperature range of 30-50°C. The method of any one of claims 1-4, wherein the reaction time is from about 5 minutes to about 30 minutes. The method of any one of claims 1-5, wherein the peroxidase consists of the acid sequence SEQI ID NO:1 or SEQI. A method for changing the color of a textile product comprising (a) contacting the textile product with cellulase; (b) contacting the textile product according to any one of claims 1-6 with a peroxidase, a hydrogen peroxide source and a vehicle, wherein steps (a) and (b) are performed sequentially or simultaneously in the same bath. The method of claim 7 wherein step (a) is the method of claim 8 after an enzymatic debarking step, wherein the enzymatic debarking step is the method of claim 9 wherein the step of contacting the textile with an amylase is the step (a) and step (b) are carried out in the same bath sequentially or simultaneously. The method according to any preceding claim, wherein the textile product is processed in a textile manufacturing method.