EP2630291A1 - Local color modification of dyed fabrics using a laccase system - Google Patents
Local color modification of dyed fabrics using a laccase systemInfo
- Publication number
- EP2630291A1 EP2630291A1 EP11776663.4A EP11776663A EP2630291A1 EP 2630291 A1 EP2630291 A1 EP 2630291A1 EP 11776663 A EP11776663 A EP 11776663A EP 2630291 A1 EP2630291 A1 EP 2630291A1
- Authority
- EP
- European Patent Office
- Prior art keywords
- laccase
- textile
- dyed
- color
- enzyme system
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Withdrawn
Links
Classifications
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- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
- D06M16/00—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic
- D06M16/003—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic with enzymes or microorganisms
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06P—DYEING OR PRINTING TEXTILES; DYEING LEATHER, FURS OR SOLID MACROMOLECULAR SUBSTANCES IN ANY FORM
- D06P5/00—Other features in dyeing or printing textiles, or dyeing leather, furs, or solid macromolecular substances in any form
- D06P5/02—After-treatment
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06P—DYEING OR PRINTING TEXTILES; DYEING LEATHER, FURS OR SOLID MACROMOLECULAR SUBSTANCES IN ANY FORM
- D06P5/00—Other features in dyeing or printing textiles, or dyeing leather, furs, or solid macromolecular substances in any form
- D06P5/15—Locally discharging the dyes
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06P—DYEING OR PRINTING TEXTILES; DYEING LEATHER, FURS OR SOLID MACROMOLECULAR SUBSTANCES IN ANY FORM
- D06P5/00—Other features in dyeing or printing textiles, or dyeing leather, furs, or solid macromolecular substances in any form
- D06P5/15—Locally discharging the dyes
- D06P5/158—Locally discharging the dyes with other compounds
Definitions
- compositions, and methods relate to local color modification of dyed fabrics using a laccase enzyme system.
- Laccases are copper-containing phenol oxidizing enzymes that are known to be good oxidizing agents in the presence of oxygen. Laccases are found in microbes, fungi, and higher organisms. Laccase enzymes are used for many applications, including pulp and paper bleaching, treatment of pulp waste water, de-inking, industrial color removal, bleaching in laundry detergents, oral care teeth whiteners, as catalysts or facilitators for polymerization and oxidation reactions, in the textiles industry, and in the food industry.
- Laccases are known to be produced by a wide variety of fungi, including species of the genii Aspergillus, Neurospora, Podospora, Botrytis, Pleurotus, Fornes, Phlebia, Trametes, Polyporus, Stachybotrys, Rhizoctonia, Bipolaris, Curvularia, Amerosporium, Lentinus, Myceliophtora, Coprinus, Thielavia, Cerrena, Streptomyces, and Melanocarpus.
- a mediator also known as an enhancing agent.
- a textile processing method comprising contacting a portion of dyed textile with a laccase enzyme system for a length of time and under conditions sufficient to cause a localized color modification to the portion of the textile.
- the method is performed by wetting but not submerging the portion of the dyed textile with a composition comprising the laccase enzyme system. In some embodiments, the method is performed by applying a composition comprising the laccase enzyme system to the portion of the dyed textile, and then wetting but not submerging the portion of the dyed textile.
- the laccase enzyme system is provided in a single composition. In some embodiments, the laccase enzyme system is provided as an aqueous, gel, semi-solid, or solid formulation.
- the color modification is selected from lightening of color, change of color, change in color cast, and bleaching.
- the textile is indigo-dyed denim. In some embodiments, the textile is indigo and sulfur-dyed denim.
- the textile is a pair of jeans.
- the portion of the textile is a pant leg, sleeve, cuff, collar, pocket, or belt loop.
- the portion of the textile is in the form of a predetermined shape.
- the portion of the textile is in the form of a letter, word, logo, or trademark.
- the laccase enzyme system comprises a laccase enzyme and a mediator.
- the laccase is a microbial laccase.
- the laccase is from a Cerrena species.
- the laccase is from Cerrena unicolor.
- the laccase is laccase D from C. unicolor.
- the mediator is syringonitrile.
- the method is performed at a temperature of from about 20°C to about 40°C. In some embodiments, the method is performed at a temperature of from about 20°C to about 30°C. In some embodiments, the method is performed at the ambient temperature of tap water. In some embodiments, the method is performed at ambient air temperature.
- Figure 1 is an image of indigo-dyed jeans that were subjected to localized color modification in the shape of a heart.
- the systems, compositions, and methods are useful, for example, for processing textiles to affect local color modification on fabrics and garments, including complete, consumer-ready garments.
- Various aspects and embodiments of the systems, compositions, and methods are to be described.
- enzyme refers to a protein that catalyzes a chemical reaction.
- the catalytic function of an enzyme constitutes its "enzymatic activity” or "activity.”
- An enzyme is typically classified according to the type of reaction it catalyzes, e.g. , oxidation of phenols, hydrolysis of peptide bonds, incorporation of nucleotides, etc.
- substrate refers to a substance (e.g., a chemical compound) on which an enzyme performs its catalytic activity to generate a product.
- a "laccase” is a multi-copper containing oxidase (EC 1.10.3.2) that catalyzes the oxidation of phenols, polyphenols, and anilines by single-electron abstraction, with the concomitant reduction of oxygen to water in a four-electron transfer process.
- laccase activity is measured in units/gram (U/g), wherein one unit is defined as the amount of laccase activity required to oxidize 1 nmol of 2,2'-azinobis(3- ethylbenzthiazoline-6-sulfonate; ABTS) substrate per second under conditions of an assay based on the ability of laccase enzyme to oxidize ABTS into its corresponding stable cation radical,
- the radical form is dark green in color with increased absorbance at 420 nm.
- the amount of green color formation is proportional to the amount of laccase activity, and can be compared to a laccase standard curve to determine the absolute amount of laccase activity.
- variant proteins encompass related and derivative proteins that differ from a parent/reference protein by a small number of amino acid substitutions, insertions, and/or deletions.
- the number of different amino acid residues is any of about 1, 2, 3, 4, 5, 10, 20, 25, 30, 35, 40, 45, or 50.
- variants differ by about 1 to about 10 amino acids residues.
- variant proteins have at least about 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or even 99.5% amino acid sequence identity to a parent/reference protein.
- analogous sequence refers to a polypeptide sequence within a protein that provides a similar function, tertiary structure, and/or conserved residues with respect to a sequence within a parent/reference protein. For example, in structural regions that contain an alpha helix or a beta sheet structure, replacement amino acid residues in an analogous sequence maintain the same structural feature. In some embodiments, analogous sequences result in a variant protein that exhibits a similar or improved function with respect to the parent protein from which the variant is derived.
- a "homologous protein” or “homolog” refers to a protein (e.g. , a laccase enzyme) that has a similar function (e.g. , enzymatic activity) and/or structure as a reference protein (e.g. , a laccase enzyme from a different source). Homologs may be from evolutionarily related or unrelated species.
- a homolog has a quaternary, tertiary and/or primary structure similar to that of a reference protein, thereby potentially allowing for replacement of a segment or fragment in the reference protein with an analogous segment or fragment from the homolog, with reduced disruptiveness of structure and/or function of the reference protein in comparison with replacement of the segment or fragment with a sequence from a non-homologous protein.
- wild-type As used herein, wild-type, “native,” and “naturally-occurring” proteins are those found in nature.
- wild-type sequence refers to an amino acid or nucleic acid sequence that is found in nature or naturally occurring.
- a wild- type sequence is the starting point of a protein engineering project, for example, production of variant proteins.
- a “signal sequence” refers to a sequence of amino acids bound to the N- terminal portion of a protein, and which facilitates the secretion of the mature form of the protein from the cell.
- the mature form of the extracellular protein lacks the signal sequence which is cleaved off during the secretion process.
- the term "derivative” refers to a protein that is derived from a parent/reference protein by addition of one or more amino acids to either or both the N- and C- terminal end(s), substitution of one or more amino acid residues at one or a number of different sites in the amino acid sequence, deletion of one or more amino acid residues at either or both ends of the protein or at one or more sites in the amino acid sequence, and/or insertion of one or more amino acids at one or more sites in the amino acid sequence.
- the preparation of a protein derivative is often achieved by modifying a DNA sequence which encodes for the native protein, transformation of that DNA sequence into a suitable host, and expression of the modified DNA sequence to form the derivative protein.
- polypeptide, protein, and peptide refer to a composition comprised of amino acids (i.e., amino acid residues).
- amino acids i.e., amino acid residues
- the conventional one-letter or three-letter codes for amino acid residues are used.
- a polypeptide may be linear or branched, may comprise modified amino acids, and may be interrupted by non-amino acids.
- the terms also encompass an amino acid polymer that has been modified naturally or by intervention; for example, disulfide bond formation, glycosylation, lipidation, acetylation, phosphorylation, or any other manipulation or modification, such as conjugation with a labeling component.
- polypeptides containing one or more analogs of an amino acid including, for example, unnatural amino acids, etc.
- the term “textile” refers to fibers, yarns, fabrics, garments, and non- woven materials.
- the term encompasses textiles made from natural and synthetic (e.g., manufactured) materials, as well as natural and synthetic blends.
- the term “textile” refers to both unprocessed and processed fibers, yarns, woven or knit fabrics, non-wovens, and garments.
- a textile contains cellulose.
- the term “fabric” refers to a manufactured assembly of fibers and/or yarns that has substantial surface area in relation to its thickness and sufficient cohesion to give the assembly useful mechanical strength.
- Garment refers to a clothing item made from one or more fabrics. Garments typically include fabrics that are already cut to size and sewn or stitched together. Garments may or may not include buttons, eyelets, straps, zippers, hook-and-loop closures, and the like, which can be attached before or after localized color modification.
- color modification refers to a change in the chroma, saturation, intensity, luminance, and/or tint of a color associated with a fiber, yarn, fabric, garment, or non- woven material, collectively referred to as textile materials.
- Color modification encompasses chemical modification to a chromophore as well as chemical modification to the material to which a chromophore is attached. Examples of color modification include fading, bleaching, and altering tint.
- a particular color modification to indigo-dyed denim is fading to a "vintage look," which has a less intense blue/violet tint and more subdued grey appearance than the freshly-dyed denim.
- local color modification refers to color modification, as defined, above, that is performed on only a portion of a fabric or garment.
- generalized textile color modification which is typically performed in a bath, i.e. , in a submerged environment
- local color modification is performed using a wetted but not submerged fabric or garment, typically on a table, work bench, or other hard surface, on a hanging or otherwise suspended fabric or garment, or using rollers or other processing equipment that do not subject the fabric or garment to a submerged environment, such that only a portion of the garment can be subjected to color modification without affecting the remainder of the fabric or garment.
- a portion of a fabric or garment refers to anything less than the whole fabric or garment. Where specified, a portion of a fabric or garment may refer to an indicated structural or decorative feature a fabric or garment, such as a pant leg, a sleeve, a pocket, a belt loop, a cuff, a hem, and the like.
- the term “bleaching” refers to the process of treating a textile material such as a fiber, yarn, fabric, garment or non- woven material to produce a lighter color. This term includes the production of a brighter and/or whiter textile, e.g. , in the context of a textile processing application, as well as lightening of the color of a stain, e.g., in the context of a cleaning application.
- size and “sizing” refer to compounds used in the textile industry to improve weaving performance by increasing the abrasion resistance and strength of a yarn. Size is usually made of starch or starch-like compounds.
- the term "desizing enzyme” refers to an enzyme used to remove size.
- exemplary enzymes are amylases, cellulases, and mannanases.
- % identity refers to the level of nucleic acid sequence identity between a nucleic acid sequence that encodes a laccase as described herein and another nucleic acid sequence, or the level of amino acid sequence identity between a laccase enzyme as described herein and another amino aid sequence. Alignments may be performed using a conventional sequence alignment program.
- Exemplary levels of nucleic acid and amino acid sequence identity include, but are not limited to, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or even at least 99%, or more, sequence identity to a given sequence, e.g. , the coding sequence for a laccase or the amino acid sequence of a laccase, as described herein.
- Exemplary computer programs that can be used to determine identity between two sequences include, but are not limited to, the suite of BLAST programs, e.g., BLASTN, BLASTX, and TBLASTX, BLASTP and TBLASTN, publicly available on the Internet at www.ncbi.nlm.nih.gov/BLAST. See also, Altschul, et ah, 1990 and Altschul, et ah , 1997.
- the BLASTX program is preferred for searching nucleic acid sequences that have been translated in all reading frames against amino acid sequences in the GenBank Protein Sequences and other public databases. Both BLASTN and BLASTX are run using default parameters of an open gap penalty of 11.0, and an extended gap penalty of 1.0, and utilize the BLOSUM-62 matrix. (See, e.g., Altschul, et al , 1997.)
- An alignment of selected sequences in order to determine " identity" between two or more sequences may be performed using, for example, the CLUSTAL-W program in
- Mac Vector version 6.5 operated with default parameters, including an open gap penalty of 10.0, an extended gap penalty of 0.1, and a BLOSUM 30 similarity matrix.
- chemical mediator and “mediator” are used interchangeably to refer to a chemical compound that functions as a redox mediator to shuttle electrons between an enzyme exhibiting oxidase activity ⁇ e.g. , a laccase) and a secondary substrate or electron donor.
- oxidase activity e.g. , a laccase
- mediators are also known in the art as “enhancers” and “accelerators.”
- secondary substrate and “electron donor” are used interchangeably to refer to a dye, pigment ⁇ e.g. , indigo), chromophore ⁇ e.g. , polyphenolic, anthocyanin, or carotenoid), or other secondary substrate to and from which electrons can be shuttled by an enzyme exhibiting oxidase activity.
- laccases include one or more laccases or laccase-related enzymes, herein collectively referred to as "laccases” or "laccase enzymes.”
- laccases include any laccase enzyme encompassed by EC 1.10.3.2, according to the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB).
- Laccase enzymes from microbial and plant origin are known in the art.
- a microbial laccase enzyme may be derived from bacteria or fungi (including filamentous fungi and yeasts). Suitable examples include a laccase derived or derivable from a strain of
- Aspergillus Neurospora ⁇ e.g. , N. crassa), Podospora, Botrytis, Collybia, Cerrena ⁇ e.g. , C. unicolor), Stachybotrys, Panus (e.g. , P. rudis), Thielavia, Fomes, Lentinus, Pleurotus, Trametes ⁇ e.g. , T. villosa, and T. versicolor), Rhizoctonia ⁇ e.g. , R. solani), Coprinus ⁇ e.g. , C. plicatilis and C. cinereus), Psatyrella, Myceliophthora ⁇ e.g. , M.
- thermonhila Schytalidium, Phlebia ⁇ e.g., P. radita (WO 92/01046)), or Coriolus ⁇ e.g. , C. hirsutus (JP 2238885)), Spongipellis, Polyporus, Ceriporiopsis subvermispora, Ganoderma tsunodae, and Trichoderma.
- a laccase may be produced by culturing a host cell transformed with a recombinant DNA vector that includes nucleotide sequences encoding the laccase.
- the DNA vector may further include nucleotide sequences permitting the expression of the laccase in a culture medium, and optionally allowing the recovery of the laccase from the culture.
- An expression vector containing a polynucleotide sequence encoding a laccase enzyme may be transformed into a suitable host cell.
- the host cell may be a fungal cell, such as a filamentous fungal cell, examples of which include but are not limited to species of Trichoderma [e.g. , T. reesei (previously classified as T. longibrachiatum and currently also known as Hypocrea jecorina], T. viride, T. koningii, and T. harzianum), Aspergillus ⁇ e.g., A. niger, A. nidulans, A. oryzae, and A. awamori), Penicillium, Humicola ⁇ e.g.
- a host cell for expression of a laccase enzyme may also be from a species of Cerrena ⁇ e.g., C.
- Fungal cells may be transformed by a process involving protoplast formation and transformation of the protoplasts followed by regeneration of the cell wall using techniques known in the art.
- the host organism may from a species of bacterium, such as Bacillus [e.g. , B. subtilis, B. licheniformis, B. lentus, B. (now Geobacillus) stearothermophilus, and fi. brevis], Pseudomonas, Streptomyces ⁇ e.g. , S. coelicolor, S. lividans), or E. coli.
- Bacillus e.g. , B. subtilis, B. licheniformis, B. lentus, B. (now Geobacillus) stearothermophilus, and fi. brevis
- Pseudomonas Streptomyces ⁇ e.g. , S. coelicolor, S. lividans
- E. coli E. coli.
- the transformation of bacterial cells may be performed according to conventional methods, e.g. , as described in Maniatis, T. et al ,
- the medium used to culture the transformed host cells may be any conventional medium suitable for growing the host cells.
- the expressed enzyme is secreted into the culture medium and may be recovered therefrom by well-known procedures.
- laccases may be recovered from a culture medium as described in U.S. Patent Publication No. 2008/0196173.
- the enzyme is expressed intracellularly and is recovered following disruption of the cell membrane.
- the expression host may be Trichoderma reesei with the laccase coding region under the control of a CBHl promoter and terminator (see, e.g. , U.S. Patent No. 5,861,271).
- the expression vector may be, e.g. , pTrex3g, as disclosed in U.S. Patent No. 7,413,887.
- laccases are expressed as described in U.S. Patent Publication Nos. 2008/0196173 or 2009/0221030.
- a laccase D enzyme having the following amino acid sequence (SEQ ID NO: 10; signal sequence in italics) may be used:
- the mature processed form of this polypeptide is as follows (SEQ ID NO: 11):
- laccase enzymes suitable for use in the present compositions and methods are mature polypeptides that lack a signal sequence that may be used to direct secretion of a full-length polypeptide from a cell.
- a suitable mature polypeptide may have at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or even at least 99%, or more, amino acid sequence identity to an amino acid sequence selected from the group consisting of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, and SEQ ID NO: 11.
- such polypeptides have enzymatic laccase activity, as determined using the assays
- laccase enzymes suitable for use in the present compositions and methods are truncated with respect to a full-length or mature parent/reference sequence.
- Such truncated polypeptides may be generated by the proteolytic degradation of a full-length or mature polypeptide sequence or by engineering a polynucleotide to encode a truncated polypeptide.
- Exemplary polypeptides are truncated at the amino and/or carboxyl-terminus with respect to an amino acid sequence selected from the group consisting of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, and SEQ ID NO: 11.
- the truncation may be of a small number, e.g. , 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acid residues, or of entire structural or functional domains.
- a suitable truncated polypeptide may have at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or even at least 99%, or more, amino acid sequence identity to the corresponding portion of one or more of the above-references amino acid sequences.
- such polypeptides have enzymatic laccase activity, as determined using the assays and procedures described, herein.
- the present laccase enzyme systems, compositions, and methods further include one or more chemical mediator agents that enhance the activity of the laccase enzyme.
- a mediator also called an enhancer or accelerator
- a mediator is a chemical that acts as a redox mediator to effectively shuttle electrons between the enzyme exhibiting oxidase activity and a dye, pigment (e.g. , indigo), chromophore (e.g. , polyphenolic, anthocyanin, or carotenoid, for example, in a colored stain), or other secondary substrate or electron donor.
- the chemical mediator is a phenolic compound, for example, methyl syringate, or a related compound, as described in, e.g. , PCT Application Nos. WO 95/01426 and WO 96/12845.
- the mediator may also be an N-hydroxy compound, an N-oxime compound, or an N-oxide compound, for example, N-hydroxybenzotriazole, violuric acid, or N- hydroxyacetanilide.
- the mediator may also be a phenoxazine/phenothiazine compound, for example, phenothiazine-10-propionate.
- the mediator may further be 2,2'-azinobis-(3- ethylbenzothiazoline-6-sulfonic acid) (ABTS).
- ABTS 2,2'-azinobis-(3- ethylbenzothiazoline-6-sulfonic acid)
- Other chemical mediators are well known in the art, for example, the compounds disclosed in PCT Application No. WO 95/01426, which are known to enhance the activity of a laccase.
- the mediator may also be acetosyringone, methyl syringate, ethyl syringate, propyl syringate, butyl syringate, hexyl syringate, or octyl syringate.
- the mediator is 4-cyano-2,6-dimethoxyphenol, 4-carboxamido- 2,6-dimethoxyphenol or an N-substituted derivative thereof such as, for example, 4-(N-methyl carboxamido)-2,6-dimethoxyphenol, 4-[N-(2-hydroxyethyl) carboxamido]-2,6- dimethoxyphenol, or 4-(N,N-dimethyl carboxamido)-2,6-dimethoxyphenol.
- the mediator is described by the following formula:
- D is selected from the group consisting of -CO-E, -SO2-E, -CN, -NXY, and
- E is -H, -OH, -R, -OR, or -NXY
- X,Y, and Z are independently selected from - H, -OH, -OR, and -R;
- R is a Ci - Ci 6 alkyl, preferably a Ci -C 8 alkyl, which alkyl may be saturated or unsaturated, branched or unbranched and optionally substituted with a carboxy, sulfo or amino group
- B and C are independently selected from C m H2 m+ i ; 1 ⁇ m ⁇ 5.
- a in the above mentioned formula is -CN or -CO-E, wherein E may be -H, -OH, -R, -OR, or -NXY, where X and Y are independently selected from -H, -OH, -OR, and -R, where R is a Ci -C16 alkyl, preferably a Ci -C 8 alkyl, which alkyl may be saturated or unsaturated, branched or unbranched and optionally substituted with a carboxy, sulfo or amino group; and B and C are independently selected from C m H 2m+ i; 1 ⁇ m ⁇ 5.
- the mediator is 4-hydroxy-3,5-dimethoxybenzonitrile (also referred to as "syringonitrile" or "SN").
- A may be placed meta to the hydroxy group, instead of being placed in the para position as shown.
- the mediator may be present in a
- the mediators may be prepared by methods known to the skilled artisan, such as those disclosed in PCT Application Nos. WO 97/11217 and WO 96/12845 and U.S. Patent No. 5,752,980. Other suitable mediators are described in, e.g., U.S. Patent Publication No.
- the methods involve locally contacting a textile or garment with a laccase enzyme system for a length of time, and under conditions, sufficient to produce at least one measurable or visual local effect to the fabric or textile.
- exemplary effects are, e.g. , a change in color, a change in color cast, lightening, bleaching, and fading.
- the present laccase enzyme systems, compositions, and methods can be use in applications where localized color modification of dyed fabrics is desirable. Examples of localized color modification include color modification the fronts or backs of jeans, to sleeves, to collars, to cuffs, to belt loops, and the like.
- the method may be performed by wetting (but not submerging) a portion of the dyed textile with a composition comprising the laccase enzyme system, or performed by applying a composition comprising the laccase enzyme system to a portion of the dyed textile, and then wetting (but not submerging) the portion of the dyed textile.
- An important feature of the method is that less than the entire fabric or garment is contacted with the laccase enzyme system, and that color modification occurs on less than the entire fabric or garment.
- the laccase enzyme system may be provided in a single composition, which may be aqueous, gel, semi-solid, or solid in form.
- the laccase enzyme system may be provided in a plurality of compositions, which may be aqueous, gel, semi-solid, or solid, or a combination, thereof.
- the laccase system, or components, thereof are provided in liquid form, they can be applied to fabrics or garments by pouring, dripping, brushing, blotting, spraying, dipping, and the like.
- laccase system, or components, thereof are provided in gel, paste, or other semi-solid form
- they can be applied using a stick applicator, by dispensing from a tube or syringe, drawn with a crayon, or the like.
- the laccase system, or components, thereof are provided in dry or solid form, they can be applied by shaking from a container, as a talc, or the like.
- the fabric or garment may be wetted before and/or after application of the laccase; however, the fabric or garment is generally not submerged in an aqueous medium (i.e. , in a "bath"), since this procedure would allow the color modification to become generalized.
- aqueous medium i.e. , in a "bath”
- the localized color modification may be in the form of a predetermined pattern or shape, as exemplified by the heart shape illustrated in Figure 1.
- the pattern or shape may in the form of letters (including numbers and symbols), words, logos, trademarks (including tradedress), or the like.
- the pattern or shape may be designed to mimic the appearance of conventional textile processing methods, such as sandblasting.
- the predetermined pattern or shape is selected by the textile manufacturer. In other embodiments, the predetermined pattern or shape is selected by a retailer or consumer. In some cases, the term predetermined may apply to the overall aesthetic desired, rather than an exact pattern. For example, local color variant can be in the form of unique and artistic designs, even designs with a random element, which are still considered to be predetermined as used herein.
- different levels of local color modification are produced by applying different amounts of a laccase enzyme system, applying a laccase enzyme system for different amounts of time, or applying laccase enzyme systems that have been preincubated for different amounts of time to dyed fabric.
- a dyed fabric can be modified to have more than one color modification, e.g. , a "light-colored portion" and a "lighter colored portion.”
- the ability to produce different levels of color modification greatly increases the complexity of patterns and shapes that can be produced.
- Textiles that can be subjected to color modification as described include cellulosic and non-cellulosis textiles, for example, cotton, linen, flax, hemp, jute wool, silk, nylon, polyester, acrylic, and blends, thereof.
- the textile may be dyed with any dye that may be decolorized using a laccase enzyme.
- dyes include, but are not limited to, azo, monoazo, disazo, nitro, xanthene, quinoline, anthroquinone, triarylmethane, paraazoanyline, azineoxazine, stilbene, aniline, and phthalocyanine dyes, or mixtures thereof.
- the dye is an azo dye (e.g. , Reactive Black 5 (2,7-naphthalenedisulfonic acid, 4-amino-5- hydroxy-3,6-bis((4-(2-a laccase enzyme).
- the dye is an anthraquinone dye (e.g. , remazol blue), indigo (indigo carmine), or a triarylmethane/paraazoanyline dye (e.g. , crystal violet, malachite green).
- the dye is a reactive, direct, disperse, or pigment dye.
- the dye is comprised within an ink.
- the dye is indigo and/or a sulfur-based dye.
- the textile is denim dyed with indigo and/or a sulfur-based dye.
- the textile is dyed with indigo, and the laccase enzyme and mediator are used to oxidize the indigo to isatin.
- the methods contemplate the use of one or more of the laccases, many of which are described herein.
- the laccase is from a Cerrena species, such as C.
- the laccase comprises, consists of, or consists essentially of the amino acid sequence of any of the C. unicolor laccase enzymes described herein, or an amino acid sequence having any of at least about 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or even 99.5% identity to any of the C. unicolor laccase enzymes described herein, and having laccase enzymatic activity.
- the laccases is C. unicolor laccase D, or a closely related laccase.
- such methods include localized incubation of a laccase enzyme with a dyed fabric at a low temperature, for example, about 50°C or less, about 45°C or less, or even about 40°C or less.
- the temperature is between about 10°C and about 50°C. In some embodiments, the temperature is between about 15°C and about 45°C. In some embodiments, the temperature is between about 20°C and about 40°C. In some embodiments, the temperature is between about 25° to about 35 °C. In some embodiments, the temperature is about 10°C, 15°C, 20°C, 25°C, 30°C, 35°C, 40°C, 45°C, or 50°C. In some embodiments, the temperature is ambient air temperature.
- one or more laccase enzymes are used at a concentration of about 0.005 to about 5,000 mg/liter, about 0.05 to about 500 mg/liter, about 0.1 to about 100 mg/liter, or about 0.5 to about 10 mg/liter.
- a laccase is used at a concentration of about 0.005 to about 5,000 mg/kg of fabric (such as denim), e.g., about 0.05 to about 500 mg/kg of fabric, about 0.1 to about 100 mg/kg of fabric, or about 0.5 to about 10 mg/kg of fabric.
- a laccase is used at a pH of about 5 to about 8, about 5 to about 7.5, about 5 to about 7, about 5.5 to about 6.5, about 5 to about 6, or about 6.
- Exemplary pH values are about 5.0, 5.1, 5.2, 5.3, 5.4, 5.5, 5.6, 5.7, 5.8, 5.9, 6.0, 6.1, 6.2, 6.3, 6.4, 6.5, 6.6, 6.7, 6.8, 6.9, 7.0, 7.1, 7.2, 7.3, 7.4, 7.5, 7.6, 7.7, 7.8, 7.9, and 8.0.
- the present localized color modification systems, compositions, and methods can be utilized following various textile processing steps applied to whole garments or fabrics, for example, desizing, abrading (physical or enzymatic), scouring, dyeing, bleach clean-up, biopolishing, enzymatic or chemical color modification, and the like.
- Abrading and/or biopolishing may be performed using a suitable cellulase, such as those derived from microorganisms which are known to be capable of producing cellulolytic enzymes, e.g. , species of Humicola, Thermomyces, Bacillus, Trichoderma, Fusarium, Myceliophthora, Phanerochaete, Irpex, Scytalidium, Schizophyllum, Penicillium, Aspergillus or Geotricum.
- Known species capable for producing celluloytic enzymes include Humicola insolens, Fusarium oxysporum or Trichoderma reesei.
- suitable cellulases are disclosed in U.S. Patent No. 4,435,307; European patent application No. 0 495 257; PCT Patent Application No. WO 91/17244; and European Patent Application No. EP-A2-271 004, all of which are incorporated herein by reference.
- the present systems, compositions, and methods are using before or after "stonewashing" using a cellulase, bleaching using an aryl esterase, and/or color modification to the entire textile or garment using a laccase, can be combined to provide a comprehensive enzymatic textile processing system.
- Such a system allows a textile processor to produce textiles with a wide variety of finishes without the need to use conventional textile processing chemical.
- the present systems, compositions, and methods are using before or after “desizing,” e.g. , using an amylase, "scouring”, e.g. , using a pectate lyase, and/or bleach- clean-up,” using catalase.
- “desizing” e.g. , using an amylase
- “scouring” e.g. , using a pectate lyase
- bleach- clean-up using catalase.
- the present systems and compositions can be provided in one of more aqueous, gel, semi-solid, or solid compositions comprising, consisting of, or consisting essentially of a laccase enzyme and, optionally, a mediator suitable for localized fabric application.
- the present systems and compositions can be provided in the form of a single "just add water” or “ready to use” (RTU) composition.
- Such compositions may further contain one or more buffers, dispersants, surfactants, blockers, polymers, preservatives, and the like.
- An exemplary buffer is a monosodium phosphate/adipic acid system.
- the compositions are in granular form for ease of storage and transportation. Such compositions are diluted with water prior to use.
- the laccase enzyme system may be allowed to preincubate for a period of time, e.g., 5 minutes to 2 hours, 10 minutes to 1 hour, 15 minutes to 45 minutes, 20 minutes to 30 minutes, and the like. Exemplary preincubation times are about 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 80, 85, 90, 95, 100, 105, 110, 115, and 120 minutes.
- laccase compositions may then be applied to a fabric or garment by pouring, dripping, brushing, blotting, spraying, using a stick applicator, by dispensing from a tube or syringe, drawn with a crayon, shaking from a container, as a talc, or the like.
- the laccase enzyme system is in the form of a liquid, it is preferably applied by spraying (e.g. , using an air brush or aerosol bottle), or using a free-hand brush, roller, or the like.
- a stencil may be used to help define the pattern or shape.
- a textile processing method comprising contacting a portion of dyed textile with a laccase enzyme system for a length of time and under conditions sufficient to cause a localized color modification to the portion of the textile.
- the method of paragraph 1 is performed by wetting but not submerging the portion of the dyed textile with a composition comprising the laccase enzyme system.
- the method of paragraph 1 is performed by applying a composition comprising the laccase enzyme system to the portion of the dyed textile, and then wetting but not submerging the portion of the dyed textile.
- the laccase enzyme system is provided in a single composition.
- the laccase enzyme system is provided as an aqueous, gel, semi-solid, or solid formulation.
- the color modification is selected from lightening of color, change of color, change in color cast, and bleaching.
- the textile is indigo-dyed denim.
- the textile is indigo and sulfur-dyed denim.
- the textile is a pair of jeans.
- the portion of the textile is a pant leg, sleeve, cuff, collar, pocket, or belt loop.
- the portion of the textile is in the form of a predetermined shape.
- the portion of the textile is in the form of a letter, word, logo, or trademark.
- the laccase enzyme system comprises a laccase enzyme and a mediator. 14. In some embodiments of the method of paragraph 13, the laccase is a microbial laccase.
- the laccase is from a Cerrena species.
- the laccase is from Cerrena unicolor.
- the laccase is laccase D from C. unicolor.
- the mediator is syringonitrile.
- the method is performed at a temperature of from about 20°C to about 40°C.
- the method is performed at a temperature of from about 20°C to about 30°C.
- the method is performed at the ambient temperature of tap water.
- the method is performed at ambient air temperature.
- PRIMAGREEN® EcoFade LT 100 includes a Cerrena unicolor laccase D enzyme and 4-hydroxy-3,5-dimethoxybenzonitrile (syringonitrile) in a dry granular formulation, which can be prepared for use by addition of water (or other aqueous medium).
- the amount of laccase activity in the formulation is at least 38,000 U/g.
- laccase/mediator system tested were 1%, 3%, and 10% (w/v) in water, which were applied to denim after a pre-incubation at room temperature of 1 hour, and incubated on the denim for a period of 30 and 60 minutes at 40°C.
- the amount of color modification was determined using a chromameter.
- the results obtained at the 30 minute time point are shown in Table 1, wherein a higher L value indicates a higher bleaching level.
- the results obtained at the 60 minute time point were similar, suggesting that the process is essentially complete at 30 minutes.
- Increasing amounts of the laccase/mediator system produced increasing amounts of color modification, in this case a bleaching effect, demonstrating dose response.
- a 10% (w/v) solution of a laccase/mediator system (see Example 1) solution that was freshly made, and a 10% (w/v) solution that was pre-incubated for 45 minutes at room temperature, were separately applied to denim and incubated it for 25 minutes at 40°C.
- the fabric was then rinsed and dried.
- the amount of color modification was determined using a chromameter (Table 2). The color modification was more pronounced when the solution of the laccase/mediator system was pre-incubated prior to application to the fabric.
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Abstract
Description
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US39431210P | 2010-10-18 | 2010-10-18 | |
PCT/US2011/056717 WO2012054485A1 (en) | 2010-10-18 | 2011-10-18 | Local color modification of dyed fabrics using a laccase system |
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EP2630291A1 true EP2630291A1 (en) | 2013-08-28 |
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EP11776663.4A Withdrawn EP2630291A1 (en) | 2010-10-18 | 2011-10-18 | Local color modification of dyed fabrics using a laccase system |
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US (1) | US20130269118A1 (en) |
EP (1) | EP2630291A1 (en) |
CN (1) | CN103189564A (en) |
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ITFI20120116A1 (en) * | 2012-06-11 | 2013-12-12 | Soko Chimica Srl | METHOD FOR THE ARTIFICIAL AGING OF FABRICS AND PACKAGED ITEMS |
CN104131429A (en) * | 2014-07-18 | 2014-11-05 | 晋江市龙兴隆染织实业有限公司 | Color retouching technology for correcting colored light by shaping padder through padding |
CN110643583B (en) * | 2019-11-06 | 2021-05-18 | 福州大学 | Laccase from trichoderma unicolor as well as gene and application thereof |
CN113756111B (en) * | 2021-10-08 | 2023-11-21 | 芽米科技(广州)有限公司 | Yellow lyocell fabric prepared by dyeing Blakeslea trispora fermentation extract and preparation method thereof |
CN114657731B (en) * | 2022-04-20 | 2023-08-29 | 广东溢达纺织有限公司 | Foam dyeing method capable of dyeing uneven fashion effect and obtained ready-made clothes or fabric |
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DK187280A (en) | 1980-04-30 | 1981-10-31 | Novo Industri As | RUIT REDUCING AGENT FOR A COMPLETE LAUNDRY |
US4822516A (en) | 1986-12-08 | 1989-04-18 | Kao Corporation | Detergent composition for clothing incorporating a cellulase |
JPH02238885A (en) | 1989-03-13 | 1990-09-21 | Oji Paper Co Ltd | Phenol oxidase gene recombination dna, microorganism transformed with same recombinant dna, culture mixture thereof and production of phenol oxidase |
DK115890D0 (en) | 1990-05-09 | 1990-05-09 | Novo Nordisk As | ENZYME |
FI903443A (en) | 1990-07-06 | 1992-01-07 | Valtion Teknillinen | FRAMSTAELLNING AV LACKAS GENOM REKOMBINANTORGANISMER. |
ES2174820T3 (en) | 1991-01-16 | 2002-11-16 | Procter & Gamble | COMPOSITIONS OF COMPACT DETERGENTS WITH HIGH ACTIVITY CELL. |
DK77393D0 (en) | 1993-06-29 | 1993-06-29 | Novo Nordisk As | ENZYMER ACTIVATION |
US5861271A (en) | 1993-12-17 | 1999-01-19 | Fowler; Timothy | Cellulase enzymes and systems for their expressions |
DE69526104T2 (en) | 1994-10-20 | 2002-11-07 | Novozymes As | BLEACHING METHOD USING A PHENOL OXIDIZING ENZYME SYSTEM AND A REINFORCING AGENT |
WO1997011217A1 (en) | 1995-09-19 | 1997-03-27 | Novo Nordisk A/S | Stain bleaching |
TR199902580T2 (en) * | 1997-04-17 | 2000-04-21 | Novo Nordisk Biochem North America, Inc. | Enzymatic etching pressure of dyed fabrics |
US6322596B1 (en) * | 1999-01-26 | 2001-11-27 | Kimberly-Clark Worldwide, Inc. | Method of decolorizing a dyed material in a predetermined pattern |
DE19940068A1 (en) * | 1999-08-24 | 2001-03-01 | Basf Ag | Process for lightening colored textile material |
US7413887B2 (en) | 2004-05-27 | 2008-08-19 | Genecor International, Inc. | Trichoderma reesei glucoamylase and homologs thereof |
CA2672603A1 (en) | 2006-12-18 | 2008-06-26 | Danisco Us, Inc., Genencor Division | Novel laccases, compositions and methods of use |
WO2009058956A1 (en) | 2007-11-01 | 2009-05-07 | Danisco Us, Inc. | Signal sequences and co-expressed chaperones for improving protein production in a host cell |
CA2747813A1 (en) * | 2008-12-24 | 2010-07-01 | Danisco Us Inc. | Laccases and methods of use thereof at low temperature |
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- 2011-10-18 AR ARP110103851A patent/AR083471A1/en unknown
- 2011-10-18 US US13/823,693 patent/US20130269118A1/en not_active Abandoned
- 2011-10-18 WO PCT/US2011/056717 patent/WO2012054485A1/en active Application Filing
- 2011-10-18 CN CN2011800500628A patent/CN103189564A/en active Pending
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CN103189564A (en) | 2013-07-03 |
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