US20110302722A1 - Laccases and methods of use thereof at low temperature - Google Patents

Laccases and methods of use thereof at low temperature Download PDF

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US20110302722A1
US20110302722A1 US13/142,247 US200913142247A US2011302722A1 US 20110302722 A1 US20110302722 A1 US 20110302722A1 US 200913142247 A US200913142247 A US 200913142247A US 2011302722 A1 US2011302722 A1 US 2011302722A1
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Prior art keywords
laccase
seq
textile
enzyme
mediator
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Wayne Ashton
Andreas J. Krouwer
Joseph C. McAuliffe
Piera M. Pericu
Huaming Wang
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Danisco US Inc
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Danisco US Inc
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    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/0004—Oxidoreductases (1.)
    • C12N9/0055—Oxidoreductases (1.) acting on diphenols and related substances as donors (1.10)
    • C12N9/0057—Oxidoreductases (1.) acting on diphenols and related substances as donors (1.10) with oxygen as acceptor (1.10.3)
    • C12N9/0061—Laccase (1.10.3.2)
    • D—TEXTILES; PAPER
    • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
    • D06L—DRY-CLEANING, WASHING OR BLEACHING FIBRES, FILAMENTS, THREADS, YARNS, FABRICS, FEATHERS OR MADE-UP FIBROUS GOODS; BLEACHING LEATHER OR FURS
    • D06L4/00—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs
    • D06L4/40—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs using enzymes
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/0004—Oxidoreductases (1.)
    • 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
    • D06P5/13—Fugitive dyeing or stripping 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
    • D06P5/13—Fugitive dyeing or stripping dyes
    • D06P5/137—Fugitive dyeing or stripping dyes with other compounds
    • 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
    • D—TEXTILES; PAPER
    • D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21C—PRODUCTION OF CELLULOSE BY REMOVING NON-CELLULOSE SUBSTANCES FROM CELLULOSE-CONTAINING MATERIALS; REGENERATION OF PULPING LIQUORS; APPARATUS THEREFOR
    • D21C5/00—Other processes for obtaining cellulose, e.g. cooking cotton linters ; Processes characterised by the choice of cellulose-containing starting materials
    • D21C5/005—Treatment of cellulose-containing material with microorganisms or enzymes
    • D—TEXTILES; PAPER
    • D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21H—PULP COMPOSITIONS; PREPARATION THEREOF NOT COVERED BY SUBCLASSES D21C OR D21D; IMPREGNATING OR COATING OF PAPER; TREATMENT OF FINISHED PAPER NOT COVERED BY CLASS B31 OR SUBCLASS D21G; PAPER NOT OTHERWISE PROVIDED FOR
    • D21H17/00—Non-fibrous material added to the pulp, characterised by its constitution; Paper-impregnating material characterised by its constitution
    • D21H17/005—Microorganisms or enzymes
    • D—TEXTILES; PAPER
    • D21—PAPER-MAKING; PRODUCTION OF CELLULOSE
    • D21H—PULP COMPOSITIONS; PREPARATION THEREOF NOT COVERED BY SUBCLASSES D21C OR D21D; IMPREGNATING OR COATING OF PAPER; TREATMENT OF FINISHED PAPER NOT COVERED BY CLASS B31 OR SUBCLASS D21G; PAPER NOT OTHERWISE PROVIDED FOR
    • D21H21/00—Non-fibrous material added to the pulp, characterised by its function, form or properties; Paper-impregnating or coating material, characterised by its function, form or properties
    • D21H21/14—Non-fibrous material added to the pulp, characterised by its function, form or properties; Paper-impregnating or coating material, characterised by its function, form or properties characterised by function or properties in or on the paper
    • D21H21/28—Colorants ; Pigments or opacifying agents

Definitions

  • the present systems, compositions, and methods relate to laccase enzymes and nucleic acid sequences encoding such laccase enzymes.
  • the laccase enzymes may be employed in conjunction with mediators in improved methods for modifying the color of denim fabrics.
  • 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, and as catalysts or facilitators for polymerization and oxidation reactions.
  • Laccases can be utilized for a wide variety of applications in a number of industries, including the detergent industry, the paper and pulp industry, the textile industry and the food industry.
  • phenol oxidizing enzymes are used as an aid in the removal of stains, such as food stains, from clothes during detergent washing.
  • Most laccases exhibit pH optima in the acidic pH range while being inactive in neutral or alkaline pHs.
  • 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 .
  • laccases having different performance profiles in various applications.
  • oxidizing efficiency of a laccase can be improved through the use of a mediator, also known as an enhancing agent.
  • a mediator also known as an enhancing agent.
  • Systems that include a laccase and a mediator are known in the art as laccase-mediator systems (LMS).
  • LMS laccase-mediator systems
  • the same compounds can also be used to activate or initiate the action of laccase.
  • mediators for use in a laccase-mediator system. These include HBT (1-hydroxybenzotriazole), ABTS [2,2′-azinobis(3-ethylbenzothiazoline-6-sulfinic acid)], NHA (N-hydroxyacetanilide), NEIAA (N-acetyl-N-phenylhydroxylamine), HBTO (3-hydroxy 1,2,3-benzotriazin-4(3H)-one), and VIO (violuric acid). In addition, there are several compounds containing NH—OH or N—O groups that have been found to be useful as mediators.
  • a textile processing method comprising contacting a textile with a laccase enzyme and, optionally, a mediator at a temperature less than 40° C., for a length of time and under conditions sufficient to cause a color modification of the textile.
  • the color modification is selected from lightening of color, change of color, change in color cast, reduction of redeposition/backstaining, and bleaching.
  • the temperature is from about 20° C. to less than 40° C. In some embodiments, the temperature is from about 20° to about 35° C. In some embodiments, the temperature is from about 20° C. to about 30° C.
  • the temperature is from about 20° C. to about 23° C. In some embodiments, the temperature is 20° C., 21° C., 22° C., 23° C., 24° C., 25° C., 26° C., 27° C., 28° C., 29° C., 30° C., 31° C., 32° C., 33° C., 34° C., or 35° C. In some embodiments, the temperature is the ambient temperature of tap water.
  • the textile is indigo-dyed denim
  • the textile is sulfur-dyed denim
  • the denim is desized and/or stonewashed prior to or simultaneously with contacting the textile with the laccase enzyme and the mediator. In some embodiments, the stonewashing and contacting the textile with the laccase enzyme and the mediator occur in the same bath.
  • the method further comprises contacting the textile with a cellulase enzyme, simultaneously or sequentially with contacting the textile with the laccase enzyme and the mediator.
  • contacting the textile with the cellulase enzyme and contacting the textile with the laccase enzyme and the mediator are performed sequentially, and wherein contacting the textile with the cellulase enzyme is performed prior to contacting the textile with the laccase enzyme and the mediator.
  • contacting the textile with the cellulase enzyme and contacting the textile with the laccase enzyme and the mediator are performed sequentially in the same bath without draining the bath between contacting the textile with a cellulase enzyme and contacting the textile with the laccase enzyme and the mediator.
  • contacting the textile with the cellulase enzyme and contacting the textile with the laccase enzyme and the mediator are performed a temperature less than 40° C.
  • the temperature is from about 20° C. to less than 40° C.
  • the temperature is from about 20° to about 35° C.
  • the temperature is from about 20° C. to about 30° C.
  • the temperature is from about 20° C. to about 23° C.
  • the temperature is 20° C., 21° C., 22° C., 23° C., 24° C., 25° C., 26° C., 27° C., 28° C., 29° C., 30° C., 31° C., 32° C., 33° C., 34° C., or 35° C.
  • the temperature is the ambient temperature of tap water.
  • the cellulase enzyme acts synergistically with the laccase enzyme to produce a textile with a greater degree of lightening of color of the textile, change in color, change in color cast, reduction of redoposition/backstaining, and/or bleaching. In some embodiments, the cellulase enzyme acts additively with the laccase enzyme to produce a textile with a greater degree of lightening of color of the textile, change in color, change in color cast, reduction of redoposition/backstaining, and/or bleaching in comparison to an identical method in which cellulase is not included.
  • the laccase is a microbial laccase. In some embodiments, laccase is from a Cerrena species. In some embodiments, the laccase is from Cerrena unicolor . In some embodiments, the laccase is laccase D from C. unicolor.
  • the laccase has an amino acid sequence that is at least 70% identical to an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 10, SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 16, SEQ ID NO: 18, SEQ ID NO: 19, and SEQ ID NO: 20.
  • the laccase has an amino acid sequence that is at least 80% identical to an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 10, SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 16, SEQ ID NO: 18, SEQ ID NO: 19, and SEQ ID NO: 20.
  • the laccase has an amino acid sequence that is at least 90%, or even at least 95%, identical to an amino acid sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 10, SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 16, SEQ ID NO: 18, SEQ ID NO: 19, and SEQ ID NO: 20.
  • the laccase has an amino acid sequence that is at least 70% identical to SEQ ID NO: 19 or SEQ ID NO: 20. In some embodiments, the laccase has an amino acid sequence that is at least 80% identical to SEQ ID NO: 19 or SEQ ID NO: 20. In some embodiments, the laccase has an amino acid sequence that is at least 90% identical to SEQ ID NO: 19 or SEQ ID NO: 20. In some embodiments, the laccase has an amino acid sequence that is at least 95% identical to SEQ ID NO: 19 or SEQ ID NO: 20.
  • the laccase enzyme and the mediator are provided together in a ready-to-use composition.
  • the laccase enzyme and the mediator are provided in a solid form.
  • the laccase enzyme and the mediator are provided as granules.
  • the mediator is syringonitrile.
  • laccases in another aspect, laccases, nucleic acid sequences encoding such laccases, and vectors and host cells for expressing the laccases are provided.
  • the laccases can be used at low temperatures in methods in which a reduction of energy input would be desirable, such as textile processing.
  • the laccase enzyme comprises, consists of, or consists essentially of the amino acid sequence depicted in any of SEQ ID NOs: 2, 4, 6, 8, 10, 12, 14, 16, 18, 19, or 20, or an amino acid sequence having at least about 60%, 65%, 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or even 99.5%, identical to any of SEQ ID NOs: 2, 4, 6, 8, 12, 14, 16, 18, 19, or 20.
  • the laccase has an amino acid sequence that is at least 70%, 80%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or even 99.5%, identical to SEQ ID NO: 19 or SEQ ID NO: 20.
  • the laccase has the amino acid sequence SEQ ID NO: 19 or SEQ ID NO: 20.
  • such polypeptides have laccase enzymatic activity, which can be determined, e.g., using the assays described, herein.
  • compositions comprising a laccase enzyme comprising, consisting of, or consisting essentially of any of the aforementioned amino acid sequences.
  • the composition further comprises a buffering system to maintain the pH of the composition at about 5.5 to about 6.5 in solution.
  • the composition further comprises a mediator.
  • the mediator may be selected from, e.g., acetosyringone, syringaldehyde, syringamide, methyl syringamide, 2-hydroxyehyl syringamide, methyl syringate, dimethylsyringamide, shrine acid, and 4-hydroxy-3,5-dimethoxybenzonitrile (syringonitrile).
  • the mediator is 4-hydroxy-3,5-dimethoxybenzonitrile.
  • the composition is in a solid form.
  • the laccase enzyme and the mediator are provided together in a ready-to-use composition.
  • the laccase enzyme and the mediator are provided in a solid form.
  • the laccase enzyme and the mediator are provided as granules.
  • the mediator is syringonitrile.
  • the laccase enzyme is used at a pH of about 5 to about 7, a temperature of about 20° C. to about 30° C., a liquor ratio of about 5:1 to about 10:1, and for a time period of about 15 to about 60 minutes.
  • FIG. 1 shows the effects of modifying the color of stonewashed denim with laccase enzymes at different temperatures, as described in Example 1.
  • FIG. 2 shows the effects of laccase and mediator ratios on modifying the color of stonewashed denim, as described in Example 2.
  • FIG. 3 shows the effect of temperature on modifying the color of stonewashed denim with a “ready to use” laccase composition, as described in Example 3.
  • FIG. 4 shows the effect of temperature on color-modifying performance of laccase enzymes on stonewashed denim, as described in Example 3.
  • FIG. 5 shows the effect of cellulase treatment in combination with laccase-mediated color modification, as described in Examples 4-6.
  • the systems, compositions, and methods are useful, for example, for low-temperature processing of textiles to affect color modification. Such processing uses less energy than conventional textile processing technologies, and involves more environmentally-friendly chemical reagents.
  • 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.
  • 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.
  • culturing refers to growing a population of microbial cells under suitable conditions in a liquid, semi-solid, or solid medium for expressing a polypeptide of interest. In some embodiments, culturing is conducted in a vessel or reactor, as known in the art.
  • 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.
  • expression refers to the process by which a polypeptide is produced based on the nucleic acid sequence of a gene.
  • the process includes both transcription and translation.
  • the term “expression vector” refers to a DNA construct containing a DNA coding sequence (e.g., gene sequence) that is operably linked to one or more suitable control sequence(s) capable of effecting expression of the coding sequence in a host.
  • control sequences include a promoter to effect transcription, an optional operator sequence to control such transcription, a sequence encoding suitable mRNA ribosome binding sites, and sequences which control termination of transcription and translation.
  • the vector may be a plasmid, a phage particle, or simply a potential genomic insert. Once transformed into a suitable host, the vector may replicate and function independently of the host genome, or may, in some instances, integrate into the genome itself.
  • the term “host cell” refers to a cell or cell line into which a recombinant expression vector for production of a polypeptide may be transfected, transformed, or otherwise introduced for expression of a polypeptide.
  • Host cells include progeny of a single host cell, and the progeny may not necessarily be identical (in morphology or in total genomic DNA complement) to the parent cell due to natural, accidental, or deliberate mutation.
  • a host cell may be bacterial or fungal.
  • a host cell includes a cell transfected or transformed in vivo with an expression vector.
  • the term “introduced,” in the context of inserting a nucleic acid sequence into a cell includes “transfection,” “transformation,” and “transduction,” and refers to the incorporation of a nucleic acid sequence into a eukaryotic or prokaryotic cell, wherein the nucleic acid sequence is incorporated into the genome of the cell (e.g., chromosome, plasmid, plastid, or mitochondrial DNA), converted into an autonomous replicon, or transiently expressed.
  • cleaning compositions and “cleaning formulations” refer to compositions that may be used for the removal of undesired compounds from items to be cleaned, such as fabrics, dishes, contact lenses, hair (shampoos), skin (soaps and creams), teeth (mouthwashes, toothpastes), and other solid and surfaces.
  • the terms encompass any materials/compounds selected for the particular type of cleaning composition desired and the form of the product (e.g., liquid, gel, granule, or spray composition), as long as the composition is compatible with the enzyme(s) used in the composition.
  • the specific selection of cleaning composition materials are readily made by considering the surface, item or fabric to be cleaned, and the desired form of the composition for the cleaning conditions during use.
  • the terms further refer to any composition that is suitable for cleaning, bleaching, disinfecting, and/or sterilizing a object and/or surface. It is intended that the terms include, but are not limited to detergent compositions (e.g., liquid and/or solid laundry detergents and fine fabric detergents; hard surface cleaning formulations, such as for glass, wood, ceramic and metal counter tops and windows; carpet cleaners; oven cleaners; fabric fresheners; fabric softeners; and textile and laundry pre-spotters, as well as dish detergents).
  • detergent compositions e.g., liquid and/or solid laundry detergents and fine fabric detergents
  • hard surface cleaning formulations such as for glass, wood, ceramic and metal counter tops and windows
  • carpet cleaners oven cleaners
  • fabric fresheners fabric softeners
  • textile and laundry pre-spotters as well as dish detergents
  • cleaning compositions and “cleaning formulations” include (unless otherwise indicated) granular or powder-form all-purpose or heavy-duty washing agents, especially cleaning detergents; liquid, gel or paste-form all-purpose washing agents, especially the so-called heavy-duty liquid (HDL) types; liquid fine-fabric detergents; hand dishwashing agents or light duty dishwashing agents, especially those of the high-foaming type; machine dishwashing agents, including the various tablet, granular, liquid and rinse-aid types for household and institutional use; liquid cleaning and disinfecting agents, including antibacterial hand-wash types, cleaning bars, mouthwashes, denture cleaners, car or carpet shampoos, bathroom cleaners; hair shampoos and hair-rinses; shower gels and foam baths and metal cleaners; as well as cleaning auxiliaries such as bleach additives and “stain-stick” or pre-treat types.
  • HDL heavy-duty liquid
  • cleaning and disinfecting agents including antibacterial hand-wash types, cleaning bars, mouthwashes, denture cleaners, car or carpet shampoos,
  • detergent composition and “detergent formulation” are used in reference to mixtures that are intended for use in a wash medium for the cleaning of soiled objects.
  • the term is used in reference to laundering fabrics and/or garments (e.g., “laundry detergents”).
  • laundry detergents e.g., “laundry detergents”.
  • the term refers to other detergents, such as those used to clean dishes, cutlery, etc. (e.g., “dishwashing detergents”).
  • detergent compositions and “detergent formulations” encompasses detergents that contain surfactants, builders, bleaching agents, bleach activators, bluing agents and fluorescent dyes, caking inhibitors, masking agents, enzyme activators, antioxidants, and solubilizers.
  • detergent stability refers to the stability of an enzyme, and optionally an associated substrate or mediator, in a detergent composition. In some embodiments, the stability is assessed during the use of the detergent, while in other embodiments, the term refers to the stability of a detergent composition during storage.
  • hard surface cleaning composition refers to detergent compositions for cleaning hard surfaces such as floors, walls, tiles, stainless steel vessels (e.g., fermentation tanks), bath and kitchen fixtures, and the like.
  • Such compositions may be provided in any form, including but not limited to solids, liquids, emulsions, and the like.
  • washwashing composition refers to all forms of compositions for cleaning dishes, including but not limited to granular and liquid forms.
  • fecting refers to the removal or killing of microbes, including fungi, bacteria, spores, and the like.
  • fabric cleaning composition refers a form of detergent composition for cleaning fabrics, including but not limited to, granular, liquid and bar forms.
  • polynucleotide As used herein, the terms “polynucleotide,” “nucleic acid,” and “oligonucleotide,” are used interchangeably to refers to a polymeric form of nucleotides of any length and any three-dimensional structure, whether single- or multi-stranded (e.g., single-stranded, double-stranded, triple-helical, etc.), which contain deoxyribonucleotides, ribonucleotides, and/or analogs or modified forms of deoxyribonucleotides or ribonucleotides, including modified nucleotides or bases or their analogs. Because the genetic code is degenerate, more than one codon may be used to encode a particular amino acid.
  • nucleotide or nucleotide analog may be used, so long as the polynucleotide retains the desired functionality under conditions of use, including modifications that increase nuclease resistance (e.g., deoxy, 2′-O-Me, phosphorothioates, etc.).
  • Labels may also be incorporated for purposes of detection or capture, for example, radioactive or nonradioactive labels or anchors, e.g., biotin.
  • polynucleotide also includes peptide nucleic acids (PNA).
  • PNA peptide nucleic acids
  • Polynucleotides may be naturally occurring or non-naturally occurring.
  • a sequence of nucleotides may be interrupted by non-nucleotide components.
  • phosphodiester linkages may be replaced by alternative linking groups.
  • phosphate may be replaced by P(O)S (“thioate”), P(S)S (“dithioate”), (O)NR 2 (“amidate”), P(O)R, P(O)OR′, CO or CH 2 (“formacetal”), in which each R or R′ is independently H or substituted or unsubstituted alkyl (1-20 C) optionally containing an ether (—O—) linkage, aryl, alkenyl, cycloalkyl, cycloalkenyl or araldyl. Not all linkages in a polynucleotide need be identical.
  • Polynucleotides may be linear or circular or comprise a combination of linear and circular portions.
  • 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 “primer” refers to an oligonucleotide, whether occurring naturally, e.g., as in a purified restriction fragment, or produced synthetically, which is capable of acting as a point of initiation of nucleic acid synthesis when incubated with a complementary nucleic acid in the presence of nucleotides and polymerase at a suitable temperature and pH.
  • the primer is preferably single stranded but may alternatively be double stranded. If double stranded, the primer is first treated to separate its strands before being used to prepare extension products.
  • the primer is an oligodeoxyribonucleotide. The exact lengths of the primers will depend on many factors, including temperature, source of primer and the use of the method.
  • the terms “recovered,” “isolated,” “purified,” and “separated” refer to a material (e.g., a protein, nucleic acid, or cell) that is removed from at least one component with which it is naturally-associated, or associated as the result of heterologous expression.
  • the term “textile(s)” 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 phrase “textile(s) in need of processing” refers to a textile that needs to be desized, scoured, bleached, and/or biopolished to produce a desired effect.
  • the phrase “textile(s) in need of color modification” refers to a textile that needs to be altered with respect to it color. These textiles may or may not have been already subjected to other treatments. Similarly, these textiles may or may not need subsequent treatments.
  • 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.
  • 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. Without being limited to a theory, it is proposed that color modification results from the modification of chromaphores associated with a textile material, thereby changing its visual appearance.
  • the chromophores may be naturally-associated with the material used to manufacture a textile (e.g., the white color of cotton) or associated with special finishes, such as dying or printing.
  • Color modification encompasses chemical modification to a chromophore as well as chemical modification to the material to which a chromophore is attached.
  • color modification examples 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
  • 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 terms “desize” and “desizing” refer to the process of eliminating/removing size (generally starch) from a textile, usually prior to applying special finishes, dyes or bleaches.
  • the term “desizing enzyme(s)” 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 al., 1990 and Altschul, et al., 1997.
  • Sequence searches are typically carried out using the BLASTN program when evaluating a given nucleic acid sequence relative to nucleic acid sequences in the GenBank DNA Sequences and other public databases.
  • 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.”
  • draining or “dropping” with respect to a bath in which textile materials are present refers to fully or partially releasing/emptying the solvent and reagents present in a bath. Draining a bath is typically performed between process steps such that the solvent and reagents present in one processing step do not interfere with a subsequent processing step. Draining may be accompanied by one or more rinse steps to further remove such the solvent and reagents.
  • 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.
  • pigment e.g., indigo
  • chromophore e.g., polyphenolic, anthocyanin, or carotenoid
  • other secondary substrate to and from which electrons can be shuttled by an enzyme exhibiting oxidase activity.
  • 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
  • Coriolus e.g., C. hirsutus (JP 2238885)
  • Spongipellis Polyporus
  • Ceriporiopsis subvermispora Ganoderma tsunodae
  • Trichoderma 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., H.
  • a host cell for expression of a laccase enzyme may also be from a species of Cerrena (e.g., C. unicolor ).
  • 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 B. 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 B. brevis
  • Pseudomonas e.g., Streptomyces (e.g., S. coelicolor, S. lividans ), or E. coli .
  • the transformation of bacterial cells may be performed according to conventional methods, e.g., as described in Maniatis, T.
  • 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. For example, laccases may be recovered from a culture medium as described in U.S. Patent Publication No. 2008/0196173. In some embodiments, 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 CBH1 promoter and terminator (see, e.g., U.S. Pat. No. 5,861,271).
  • the expression vector may be, e.g., pTrex3g, as disclosed in U.S. Pat. No. 7,413,887.
  • laccases are expressed as described in U.S. Patent Publication Nos. 2008/0196173 or 2009/0221030.
  • Polynucleotide sequence (SEQ ID NO: 1): ATGAGCTCAA AGCTACTTGC TCTTATCACT GTCGCTCTCG TCTTGCCACT 50 AGGCACCGAC GCCGGCATCG GTCCTGTTAC CGACTTGCGC ATCACCAACC 100 AGGATATCGC TCCAGATGGC TTCACCCGAC CAGCGGTACT AGCTGGGGGC 150 ACATTCCCTG GAGCACTTAT TACCGGTCAG AAGGTATGGG AGATCAACTT 200 GGTTGAATAG AGAAATAAAA GTGACAACAA ATCCTTATAG GGAGACAGCT 250 TCCAAATCAA TGTCATCGAC GAGCTTACCG ATGCCAGCAT GTTGACCCAG 300 ACATCCATTG TGAGTATAAT TTAGGTCCGC TCTTCTGGCT ATCCTTTCTA 350 ACTCTTACCG TCTAGCATTG GCACGGCTTC TTTCAGAAGG GATCTGCGTG 400 GGCCGATGGT CCTGCCTTCG TTACTCAATG
  • Polynucleotide sequence (SEQ ID NO: 3): ATGAGCTCAA AGCTACTTGC TCTTATTACT GTCGCTCTCG TCTTGCCACT 50 AGGCACTGAC GCCGGCATCG GTCCTGTTAC CGACTTGCGC ATCACCAACC 100 AGGATATCGC TCCAGATGGC TTCACCCGAC CAGCTGTACT GGCTGGGGGC 150 ACATTCCCCG GAGCACTGAT TACCGGTCAG AAGGTATGGG AGATCGATTT 200 CGTTGAATAG AGAAATACAA CTGAAAACAA ATTCTTATAG GGAGACAGCT 250 TCCAAATCAA TGTCATCGAC GAGCTTACCG ATGCCAGCAT GTTGACCCAG 300 ACATCCATTG TGAGTATAAT ATGGGTCCGC TCTTCTAGCT ATCCTTTCTA 350 ACTCTTACCC TCTAGCATTG GCACGGCTTC TTTCAGAAGG GATCTGCGTG 400 GGCCGATGGT CCTGCCTTCG TTACTCAATG
  • Polynucleotide sequence (SEQ ID NO: 5): ATGTCTCTTC TTCGTAGCTT GACCTCCCTC ATCGTACTAG TCATTGGTGC 50 ATTTGCTGCA ATCGGTCCAG TCACTGACCT ACATATAGTG AACCAGAATC 100 TCGACCCAGA TGGTTTCAAC CGCCCCACTG TACTCGCAGG TGGTACTTTC 150 CCCGGTCCTC TGATTCGTGG TAACAAGGTA CGCTTCATAA CCGCCCTCCG 200 TAGACGTAGG CTTCGGCTGA CATGACCATC ATCTGTAGGG AGATAACTTT 250 AAAATTAATG TGATTGACGA CTTGACAGAG CACAGTATGC TCAAGGCTAC 300 GTCCATCGTA AGTCCCTGAT TAACGTTTCA CCTGGTCATA TCGCTCAACG 350 TCTCGAAGCA CTGGCATGGG TTCTTCCAGA AGGGAACCAA CTGGGCCGAT 400 GGCCCCGCCT TTGTCACCCA ATGTCC
  • Polynucleotide sequence (SEQ ID NO: 7): CACCGCGATG TCTCTTCTTC GTAGCTTGAC CTCCCTCATC GTACTAGCCA 50 CTGGTGCATT TGCTGCAATC GGTCCAGTCA CCGACCTACA TATAGTGAAC 100 CAGAATCTCG CCCCAGATGG TTTAAACCGC CCCACTGTAC TCGCAGGTGG 150 TACTTTCCCC GGTCCTCTGA TTCGTGGTAA CAAGGTACGC TTCATAACCG 200 CCCTCCGTAG ACGTAGGCTT CGGCTGACAT GACCATCATC TGTAGGGAGA 250 TAACTTTAAA ATTAATGTGA TTGACGACTT GACAGAACAC AGTATGCTCA 300 AGGCTACGTC CATTGTAAGT CCCTGATTAA CGTTTCACCT GGTCATATCG 350 CTCAACGTCT CGAAGCACTG GCATGGGTTC TTCCAGAAGG GAACCAACTG 400 GGCCGATGGC CCCGCCTTTG TCACC
  • Polynucleotide sequence (SEQ ID NO: 13): GATTCTAATA GACCAGGCAT ACCAAGAGAT CTACAGGTTG ACAGACCATT 50 CTTCTAGGCG GCATTTATGC TGTAGCGTCA GAAATTATCT CTCCATTTGT 100 ATCCCACAGG TCCTGTAATA ACACGGAGAC AGTCCAAACT GGGATGCCTT 150 TTTTCTCAAC TATGGGCGCA CATAGTCTGG ACGATGGTAT ATAAGACGAT 200 GGTATGAGAC CCATGAAGTC AGAACACTTT TGCTCTCTGA CATTTCATGG 250 TTCACACTCT CGAGATGGGA TTGAACTCGG CTATTACATC GCTTGCTATC 300 TTAGCTCTGT CAGTCGGAAG CTATGCTGCA ATTGGGCCCG TGGCCGACAT 350 ACACATTGTC AACAAAGACC TTGCTCCAGA TGGCGTACAA CGTCCAACCG 400 TGCTTGCCGG AGGCACTTTT CCTG
  • Polynucleotide sequence (SEQ ID NO: 17): TGCAATCGGA CCGGTGGCCG ACCTCAAGAT CGTAAACCGA GACATTGCAC 50 CTGACGGTTT TATTCGTCCC GCCGTTCTCG CTGGAGGGTC GTTCCCTGGT 100 CCTCTCATTA CAGGGCAGAA AGTACGTTAC GCTATCTCGG TGCTTTGGCT 150 TAATTAAACT ATTTGACTTT GTGTTCTCTT AGGGGAACGA GTTCAAAATC 200 AATGTAGTCA ATCAACTGAC CGATGGTTCT ATGTTAAAAT CCACCTCAAT 250 CGTAAGCAGA ATGAGCCCTT TGCATCTCGT TTTATTGTTA ATGCGCCCAC 300 TATAGCATTG GCATGGATTC TTCCAGAAGG GAACAAACTG GGCAGACGGT 350 CCTGCGTTCG TGAACCAATG TCCAATCGCC ACGAACAATT CGTTCTTGTA 400 TCAGTTTACC TCACAGGAAC AGCCAG
  • the mature processed form of this polypeptide is as follows (SEQ ID NO: 20):
  • 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: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 10, SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 16, SEQ ID NO: 18, SEQ ID NO: 19, and SEQ ID NO: 20.
  • such polypeptides have enzymatic laccase activity, as determined using the assays and procedures
  • 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: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 10, SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 16, SEQ ID NO: 18, SEQ ID NO: 19, and SEQ ID NO: 20.
  • 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 enzymatic oxidation 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:
  • A is a group such as —R, -D, —CH ⁇ CH-D, —CH ⁇ CH—CH ⁇ CH-D, —CH ⁇ N-D, —N ⁇ N-D, or —N ⁇ CH-D
  • D is selected from the group consisting of —CO-E, —SO 2 -E, —CN, —NXY, and —N + XYZ
  • E is —H, —OH, —R, —OR, or —NXY
  • X, Y, and Z are independently selected from —H, —OH, —OR, and —R; where R is a C 1 -C 16 alkyl, preferably a C 1 -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+1 ; 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 C 1 -C 16 alkyl, preferably a C 1 -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+1 ; 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 concentration of about 0.005 to about 1.000 mmole per g denim, about 0.05 to about 500 mmole per g denim, about 0.1 to about 100 mmole per g denim, about 1 to about 50 ⁇ mole per g denim, or about 2 to about 20 ⁇ mole per g denim
  • 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. Pat. No. 5,752,980. Other suitable mediators are described in, e.g., U.S. Patent Publication No. 2008/0189871.
  • the present systems and compositions can be use in applications where enzymatic laccase activity is useful or desirable.
  • these applications/methods is color modification of a substrate, which may be associated with a textile.
  • such methods include incubation of a laccase enzyme with a suitable substrate at a low temperature, for example, about 40° C. or less.
  • the temperature is between about 20° C. and about 40° C.
  • the temperature is between about 20° to about 35° C.
  • the temperature is about 20° C., 25° C., 30° C., or 35° C.
  • the temperature is the ambient temperature of tap water, for example, about 20° C. to about 23° C. The temperature may be maintained within a narrow range or allowed to fluctuate without significantly affecting the performance of the system and compositions.
  • the laccase is from a Cerrena species, such as C. unicolor .
  • 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 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% identity to any of the C. unicolor laccase enzymes described herein, and having laccase enzymatic activity.
  • the systems and methods are used in a textile processing method, for example a method for modifying the color of a textile product, including, e.g., fibers, yarns, cloth, or complete garments.
  • the methods involve contacting the textile with a laccase and a mediator for a length of time, and under conditions, sufficient to result in at least one (i.e., one or more) measurable effects selected from, e.g., a change in color, a change in color cast, lightening, bleaching, fading, and/or a reduction of redeposition/backstaining.
  • the methods are used to impart a “vintage look” to dyed denim products.
  • the vintage look has a less intense blue/violet tint and more subdued grey appearance than the freshly-dyed denim.
  • the vintage look is faded without the brown tint that can result from hypochlorite treatment. Accordingly, while an aspect of the color modification obtained using laccases can be characterized as a “bleaching” affect, this term does not fully describe the color modifications possible using laccases.
  • Textiles provided for color modification may be a cellulosic textiles or blends of cellulosic and synthetic fibers.
  • 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 denim may optionally be desized and/or stonewashed prior to color modification with the laccase enzyme.
  • denim strength is reduced to a greater degree at a higher temperature, compared to a lower temperature.
  • the present methods can be performed at lower temperatures compared to conventional methods, they have the advantage of reducing the damage to textiles during processing compared to conventional methods.
  • laccase enzymes generally do not react with cellulosic textile fibers to reduce their strength during processing. Accordingly, in some embodiments, the present methods do not affect the physical strength of the denim, or reduce the loss of physical strength compared to conventional methods.
  • the denim is stretch denim comprising, e.g., elastane or spandex
  • the present methods do not affect the stretch performance of the fabric, or reduce the loss of stretch performance compared to conventional methods.
  • the laccase is used in a textile processing method in combination with at least one other enzyme. Where such processing is simultaneous, enzymatic treatment may be performed at a low temperature as described herein. Where the processing is sequential, the laccase may be used at a low temperature as described herein, and the other enzyme(s) may optionally also be used at a low temperature. In some embodiments, the laccase is used in combination with a cellulase enzyme, either simultaneously or sequentially. In one embodiment, the textile is contacted with the laccase and cellulase simultaneously. In another embodiment, the textile is contacted with the laccase and cellulase sequentially.
  • the textile is contacted with the cellulase first to effect “stonewashing,” and then with the laccase to affect color modification.
  • the textile is contacted with the laccase first, and then with the cellulase.
  • cellulase and laccase treatments are sequential, the two processing steps can be performed in the same bath, and without draining the bath between treatments. Such methods are referred to as “single-bath” methods.
  • Suitable cellulases may be derived from microorganisms which are known to be capable of producing cellulolytic enzymes, such as, 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. Pat. 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.
  • enzymatic “stonewashing” using a cellulase, bleaching using an aryl esterase, and color modification 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.
  • Laccases can also be used in other aspects of textile manufacturing, generally including aspects of treatment, processing, finishing, polishing, production of fibers, or the like.
  • laccases can be used in de-coloring dyed waste (including indigo-dyed waste), in fabric dyeing, in textile bleaching work-up, in fiber modification; in achieving enhanced fiber or fabric properties, and the like.
  • the present systems and compositions may also be used in a method for modifying the color of wool.
  • European Patent No. EP 0 504 005 discloses that laccases can be used for dyeing wool. Laccases can also be used in the leather industry. For example, laccases can be used in the processing of animal hides including but not limited to de-hairing, liming, bating and/or tanning of hides.
  • the present systems and compositions may also be used in a method for modifying the color of pulp or paper products. Such methods involve contacting the pulp or paper product in need of color modification with a laccase as described, herein, for a length of time and under conditions sufficient for color modification to occur.
  • the color modification is bleaching.
  • the present systems and compositions may also be used in a method for hair color modification.
  • Laccases have reportedly been found to be useful for hair dyeing (see, e.g., WO 95/33836 and WO 95/33837). Such methods involve contacting the hair having a color to be modified with the laccase for a length of time and under conditions suitable for changing the color of the hair.
  • laccases can be used in decolorization of colored compounds; in detoxification of phenolic components; for anti-microbial activity (e.g., in water recycling); in bio-remediation; etc.
  • the present systems and compositions may also be used in the depolymerization of high-molecular-weight aggregates, deinking waste paper, the polymerization of aromatic compounds, radical-mediated polymerization and cross-linking reactions (e.g., paints, coatings, biomaterials), the activation of dyes, and coupling organic compounds.
  • radical-mediated polymerization and cross-linking reactions e.g., paints, coatings, biomaterials
  • laccases can be used in the cleaning, treatment or care of laundry items such as clothing or fabric; in the cleaning of household hard surfaces; in dish care, including machine dishwashing applications; and in soap bars and liquids and/or synthetic surfactant bars and liquids.
  • the enzymes presented herein can be useful, for example, in stain removal/de-colorization, and/or in the removal of odors, and/or in sanitization, etc.
  • Laccase mediators can be used as sanitization and antimicrobial agents (e.g., wood protection, detergents), independently of or in conjunction with laccase enzymes.
  • Laccases can be used in other aspects of field of personal care.
  • laccases can be used in the preparation of personal products for humans such as fragrances, and products for skin care, hair care, oral hygiene, personal washing and deodorant and/or antiperspirants, for humans.
  • Laccases can be useful, for example, in hair dyeing and/or bleaching, nails dyeing and/or bleaching; skin dyeing and/or bleaching; surface modification (e.g., as coupling reagent); as an anti-microbial agent; in odor removal; teeth whitening; etc.
  • Laccases can be used in the field of contact lens cleaning.
  • laccases can be used in the cleaning, storage, disinfecting, and/or preservation of contact lenses.
  • Laccases can be used in the field of bio-materials.
  • laccases can be used as bio-catalysts for various organic reactions; and/or in connection with biopolymers; in connection with packaging; in connection with adhesives; in surface modification (activation and coupling agent); in production of primary alcohols; in connection with biosensors and/or organic syntheses; etc.
  • Laccases are capable of oxidizing a wide variety of colored compounds having different chemical structures, using oxygen as the electron acceptor.
  • the present systems and compositions may also be used for the removal of lignin from lignocellulose-containing material (e.g., the delignification of pulp), the bleaching of lignocellulose-containing material (i.e. the enzymatic de-inking of recycled paper) and/or the treatment of waste water arising from the manufacture of paper or cellulose.
  • lignin e.g., the delignification of pulp
  • bleaching of lignocellulose-containing material i.e. the enzymatic de-inking of recycled paper
  • waste water arising from the manufacture of paper or cellulose.
  • Such processes may use a laccase enzyme in combination with adding or metering-in non-aromatic redox agents plus phenolic and/or non-phenolic aromatic redox compounds, the phenolic and non-phenolic units of the lignin either being oxidized directly by the action of these phenolic and/or non-phenolic aromatic compounds, or the lignin being oxidized by other phenolic and/or non-phenolic compounds produced by the oxidizing action of these compounds.
  • Laccases can be used in other aspects relating to pulp and paper.
  • laccases can be used in the manufacture of paper pulps and fluff pulps from raw materials such as wood, bamboo, and cereal rice straw; the manufacture of paper and boards for printing and writing, packaging, sanitary and other technical uses; recycling of cellulose fiber for the purpose of making paper and boards; and the treatment of waste products generated by and treated at pulp or paper mills and other facilities specifically dedicated to the manufacture of paper, pulp, or fluff.
  • Laccases can be useful, for example, in wood processing; in pulp bleaching; in wood fiber modification; in bio-glue (lignin activation) for MDF manufacturing; for enhanced paper properties; in ink removal; in paper dyeing; in adhesives (e.g. lignin based glue for particle- or fiber boards); etc.
  • Laccases can be used in the field of feed.
  • the laccases can be used as a feed additive alone or as part of a feed additive with the aim to increase the nutritional value of feed for any kind of animals such as chicken, cows, pigs, fish and pets; and/or as a processing aid to process plant materials and food industry by products with the aim to produce materials/products suitable as feed raw materials.
  • Laccases can be used in the field of starch processing.
  • laccases can be used in the processing of a substrate including starch and/or grain to glucose (dextrose) syrup, fructose syrup or any other syrup, alcohol (potable or fuel) or sugar.
  • starch processing may include processing steps such as liquefaction, saccharification, isomerization, and de-branching of a substrate.
  • Laccases can be used in the field of food.
  • laccases can be used in the preparation, processing, or as an active ingredient in foods such as yellow fat, tea based beverages, culinary products, bakery, and frozen foods for human consumption.
  • Laccases can be used, for example, as a bread improver, in food preservation, as an oxygen scavenger, etc.
  • Laccases can be used for reducing or eliminating the microbial load of various foods (e.g., meats) or feed.
  • any of the methods or uses for laccases described herein may be performed at a low temperature, e.g., at a temperature lower than about 40° C., e.g., less than about 40° C., less than about 37° C., less than about 35° C., less than about 32° C., less than about 30° C., less than about 27° C., less than about 25° C., and less than about 22° C.
  • Exemplary temperature ranges are from about 20° C. to less than about 40° C.
  • Exemplary temperatures are 20° C., 21° C., 22° C., 23° C., 24° C., 25° C., 26° C., 27° C., 28° C., 29° C., 30° C., 31° C., 32° C., 33° C., 34° C., or 35° C.
  • the temperature is at room temperature or the ambient temperature of tap water, for example, about 20° C. to about 23° C.
  • laccases are used at a concentration of about 0.005 to about 5000 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 5000 mg/kg of denim, about 0.05 to about 500 mg/kg of denim, about 0.1 to about 100 mg/kg of denim, or about 0.5 to about 10 mg/kg of denim.
  • a laccase is used at a pH of 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, and 7.0.
  • the present compositions include one or more laccases, and optionally one or more mediators.
  • the compositions comprise a polypeptide comprising, consisting of, or consisting essentially of an amino acid sequence selected from SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 10, SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 16, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20, or a variant or fragment, thereof.
  • the compositions comprise a polypeptide comprising, consisting of, or consisting essentially of an amino acid sequence selected from SEQ ID NO: 19 and 20, or a variant or fragment, thereof.
  • such polypeptides have enzymatic laccase activity, which can be determined using the assays and procedures described, herein
  • composition can also be provided in the form of a “ready to use” (RTU) composition
  • RTU ready to use
  • the mediator is selected from acetosyringone, syringaldehyde, syringamide, methyl syringamide, 2-hydroxyethyl syringamide, methyl syringate, syringonitrile, dimethylsyringamide, and syringic acid.
  • the mediator is syringonitrile (4-hydroxy-3,5-dimethoxybenzonitrile).
  • the RTU composition may further contain one or more compounds to provide a pH buffer when the composition is in solution.
  • the composition contains monosodium phosphate and adipic acid as a buffering system.
  • the RTU composition may be in a solid, granular form for ease of storage and transportation. The composition is then diluted with water to provide an aqueous solution for use, e.g., as described.
  • RTU compositions may also include any number of additional reagents, such as dispersants, surfactant, blockers, polymers, preservatives, and the like.
  • Granular Laccase D enzyme from Cerrena unicolor (38,000 U/g) was used in this experiment.
  • One laccase unit is defined as the amount of laccase activity that oxidizes 1 nmol of ABTS substrate per second under conditions of an assay based on the ability of laccase enzyme to oxidize ABTS (2,2′-azinobis(3-ethylbenzthiazoline-6-sulfonate)) into its corresponding stable cation radical, ABTS + .
  • Accumulation of the radical causes the ABTS to turn a dark green color and an increase in absorbance at 420 nm. The color formation is proportional to laccase activity and is monitored against a laccase standard.
  • laccase treatment was performed in a Unimac UF 50 washing machine according to the following process:
  • the amount of color modification, reported as “bleaching,” of denim legs was evaluated after laccase treatment with a Minolta Chromameter CR 310 in the CIE Lab color space with a D 65 light source.
  • the CIE color space also known as the CIELUV color space, was adopted by the International Commission on Illumination (CIE) in 1976, and involves the values L*, u*, and v* calculated as follows:
  • RTU ready-to-use
  • the denim was stonewashed and bleached in a Unimac UF 50 washing machine under the following conditions:
  • the denim was bleached in a Unimac UF 50 washing machine under the following conditions:
  • This Example shows that effective stonewashing and color modification can be obtained using laccase and cellulase in a single-bath process.
  • PRIMAGREEN® EcoFade LT 100 laccase (Batch No. 780913616, 6,292 GLacU/g).
  • the denim was stonewashed in a Renzacci LX 22 washing machine under the following conditions:
  • This Example shows that effective stonewashing and color modification can be obtained using pumice stones and a laccase-mediator system in a single-bath process.
  • PRIMAGREEN® EcoFade LT 100 laccase (Batch No. 7809136160, 6,292 GLacU/g).
  • laccase treatment provides color modification even if pumice stones are present, and further shows reduction/removal of backstaining.
  • test garments were made of 100% cotton Twill fabric dyed with sulphur khaki brown dye. 21 garments weighing approximately 7 kg (total) were stonewashed in a 25 kg belly washer (36 rpm) under the following conditions:
  • PRIMAGREEN® EcoFade LT 100 laccase (Batch No. 780913616, 6,292 GLacU/g).

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