EP0935692B1 - Tissu traite avec de la cellulase et de l'oxydoreductase - Google Patents

Tissu traite avec de la cellulase et de l'oxydoreductase Download PDF

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Publication number
EP0935692B1
EP0935692B1 EP97900194A EP97900194A EP0935692B1 EP 0935692 B1 EP0935692 B1 EP 0935692B1 EP 97900194 A EP97900194 A EP 97900194A EP 97900194 A EP97900194 A EP 97900194A EP 0935692 B1 EP0935692 B1 EP 0935692B1
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fabric
use according
cellulase
enzyme
alkyl
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EP0935692A1 (fr
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Thomas Vollmond
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Novozymes AS
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Novozymes AS
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    • 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
    • D06P1/00—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed
    • D06P1/44—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed using insoluble pigments or auxiliary substances, e.g. binders
    • D06P1/64—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed using insoluble pigments or auxiliary substances, e.g. binders using compositions containing low-molecular-weight organic compounds without sulfate or sulfonate groups
    • D06P1/651—Compounds without nitrogen
    • D06P1/65106—Oxygen-containing compounds
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/26—Organic compounds containing nitrogen
    • C11D3/28—Heterocyclic compounds containing nitrogen in the ring
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/34—Organic compounds containing sulfur
    • C11D3/349—Organic compounds containing sulfur additionally containing nitrogen atoms, e.g. nitro, nitroso, amino, imino, nitrilo, nitrile groups containing compounds or their derivatives or thio urea
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38645—Preparations containing enzymes, e.g. protease or amylase containing cellulase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38654—Preparations containing enzymes, e.g. protease or amylase containing oxidase or reductase
    • 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
    • D06P1/00—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed
    • D06P1/44—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed using insoluble pigments or auxiliary substances, e.g. binders
    • D06P1/64—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed using insoluble pigments or auxiliary substances, e.g. binders using compositions containing low-molecular-weight organic compounds without sulfate or sulfonate groups
    • D06P1/642—Compounds containing nitrogen
    • D06P1/6426—Heterocyclic 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
    • D06P1/00—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed
    • D06P1/44—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed using insoluble pigments or auxiliary substances, e.g. binders
    • D06P1/64—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed using insoluble pigments or auxiliary substances, e.g. binders using compositions containing low-molecular-weight organic compounds without sulfate or sulfonate groups
    • D06P1/651—Compounds without nitrogen
    • D06P1/65106—Oxygen-containing compounds
    • D06P1/65118—Compounds containing hydroxyl groups
    • 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
    • D06P1/00—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed
    • D06P1/44—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed using insoluble pigments or auxiliary substances, e.g. binders
    • D06P1/64—General processes of dyeing or printing textiles, or general processes of dyeing leather, furs, or solid macromolecular substances in any form, classified according to the dyes, pigments, or auxiliary substances employed using insoluble pigments or auxiliary substances, e.g. binders using compositions containing low-molecular-weight organic compounds without sulfate or sulfonate groups
    • D06P1/651—Compounds without nitrogen
    • D06P1/65168—Sulfur-containing compounds
    • D06P1/65193—Compounds containing sulfite or sulfone groups
    • 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
    • D06P5/02—After-treatment
    • D06P5/04—After-treatment with organic 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
    • D06P5/02—After-treatment
    • D06P5/04—After-treatment with organic compounds
    • D06P5/06—After-treatment with organic compounds containing nitrogen
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/34—Organic compounds containing sulfur
    • C11D3/3418—Toluene -, xylene -, cumene -, benzene - or naphthalene sulfonates or sulfates
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/34—Organic compounds containing sulfur
    • C11D3/3472—Organic compounds containing sulfur additionally containing -COOH groups or derivatives thereof
    • 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

  • the present invention relates to the use of cellulase, in combination with a phenol oxidising enzyme system and certain enhancing agents, for providing a worn look in dyed fabric, especially cellulosic fabric such as denim.
  • the first step in the processing evolution was to sell jeans that had been laundered by the manufacturer. These "pre-washed” jeans had a slightly faded appearance and a softer hand that felt comfortable, as though they had been laundered several times. This trend became fashionable as well, and consumers were willing to pay the extra cost involved for this additional processing.
  • the former is a result of removal (bleaching) of dye from the dyed warp yarn. Since the bleaching takes place on the whole surface of every dyed yarn, the result is a general reduction in colour intensity. Thus, the bleached look of a pair of indigo-dyed jeans is characterised by a lighter blue shade than the corresponding reference.
  • the latter - the worn look - is a result of a treatment of denim with cellulase and/or pumice stone.
  • This process is characterised by an uneven removal of dye from the fabric, hence it results in a high level of contrast between dyed areas and areas from which dye has been removed.
  • the worn look is obtained by a process involving cellulase and/or pumice stone
  • the bleached look can be obtained by a process involving non-enzymatic bleaching agents such as hypochlorite or by a process involving oxidoreductase and an enhancing agent.
  • the present invention relates to providing a worn but not bleached look, comprising a mild treatment with a cellulase and a simultaneous or subsequent mild treatment with an oxidoreductase and an enhancing agent.
  • the invention may be applied to any dyed fabric known in the art, in particular to synthetic fabrics such as polyester or to natural fabrics.
  • the invention is most beneficially applied to cellulose-containing fabrics, such as cotton, viscose, rayon, ramie, linen, Tencel, or mixtures thereof, or mixtures of any of these fibres, or mixtures of any of these fibres together with synthetic fibres.
  • the fabric is denim.
  • the fabric may be dyed with vat dyes such as indigo, or indigo-related dyes such as thioindigo.
  • the fabric may also be dyed with more than one dye, e.g., first with a sulphur dye and then with an indigo dye, or vice versa.
  • the fabric is an indigo-dyed denim with a sulphur-bottom,(i.e. the denim is first dyed with a sulphur dye and then with an indigo dye); including clothing items manufactured therefrom.
  • cellulase refers to an enzyme which catalyses the degradation of cellulose to glucose, cellobiose, triose and other cello-oligosaccharides.
  • cellulase is understood to include a mature protein or a precursor form thereof or a functional fragment thereof which essentially has the activity of the full-length enzyme.
  • cellulase is intended to include homologues or analogues of said enzyme.
  • homologues comprise an amino acid sequence exhibiting a degree of identity of at least 60% with the amino acid sequence of the parent enzyme, i.e. the parent cellulase. The degree of identity may be determined by conventional methods, see for instance, Altshul et al., Bull. Math. Bio. 48 , 1986, pp. 603-616, and Henikoff and Henikoff, Proc. Natl. Acad. Sci. USA 89 , 1992, pp. 10915-10919.
  • the cellulase to be used in the present invention is a monocomponent (recombinant) cellulase, i.e. a cellulase essentially free from other proteins or cellulase proteins.
  • a recombinant cellulase component may be cloned and expressed according to standard techniques conventional to the skilled person.
  • the cellulase to be used in the method is an endoglucanase (EC 3.2.1.4), preferably a monocomponent (recombinant) endoglucanase.
  • the cellulase is a microbial cellulase, more preferably a bacterial or fungal cellulase.
  • bacterial cellulases are cellulases derived from or producible by bacteria from the group of genera consisting of Pseudomonas or Bacillus, in particular Bacillus lautus.
  • the cellulase or endoglucanase may be an acid, a neutral or an alkaline cellulase or endoglucanase, i.e. exhibiting maximum cellulolytic activity in the acid, neutral or alkaline range, respectively.
  • a useful cellulase is an acid cellulase, preferably a fungal acid cellulase, which is derived from or producible by fungi from the group of genera consisting of Trichoderma, Actinomyces, Myrothecium, Aspergillus, and Botrytis.
  • a preferred useful acid cellulase is derived from or producible by fungi from the group of species consisting of Trichoderma viride , Trichoderma reesei , Trichoderma longibrachiatum, Myrothecium verrucaria , Aspergillus niger , Aspergillus oryzae, and Botrytis cinerea.
  • Another useful cellulase or endoglucanase is a neutral or alkaline cellulase, preferably a fungal neutral or alkaline cellulase, which is derived from or producible by fungi from the group of genera consisting of Aspergillus, Penicillium, Myceliophthora, Humicola, Irpex , Fusarium, Stachybotrys, Scopulariopsis, Chaetomium, Mycogone, Verticillium, Myrothecium, Papulospora, Gliocladium, Cephalosporium and Acremonium.
  • a preferred alkaline cellulase is derived from or producible by fungi from the group of species consisting of Humicola insolens, Fusarium oxysporum , Myceliopthora thermophila, or Cephalosporium sp., preferably from the group of species consisting of Humicola insolens, DSM 1800, Fusarium oxysporum, DSM 2672, Myceliopthora thermophila, CBS 117.65, or Cephalosporium sp., RYM-202.
  • a preferred example of a native or parent cellulase is an alkaline endoglucanase which is immunologically reactive with an antibody raised against a highly purified ⁇ 43kD endoglucanase derived from Humicola insolens, DSM 1800, or which is a derivative of the ⁇ 43kD endoglucanase exhibiting cellulase activity.
  • useful cellulases are variants having, as a parent cellulase, a cellulase of fungal origin, e.g. a cellulase derivable from a strain of the fungal genus Humicola, Trichoderma or Fusarium.
  • the concentration of the cellulase enzyme in the aqueous medium may be 0.1-250 ⁇ g of enzyme protein per g of fabric, in particular 0.5-50 ⁇ g of enzyme protein per g of fabric.
  • cellulase activity can be expressed in ECU.
  • Cellulolytic enzymes hydrolyse CMC, thereby increasing the viscosity of the incubation mixture.
  • the resulting reduction in viscosity may be determined by a vibration viscosimeter (e.g. MIVI 3000 from Sofraser, France).
  • Determination of the cellulolytic activity, measured in terms of ECU, may be determined according to the following analysis method (assay):
  • the ECU assay quantifies the amount of catalytic activity present in the sample by measuring the ability of the sample to reduce the viscosity of a solution of carboxy-methylcellulose (CMC).
  • the assay is carried out at 40°C; pH 7.5; 0.1M phosphate buffer; time 30 min; using a relative enzyme standard for reducing the viscosity of the CMC (carboxymethylcellulose Hercules 7 LFD) substrate; enzyme concentration approx. 0.15 ECU/ml.
  • the arch standard is defined to 8200 ECU/g.
  • a phenol oxidizing enzyme system is meant a system in which an enzyme, by using hydrogen peroxide or molecular oxygen, is capable of oxidizing organic compounds containing phenolic groups.
  • an enzyme by using hydrogen peroxide or molecular oxygen, is capable of oxidizing organic compounds containing phenolic groups. Examples of such enzymes are peroxidases and oxidases.
  • the source may be hydrogen peroxide or a hydrogen peroxide precursor for in situ production of hydrogen peroxide, e.g., percarbonate or perborate, or a hydrogen peroxide generating enzyme system, e.g., an oxidase and a substrate for the oxidase, or an amino acid oxidase and a suitable amino acid, or a peroxycarboxylic acid or a salt thereof.
  • Hydrogen peroxide may be added at the beginning of or during the process, e.g., in a concentration corresponding to 0.001-25 mM H 2 O 2 .
  • the enzyme of the phenol oxidizing enzyme system may be an enzyme exhibiting peroxidase activity or a laccase or a laccase related enzyme as described below.
  • the concentration of the phenol oxidizing enzyme in the aqueous medium may be 0.01-250 ⁇ g of enzyme protein per g of fabric, preferably 0.1-250 ⁇ g of enzyme protein per g of fabric, in particular 0.5-50 ⁇ g of enzyme protein per g of fabric.
  • An enzyme exhibiting peroxidase activity may be any peroxidase enzyme comprised by the enzyme classification (EC 1.11.1.7), or any fragment derived therefrom, exhibiting peroxidase activity, or synthetic or semisynthetic derivatives thereof (e.g. porphyrin ring systems or microperoxidases, cf. e.g. US 4,077,768, EP 537 381, WO 91/05858 and WO 92/16634).
  • Such enzymes are known from microbial, plant and animal origins.
  • the peroxidase employed in the method of the invention is producible by plants (e.g. horseradish or soybean peroxidase) or microorganisms such as fungi or bacteria.
  • Some preferred fungi include strains belonging to the subdivision Deuteromycotina, class Hyphomycetes, e.g., Fusarium, Humicola, Tricoderma, Myrothecium, Verticillum, Arthromyces, Caldariomyces, Ulocladium, Embellisia, Cladosporium or Dreschlera, in particular Fusarium oxysporum (DSM 2672), Humicola insolens, Trichoderma resii , Myrothecium verrucana (IFO 6113), Verticillum alboatrum, Verticillum dahlie, Arthromyces ramosus (FERM P-7754), Caldariomyces fumago , Ulocladium chartarum, Embellisia alli or Dreschl
  • fungi include strains belonging to the subdivision Basidiomycotina, class Basidiomycetes, e.g. Coprinus , Phanerochaete , Coriolus or Trametes, in particular Coprinus cinereus f. microsporus (IFO 8371), Coprinus macrorhizus, Phanerochaete chrysosporium (e.g. NA-12) or Trametes (previously called Polyporus), e.g. T. versicolor (e.g. PR4 28-A).
  • Basidiomycotina class Basidiomycetes
  • Coprinus cinereus f. microsporus IFO 8371
  • Coprinus macrorhizus Phanerochaete chrysosporium
  • Trametes previously called Polyporus
  • T. versicolor e.g. PR4 28-A
  • fungi include strains belonging to the subdivision Zygomycotina, class Mycoraceae, e.g. Rhizopus or Mucor, in particular Mucor hiemalis.
  • Some preferred bacteria include strains of the order Actinomycetales, e.g., Streptomyces spheroides (ATTC 23965), Streptomyces thermoviolaceus (IFO 12382) or Streptoverticillum verticillium ssp. verticillium.
  • Actinomycetales e.g., Streptomyces spheroides (ATTC 23965), Streptomyces thermoviolaceus (IFO 12382) or Streptoverticillum verticillium ssp. verticillium.
  • Bacillus pumilus ATCC 12905
  • Bacillus stearothermophilus Rhodobacter sphaeroides
  • Rhodomonas palustri Rhodomonas palustri
  • Streptococcus lactis Pseudomonas purrocinia
  • Pseudomonas fluorescens NRRL B-11
  • bacteria include strains belonging to Myxococcus, e.g., M. virescens.
  • the peroxidase may furthermore be one which is producible by a method comprising cultivating a host cell transformed with a recombinant DNA vector which carries a DNA sequence encoding said peroxidase as well as DNA sequences encoding functions permitting the expression of the DNA sequence encoding the peroxidase, in a culture medium under conditions permitting the expression of the peroxidase and recovering the peroxidase from the culture.
  • a recombinantly produced peroxidase is a peroxidase derived from a Coprinus sp ., in particular C. macrorhizus or C. cinereus according to WO 92/16634, or a variant thereof, e.g., a variant as described in WO 94/12621.
  • peroxidase acting compounds comprise peroxidase active fragments derived from cytochromes, haemoglobin or peroxidase enzymes, and synthetic or semisynthetic derivatives thereof, e.g. iron porphins, iron porphyrins, and iron phthalocyanine and derivatives thereof.
  • 1 peroxidase unit is the amount of enzyme that catalyzes the conversion of 1 ⁇ mole hydrogen peroxide per minute at the following analytical conditions: 0.88 mM hydrogen peroxide, 1.67 mM 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonate), 0.1 M phosphate buffer, pH 7.0, incubated at 30°C, photometrically followed at 418 nm.
  • laccases and laccase related enzymes contemplate any laccase enzyme comprised by the enzyme classification (EC 1.10.3.2), any chatechol oxidase enzyme comprised by the enzyme classification (EC 1.10.3.1), any bilirubin oxidase enzyme comprised by the enzyme classification (EC 1.3.3.5) or any monophenol mono-oxygenase enzyme comprised by the enzyme classification (EC 1.14.99.1).
  • the laccase enzymes are known from microbial and plant origin.
  • the microbial laccase enzyme may be derived from bacteria or fungi (including filamentous fungi and yeasts) and suitable examples include a laccase derivable from a strain of Aspergillus , Neurospora, e.g., N. crassa, Podospora, Botrytis, Collybia, 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. thermophila, Schytalidium, Polyporus, e.g., P. pinsitus , Phlebia, e.g., P. radita (WO 92/01046), or Coriolus, e.g., C. hirsutus (JP 2-238885).
  • the laccase or the laccase related enzyme may furthermore be one which is producible by a method comprising cultivating a host cell transformed with a recombinant DNA vector which carries a DNA sequence encoding said laccase as well as DNA sequences encoding functions permitting the expression of the DNA sequence encoding the laccase, in a culture medium under conditions permitting the expression of the laccase enzyme, and recovering the laccase from the culture.
  • LACU Laccase Activity
  • Laccase activity is determined from the oxidation of syringaldazin under aerobic conditions.
  • the violet colour produced is photometered at 530 nm.
  • the analytical conditions are 19 ⁇ M syringaldazin, 23.2 mM acetate buffer, pH 5.5, 30°C, 1 min. reaction time.
  • LACU laccase unit
  • enhancing agents are used that enhance the bleaching process.
  • the enhancing agent is an organic compound as defined by the formulas I and II in claim 1.
  • the enhancing agent of formula I is acetosyringone, syringaldehyde, syringic acid, methylsyringate, ethylsyringate, propylsyringate, butylsyringate, hexylsyringate, or octylsyringate.
  • enhancing agents described above may be prepared using methods well known to those skilled in the art; some of the enhancing agents are also commercially available, e.g., acetosyringone. Methylsyringate, ethylsyringate, propylsyringate, butylsyringate, hexylsyringate and octylsyringate may be produced as disclosed in Chem. Ber. 67 , 1934, p. 67.
  • the enhancing agent of formula II may be in particular 10-methylphenothiazine, phenothiazine-10-propionic acid, N-hydroxysuccinimide phenothiazine-10-propionate, 10-ethylphenothiazine-4-carboxylic acid, 10-ethylphenothiazine, 10-propylphenothiazine, 10-isopropylphenothiazine, methyl phenothiazine-10-propionate, 10-phenylphenothiazine, 10-allylphenothiazine, 10-(3-(4-methylpiperazin-1-yl)propyl)phenothiazine, 10-(2-pyrrolidin-1-yl-ethyl)phenothiazine, 2-methoxy-10-methyl-phenothiazine, 1-methoxy-10-methylphenothiazine, 3-methoxy-10-methylphenothiazine, 3,10-dimethylphenothiazine, 3,
  • the enhancing agents may be obtained from Sigma-Aldrich, Janssen Chimica, Kodak, Tokyo Kasai Organic Chemicals, Daiichi Pure Chemicals Co. or Boehringer Mannheim; N-methylated derivatives of phenothiazine and phenoxazine may be prepared by methylation with methyliodide as described by Cornel Bodea and Immun Silberg in "Recent Advances in the Chemistry of Phenothiazines" (Advances in heterocyclic chemistry, 1968, Vol. 9, pp. 321-460); B. Cardillo & G. Casnati in Tetrahedron, 1967, Vol. 23, p. 3771.
  • Phenothiazine and phenoxazine propionic acids may be prepared as described in J. Org. Chem. 15 , 1950, pp. 1125-1130. Hydroxyethyl and hydroxypropyl derivatives of phenothiazine and phenoxazine may be prepared as described by G. Cauquil in Bulletin de la Society Chemique de France, 1960, p.1049.
  • the enhancing agent used according to the invention may be present in concentrations of from 0.05 to 500 ⁇ mole per g denim, preferably 0.05 to 100 ⁇ mole per g denim, in particular 0.05 to 20 ⁇ mole per g denim.
  • the present invention is typically used in industrial machines for cellulase treatment of fabric.
  • the fabric is normally added to the machine according to the machine capacity per the manufacturer's instructions.
  • the fabric may be added to the machine prior to introducing water or the fabric may be added after water is introduced.
  • the cellulase treatment will be performed first, followed by the treatment with the phenol oxidizing enzyme system and the enhancing agent, but the two processes may also be performed simultaneously.
  • the cellulase may be present in the water prior to adding the fabric or it may be added after the fabric has been wetted. Normally a buffer will be used in order to be close to the pH optimum of the enzyme in question. After the fabric has been contacted with the cellulase it should be agitated in the machine for a sufficient period of time to ensure that the fabric is fully wetted and to ensure the action of the enzyme. Typically a reaction time between 5 and 60 minutes and a reaction temperature between 20°C and 90°C, preferably between 30°C and 80°C, more preferably between 40°C and 70°C, will be suitable.
  • the phenol oxidizing enzyme system and the enhancing agent of the invention may be present in the water prior to adding the fabric or they may be added after the fabric has been wetted.
  • the phenol oxidizing enzyme system may be added simultaneously with the enhancing agent or they may be added separately. Normally a buffer will be used in order to be close to the pH optimum of the enzyme in question.
  • a reaction time between 5 and 60 minutes and a reaction temperature between 20°C and 90°C, preferably between 30°C and 80°C, more preferably between 40°C and 70°C, will be suitable.
  • denim all manufactured by Levi Strauss & Co
  • the 5 types of denim were all of the "sulphur-bottom” type but the ratio between indigo and sulphur dye varied, as did the fabric construction.
  • Step 1 Abrasion with cellulase/pumice stone.
  • the denim was split into 2 different abrasion processes:
  • Step 2 Treatment with laccase and enhancing agent
  • the jeans from step 1 (except one of each type, which were kept as reference) were then treated with a laccase and an enhancing agent using following dosages and conditions:
  • a Wascator FOM 71 wash extractor was used for abrasion enhancement of the denim.
  • Denim load 0.8 kg Water 20 l Buffer 4.2 g Sodium acetate, 3 H 2 O 4.0 g Succinic acid pH 5.1
  • Enzyme 670 LACU Myceliophthora thermophila laccase (available from Novo Nordisk A/S) Enhancing agent 0.5 g Methyl syringate Time 20 minutes Temperature 60°C
  • a decrease in L* means an increase in blackness (decrease of white colour)
  • an increase in L* means an increase in whiteness (a decrease in black colour)
  • a decrease in a* means an increase in green colour (decrease in red colour)
  • an increase in a* means an increase in red colour (a decrease in green colour)
  • a decrease in b* means an increase in blue colour (a decrease in yellow colour)
  • an increase in b* means an increase in yellow colour (a decrease in blue colour).
  • the Texflash 2000 was operated in the L*a*b* coordinate system.
  • the light source used was a CIE light standard C. Each measurement was an average of 10 measurements.
  • the instrument was calibrated using calibration plates (black and white).
  • a Wascator FOM 71 wash extractor was used for abrasion enhancement of the denim.
  • the dosage of laccase and mediator was varied in 3 trials.
  • Denim load 0.8 kg Water 20 l Buffer 4.2 g sodium acetate, 3 H 2 O 4.0 g succinic acid pH 5.1
  • Enzyme Trametes villosa laccase (available from Novo Nordisk A/S)
  • a 300 LACU ( 5.9 ⁇ g laccase/g fabric)
  • B 600 LACU ( 11.7 ⁇ g laccase/g fabric)
  • C 900 LACU ( 17.6 ⁇ g laccase/g fabric)
  • the dosage of laccase and the dosage of enhancing agent below a certain limit (otherwise the result will be a bleached appearance). Also, it is seen that this limit depends on the dosage of cellulase in the abrasion step - the higher the cellulase dosage, the lower the limit is, i.e. according to the following approximate rules:

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  • Engineering & Computer Science (AREA)
  • Chemical & Material Sciences (AREA)
  • Textile Engineering (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Wood Science & Technology (AREA)
  • Organic Chemistry (AREA)
  • Biochemistry (AREA)
  • Microbiology (AREA)
  • General Chemical & Material Sciences (AREA)
  • Chemical Or Physical Treatment Of Fibers (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Detergent Compositions (AREA)
  • Coloring (AREA)
  • Treatments For Attaching Organic Compounds To Fibrous Goods (AREA)

Claims (17)

  1. Utilisation (a) d'une cellulose, selon une concentration correspondant à 0,1-250 µg de protéine enzymatique par gramme de tissu, et (b) simultanément, ou ultérieurement, d'un système enzymatique d'oxydation des phénols et d'un agent renforçateur, pour donner un aspect abradé à un tissu teint, dans un milieu aqueux, où l'agent renforçateur a la formule I :
    Figure 00320001
    dans laquelle R20 est Y, -CH=CH-Y ou -CH=CH-CH=CH-Y, où Y est choisi dans l'ensemble comprenant -CO-E, -SO2-E, -N-RR' et -N+-RR'R" où E est -H, -OH, -R ou -OR, et R et R' et R" peuvent être identiques ou différents et sont choisis chacun parmi -H ou un groupé alkyle en C1-C8, lequel groupe alkyle peut être saturé ou insaturé à chaíne droite ou ramifiée ; et R21 et R22 peuvent être identiques ou différents et sont choisis chacun parmi CmH2m+1 ; 1 ≤ m ≤ 5 ;
       ou la formule II :
    Figure 00320002
    dans laquelle formule X représente (-O-) ou (-S-), et les groupes substituants R1-R4 et R6-R9, qui peuvent être identiques ou différents, représentent chacun indépendamment des autres l'un quelconque des radicaux suivants : hydrogène, halogéno, hydroxy, formyle, carboxy, et leurs esters et sels, carbamoyle, sulfo et leurs esters et sels, sulfamoyle, nitro, amino, amino(alkyle en C1-C5), et R1-R9 représentent chacun l'un quelconque des radicaux suivants phényle, alkyle en C1-C14, alcoxy en C1-C5, carbonyl(alkyle en C1-C5), aryl (alkyle en C1-C5) ; lesquels groupes carbamoyle et sulfamoyle peuvent en outre être non substitués, ou substitués une ou deux fois par un groupe substituant R10 ; et lequel groupe phényle peut en outre être non substitué, ou substitué par un ou deux groupes substituants R10 ; et lesquels groupes alkyle en C1-C14, alcoxy en C1-C5, carbonyl (alkyle en C1-C5) et aryl (alkyle en C1-C5) peuvent être saturés ou insaturés à chaíne droite ou ramifiée et peuvent en outre être non substitués, ou substitués par un ou plusieurs groupes substituants R10 ;
       lequel groupe substituant R10 représente l'un quelconque des radicaux suivants : halogéno, hydroxy, formyle, carboxy et leurs esters et sels, carbamoyle, sulfo et leurs esters et sels, sulfamoyle, nitro, amino, phényle, aminoalkyle, pipéridino, pipérazinyle, pyrrolidino, alkyle en C1-C5, alcoxy en C1-C5 ;
       ou dans laquelle formule générale deux des substituants R1-R9 peuvent former ensemble un groupe -Z-, où Z représente l'un quelconque des groupes suivants : (-CHR10-N=N-) , (-CH=CH-)n, (-CH=N-)n ou (-N=CR10-NR11-), dans lesquels groupes n représente un entier de 1 à 3, R10 est un groupe substituant tel que défini ci-dessus et R11 est tel que défini pour R10.
  2. Utilisation selon la revendication 1, pour laquelle le tissu est teint avec un colorant de cuve.
  3. Utilisation selon la revendication 2, pour laquelle le colorant de cuve est l'indigo ou le thioindigo.
  4. Utilisation selon l'une quelconque des revendications 1 à 3, pour laquelle le tissu est un tissu cellulosique ou un mélange de fibres cellulosiques ou un mélange de fibres cellulosiques et de fibres synthétiques.
  5. Utilisation selon l'une quelconque des revendications 1 à 4, pour laquelle le tissu est un denim, de préférence un denim teint avec de l'indigo ou du thioindigo.
  6. Utilisation selon la revendication 1, pour laquelle la cellulase peut être obtenue à partir de Humicola, par exemple Humicola insolens, Fusarium par exemple Fusarium oxysporum, Myceliophthora, par exemple Myceliophthora thermophila ou Cephalosporium sp.
  7. Utilisation selon la revendication 1, pour laquelle la concentration de la cellulase correspond à 0,5-50 µg de protéine enzymatique par g de tissu.
  8. Utilisation selon la revendication 1, pour laquelle le système enzymatique d'oxydation des phénols est une peroxydase ou une source de peroxyde d'hydrogène.
  9. Utilisation selon la revendication 7, pour laquelle la peroxydase est la peroxydase du raifort, la peroxydase du soja ou une enzyme peroxydase pouvant être obtenue à partir de Coprinus, par exemple C. cinereus ou C. macrorhizus, ou de Bacillus, par exemple B. pumilus, ou Myxococcus, par exemple M. virescens.
  10. Utilisation selon la revendication 8 ou 9, pour laquelle la source de peroxyde d'hydrogène est le peroxyde d'hydrogène ou un précurseur de peroxyde d'hydrogène, par exemple un perborate ou un percarbonate, ou un système enzymatique générateur de peroxyde d'hydrogène, par exemple une oxydase et son substrat, ou un acide peroxycarboxylique ou un sel de ce dernier.
  11. Utilisation selon l'une quelconque des revendications 1 à 10, pour laquelle le milieu aqueux contient du H2O2 ou un précurseur de H2O2 à une concentration correspondant à 0,001-25 mM de H2O2.
  12. Utilisation selon la revendication 1, pour laquelle le système enzymatique d'oxydation des phénols est une laccase ou une enzyme apparentée à la laccase, avec de l'oxygène.
  13. Utilisation selon la revendication 12, pour laquelle la laccase peut être obtenue à partir de Trametes, par exemple Trametes villosa, Coprinus, par exemple Coprinus cinereus, ou Myceliophthora, par exemple Myceliophthora thermophila.
  14. Utilisation selon l'une quelconque des revendications 1 à 13, pour laquelle la concentration de l'enzyme d'oxydation des phénols correspond à 0,01-250 µg de protéine enzymatique par g de tissu, en particulier 0,5-50 µg de protéine enzymatique par g de tissu.
  15. Utilisation selon la revendication 1, pour laquelle l'agent renforçateur appartient à l'ensemble comprenant l'acétosyringone, le syringaldéhyde, le syringate de méthyle et l'acide syringique.
  16. Utilisation selon la revendication 1, pour laquelle l'agent renforçateur appartient à l'ensemble comprenant la 10-méthylphénothiazine, l'acide phénothiazine-10-propionique, l'acide phénoxazine-10-propionique, le phénoxazine-10-hydroxyéthyle, le phénothiazine-10-éthyl-4-carboxy, le chlorhydrate de promazine et l'alcool phénothiazine-10-éthylique.
  17. Utilisation selon l'une quelconque des revendications 1 à 16, pour laquelle l'agent renforçateur dans le milieu aqueux est présent à des concentrations de 0,05 à 500 µmoles par g de denim, de préférence de 0,05 à 100 µmoles par g de denim.
EP97900194A 1996-01-12 1997-01-08 Tissu traite avec de la cellulase et de l'oxydoreductase Expired - Lifetime EP0935692B1 (fr)

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JP3691516B2 (ja) * 1994-09-27 2005-09-07 ノボザイムス アクティーゼルスカブ アセトシリンゴンのような増強剤
DE69802204T2 (de) * 1997-09-08 2002-04-18 Unilever N.V., Rotterdam Verfahren zur verbesserung der enzymeaktivität
WO1999032652A1 (fr) * 1997-12-19 1999-07-01 Novo Nordisk A/S Modification de polysaccharides a l'aide d'une enzyme oxydant le phenol
WO2000050388A1 (fr) * 1999-02-24 2000-08-31 Sca Hygiene Products Zeist B.V. Procede de production d'ions nitrosonium
US7319112B2 (en) 2000-07-14 2008-01-15 The Procter & Gamble Co. Non-halogenated antibacterial agents and processes for making same
US8558058B2 (en) 2001-12-06 2013-10-15 Applied Biotechnology Institute Monocotyledonous seed expressing exo-1,4B-glucanase
WO2006032724A2 (fr) * 2004-09-21 2006-03-30 Ab Enzymes Oy Nouvelles enzymes laccase et leurs utilisations
JP5189364B2 (ja) * 2004-09-21 2013-04-24 アーベー エンザイムス オーワイ 新規ラッカーゼ酵素およびその使用
FI118339B (fi) 2004-09-21 2007-10-15 Ab Enzymes Oy Uusi lakkaasientsyymi ja sen käyttö
MX2011006779A (es) * 2008-12-24 2011-08-03 Danisco Us Inc Lacasas y metodos de uso de las mismas a temperatura baja.
US10308948B2 (en) 2011-07-27 2019-06-04 Applied Biotechnology Institute, Inc. Method of increasing expression of nucleic acid molecules in plants using multiple transcription units
EP2791330B1 (fr) 2011-12-16 2017-07-26 Novozymes, Inc. Polypeptides ayant une activité laccase et polynucléotides les codant
US10781428B2 (en) 2014-12-02 2020-09-22 Novozymes A/S Laccase variants and polynucleotides encoding same

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