EP0424398A1 - Additif de detergent pour le blanchissage de tissu. - Google Patents

Additif de detergent pour le blanchissage de tissu.

Info

Publication number
EP0424398A1
EP0424398A1 EP89905395A EP89905395A EP0424398A1 EP 0424398 A1 EP0424398 A1 EP 0424398A1 EP 89905395 A EP89905395 A EP 89905395A EP 89905395 A EP89905395 A EP 89905395A EP 0424398 A1 EP0424398 A1 EP 0424398A1
Authority
EP
European Patent Office
Prior art keywords
peroxidase
detergent additive
hydrogen peroxide
additive according
oxidase
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Granted
Application number
EP89905395A
Other languages
German (de)
English (en)
Other versions
EP0424398B1 (fr
Inventor
Ole Kirk
Ture Damhus
Sven Erik Gotfredsen
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Novo Nordisk AS
Original Assignee
Novo Nordisk AS
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Family has litigation
First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=8110229&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=EP0424398(A1) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.
Application filed by Novo Nordisk AS filed Critical Novo Nordisk AS
Priority to AT89905395T priority Critical patent/ATE73485T1/de
Publication of EP0424398A1 publication Critical patent/EP0424398A1/fr
Application granted granted Critical
Publication of EP0424398B1 publication Critical patent/EP0424398B1/fr
Anticipated expiration legal-status Critical
Revoked legal-status Critical Current

Links

Classifications

    • 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
    • C11D3/395—Bleaching agents
    • 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
    • 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
    • C11D3/39—Organic or inorganic per-compounds

Definitions

  • the present invention relates to a detergent additive comprising an enzyme system capable of exerting a bleaching effect on fabrics in the course of washing procedures, a detergent composition containing the detergent additive as well as a process for bleaching fabrics by treating the fabrics with an enzyme exerting a bleaching effect.
  • perborate and percarbonate bleaching The detailed mechanism of perborate and percarbonate bleaching is not known at present, but it is generally assumed that hydrogen peroxide converts coloured substances responsible for the staining of fabric into un- coloured materials by oxidation and that some oxidation of the coloured substances may also take place due to their direct interaction with perborate or percarbonate.
  • the present invention relates to a detergent additive capable of exerting a bleaching effect on fabrics and comprising an enzyme exhibiting a peroxidase effect.
  • the detergent additive of the invention will usually also comprise hydrogen peroxide or a precursor of hydrogen peroxide, preferably perborate or percarbonate.
  • the term "enzyme exhibiting a peroxidase effect" is understood to indicate an enzyme with a mode of action similar to that of peroxidase and will be used synonymously therewith.
  • peroxidases act on various amino and phenolic compounds resulting in the production of a colour. In view of this, it must be considered surprising that peroxidases may also exert a bleaching effect on coloured substances.
  • peroxidase will generally show affinity for coloured substances present in the stain which act as substrates for the enzyme (these will typically be natural dyestuffs such as various polyphenols) , bleaching will be targeted to the stains, for which reason a more efficient utilization of hydrogen peroxide is obtained by employing peroxidase for bleaching than with the conventional bleaching methods where an excess of hydrogen peroxide must be present in order to achieve an adequate bleaching effect.
  • the detergent additives of the invention may be possible, by using the detergent additives of the invention to bleach stains on fabric, to reduce the amount of hydrogen peroxide or precursors thereof in the additive or in detergent compositions containing the additive and yet provide a satisfactory bleaching effect.
  • the environmental load i.e. the amount of unspent bleaching agent released into the environment
  • the overall performance of detergent compositions in which such bleaching agents are included may be improved.
  • peroxidases with specificity for a particular class of colourant e.g. betalaines, carotenoids, flavonoids, etc.
  • a peroxidase of low specificity i.e. acting on several natural colourants
  • a peroxidase of low specificity i.e. acting on several natural colourants
  • peroxidases may be efficient for bleaching usually dry stains in fabrics in which the coloured substance(s) may have become absorbed or partly absorbed into the fibers of the fabric so that they are less accessible to enzymatic action and/or in which the coloured substances may have been oxidized by atmospheric oxygen so that, in effect, a different coloured substance than that present in a solution of the dye may have been produced.
  • Ben Aziz et al. and Wasserman et al. present the bleaching action of peroxidase on carotene and betalain, respectively, as a problem when using these pigments as food colourants, which problem must be counteracted by including an antioxidant in the foodstuff in question. Thus, they do not consider the peroxidase- mediated bleaching of these pigments to have any practical utility in itself.
  • Peroxidases which may be employed for the present purpose as detergent additives may be isolated from and are producible by plants (e.g. horseradish peroxidase) or microorganisms such as basidiomycetes, fungi, actinomycetes, or bacteria.
  • Some preferred microorganisms include strains of Fusarium, in particular Fusarium oxysporum, strains of Streptomyces. in particular Streptomyces thermoviolaceus or Streptomyces viridosporus. strains of Pseudomonas. preferably Pseudomonas putida or Pseudomonas fluorescens. strains of Coprinus.
  • strains are Coprinus cinereus f. microsporus IFO 8371, Coprinus cinereus IFO 30114, Pseudomonas fluorescens NRRL B-ll, Streptoverticillium verticillium ssp. verticillium IFO 13864, Streptomyces thermoviolaceus CBS 278.66, Streptomyces viridosporus.
  • Particularly preferred peroxidases are those which are active at the typical pH of washing liquors, i.e. at a pH of 6.5 - 10.5, preferably 6.5 - 9.5, and most preferably 7.5 - 9.5. More specifically, the peroxidases of interest for the present purpose are those which exhibit at least 25% of their optimal activity (i.e. their activity at the pH optimum) in these pH ranges, e.g. as determined by the ABTS assay described in Example 1 below. Such peroxidases may be isolated by screening for peroxidase production by alkalophilic microorganisms, e.g. by the ABTS assay described in Example 1 below.
  • preferred peroxidases are those which exhibit a good thermostability, in particular those retaining at least 25% of their initial activity after 20 minutes at 40 * C, as well as a good stability towards commonly used detergent components such as non-ionic, cationic, or anionic surfactants, detergent builders, phosphate etc., in particular those retaining at least 25% of their initial activity after exposure to such detergent ingredients for 20 minutes.
  • ligninases Another group of useful peroxidases is constituted by the ligninases: these enzymes which exert a strong peroxidase activity are instrumental in the degradation of lignin (e.g. in wood) and are produced by a variety of wood rot fungi. They have previously been suggested for the bleaching of paper pulp (cf. for instance US 4,690,895).
  • Further useful peroxidases are haloperoxidases, such as chloro- and bromoperoxidases, as they are able to oxidize halide ions to hypohalites which are powerful bleaching agents, apart from being able to oxidize organic compounds.
  • 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 DNA fragment encoding the peroxidase may, for instance, be isolated by establishing a cDNA or genomic library of a peroxidase-producing microorganism, such as one of the organisms mentioned above, and screening for positive clones by conventional procedures such as by hybridization to oligonucleotide probes synthesized on the basis of the full or partial amino acid sequence of the peroxidase, or by selecting for clones expressing the appropriate enzyme activity, or by selecting for clones producing a protein which is reactive with an antibody against a native peroxidase.
  • the DNA sequence may be inserted into a suitable replicable expression vector comprising appropriate promotor, operator and terminator sequences permitting the peroxidase to be expressed in a particular host organism, as well as an origin of replication enabling the vector to replicate in the host organism in question.
  • the resulting expression vector may then be transformed into a suitable host cell, such as a fungal cell, preferred examples of which are a species of Aspergillus. most preferably Aspergillus oryzae or Aspergillus niger.
  • Fungal cells may be transformed by a process involving protoplast formation and transformation of the protoplasts followed by regeneration of the cell wall in a manner known per se.
  • Aspergillus as a host microorga ⁇ nism is described in EP 238,023 (of Novo Industri A/S), the contents of which are hereby incorporated by reference.
  • the host organisms may be a bacterium, in particular strains of Streptomyces and Bacillus, or E. coli.
  • the transformation of bacterial cells may be performed according to conventional methods, e.g. as described in T. Maniatis et al.. Molecular Cloning; A Laboratory Manual, Cold Spring Harbor, 1982.
  • the medium used to cultivate the transformed host cells may be any conventional medium suitable for growing the host cells in question.
  • the expressed peroxidase may conveniently be secreted into the culture medium and may be recovered thereform by well-known procedures including separating the cells from the medium by centrifugation or filtration, precipitating proteinaceous components of the medium by means of a salt such as ammonium sulphate, followed by chromatographic procedures such as ion exchange chromatography, affinity chromatography, or the like.
  • the detergent additive according to the invention may additionally comprise a enzymatic system (i.e. an enzyme and a substrate therefor) which is capable of generating hydrogen peroxide.
  • One such category of hydrogen peroxide generating systems comprises oxidases which are able to convert molecular oxygen and an organic or inorganic substrate into hydrogen peroxide and the oxidized substrate, respectively.
  • oxidases which are able to convert molecular oxygen and an organic or inorganic substrate into hydrogen peroxide and the oxidized substrate, respectively.
  • these enzymes are of limited or no use for bleaching stained fabric as they produce too small quantities of hydrogen peroxide, but they may be employed to great advantage in detergent additives of the invention as the presence of peroxidase ensures an efficient utilization of the hydrogen peroxide produced, as indicated above.
  • Preferred oxidases are those which act on cheap and readily available substrates which may conveniently be included into detergent compositions.
  • An example of such a substrate is glucose which may be utilized for hydrogen peroxide production by means of glucose oxidase.
  • Other suitable oxidases are urate oxidase, galactose oxidase, alcohol oxidases, amine oxidases, amino acid oxidase and cholesterol oxidase.
  • the detergent additive of the invention may suitably be in the form of a non-dusting granulate, a liquid, in particular a stabilized liquid, or a protected enzyme.
  • Non-dusting granulates may be produced, e.g., as disclosed in US 4,106,991 and 4,661,452 (both to Novo Industri A/S) and may optionally be coated by methods known in the art.
  • Liquid enzyme preparations may, for instance, be stabilized by adding a polyol such as propylene glycol, a sugar or sugar alcohol, lactic acid or boric acid according to established methods. Other enzyme stabilizers are well known in the art.
  • Protected enzymes may be prepared according to the method disclosed in EP 238,216.
  • the detergent additive may further include one or more other enzymes, such as protease, lipase or amylase, conventionally included in detergent additives.
  • enzymes such as protease, lipase or amylase, conventionally included in detergent additives.
  • the invention relates to a detergent composition
  • a detergent composition comprising an enzyme exhibiting peroxidase activity as well as hydrogen peroxide or a precursor thereof, preferably a perborate or percarbonate.
  • an enzyme exhibiting peroxidase activity as well as hydrogen peroxide or a precursor thereof, preferably a perborate or percarbonate.
  • These and other components essential and/or advantageous for obtaining a bleaching of stained fabric may be added to the detergent composition seperately or may be included in the form of a detergent additive as described above.
  • Detergent compositions of the invention additionally comprise surfactants which may be of the anionic, non- ionic, cationic, amphoteric, or zwitterionic type as well as mixtures of these surfactant classes.
  • anionic surfactants are linear alkyl benzene sulfonates (LAS) , alpha olefin sulfonates (AOS) , alcohol ethoxy sulfates (AES) and alkali metal salts of natural fatty acids.
  • Detergent compositions of the invention may contain other detergent ingredients known in the art as e.g. builders, anti-corrosion agents, sequestering agents, anti soil- redeposition agents, perfumes, enzyme stabilizers, etc.
  • the detergent composition of the invention may contain the peroxidase in an amount corresponding to 0.1-100 mg peroxidase per liter of washing liquors.
  • the detergent composition of the invention may be formulated in any convenient form, e.g. as 'a powder or liquid.
  • the enzyme may be stabilized in a liquid detergent by inclusion of enzyme stabilizers as indicated above.
  • Liquid detergents may further include stabilized hydrogen peroxide precursors.
  • the pH of a solution of the detergent composition of the invention will be 7-12 and in some instances 7.0-10.5.
  • Other detergent enzymes such as proteases, lipases or amylases may be included the detergent compositions of the invention, either separately or in a combined additive as described above.
  • the present invention relates to a process for bleaching fabric which comprises treating fabric with a detergent additive or detergent composition as described above.
  • the invention also relates to a bleaching process wherein fabric is treated with an enzyme exhibiting peroxidase activity in the presence of hydrogen peroxide or a precursor thereof, optionally in the presence of an oxidase and a substrate for the oxidase.
  • the process is particularly well suited for bleaching stains caused by natural coloured substances, e.g. polyphenols, found in, for instances, fruit juice, wine, tea, and the like.
  • the bleaching treatment may suitably be conducted in a soaking, washing or rinsing process.
  • the detergent additive or detergent composition may also be employed for the bleaching of textiles, e.g. during their manufacture.
  • Cotton swatches homogeneously soiled with unsweetened blackcurrant juice were subjected to a model washing treatment to evaluate the bleaching effect of the system horseradish peroxidase + hydrogen peroxide.
  • a dosage of 5 mg/1 horseradish peroxidase (Boehringer-Mannheim) was found to be advantageous.
  • ABTS 2,2'-azino-bis(3-ethylbenzthiazo- line-6-sulphonic acid) , supplied by Boehringer-Mannheim as the diammonium salt
  • Cotton swatches homogeneously soiled with unsweetened blackcurrant juice, red wine and tea were subjected to a model washing treatment to evaluate the bleaching effect of the horseradish peroxidase/H 2 02 system.
  • the experimental conditions were :
  • Bleaching agent H2 ⁇ 2 , dosed to 10 mM.
  • Enzyme Sigma P-8125 horseradish peroxidase, dosed to 2 mg/1.
  • Evaluation of bleaching effect determined as described in Example 1, except that tap water was used to rinse the swatches.
  • Cotton swatches homogeneously soiled with beetroot juice were subjected several model washing treatments to evaluate the bleaching effect of the system H2O2 + peroxidase derived from Coprinus macrorhizus + H2O2.
  • the experimental conditions were :
  • Washing liquor Potassium phosphate buffer 0.05 M (see further below) , with pH adjusted to 7.0. 17 Duration of wash : Varying, as specified below.
  • Enzyme 20 mg/1 peroxidase derived from Coprinus macrorhizus (Chemical Dynamics Corporation, New Jersy, U.S., prod. no. 70-9590-00) .
  • experiment (1) the wash was followed by soaking over ⁇ night.
  • experiment (2) and (3) the buffer solution was prepared with water with a hardness equivalent to 1.6 mM Ca 2+ , in (1) and (4) the buffer was made with demineral- ized water.

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  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Wood Science & Technology (AREA)
  • Organic Chemistry (AREA)
  • Inorganic Chemistry (AREA)
  • Detergent Compositions (AREA)
  • Enzymes And Modification Thereof (AREA)

Abstract

Un additif de détergent utilisé dans un procédé de blanchissage de tissu taché comprend une enzyme présentant une activité de peroxydase et facultativement du peroxyde d'hydrogène ou un précurseur de ce dernier, par exemple un perborate ou un percarbonate. L'additif de détergent peut également comprendre une enzyme capable de produire du peroxyde d'hydrogène, par exemple une oxydase, ainsi qu'un substrat pour celui-ci.
EP89905395A 1988-04-15 1989-04-14 Additif de detergent pour le blanchissage de tissu Revoked EP0424398B1 (fr)

Priority Applications (1)

Application Number Priority Date Filing Date Title
AT89905395T ATE73485T1 (de) 1988-04-15 1989-04-14 Waschmittelzusatzverbindung beim bleichen von gewebe.

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
DK2123/88 1988-04-15
DK212388A DK212388D0 (da) 1988-04-15 1988-04-15 Detergent additiv

Publications (2)

Publication Number Publication Date
EP0424398A1 true EP0424398A1 (fr) 1991-05-02
EP0424398B1 EP0424398B1 (fr) 1992-03-11

Family

ID=8110229

Family Applications (1)

Application Number Title Priority Date Filing Date
EP89905395A Revoked EP0424398B1 (fr) 1988-04-15 1989-04-14 Additif de detergent pour le blanchissage de tissu

Country Status (8)

Country Link
EP (1) EP0424398B1 (fr)
JP (1) JP2716233B2 (fr)
KR (1) KR960010589B1 (fr)
AU (1) AU617811B2 (fr)
DK (1) DK212388D0 (fr)
FI (1) FI95596C (fr)
NO (1) NO176404C (fr)
WO (1) WO1989009813A1 (fr)

Cited By (6)

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CN1035886C (zh) * 1991-11-06 1997-09-17 普罗格特-甘布尔公司 抑制染料转移的组合物
US6169065B1 (en) 1997-09-08 2001-01-02 Lever Brothers Company Division Of Conopco Company Method for the activity of an enzyme
US6225275B1 (en) 1997-06-10 2001-05-01 Lever Brothers Company, Division Of Conopco, Inc. Method for enhancing the activity of an enzyme
US6323014B1 (en) 1999-06-23 2001-11-27 Unilever Home & Personal Care Division Of Conopco, Inc. Method and composition for enhancing the activity of an enzyme
US6380146B1 (en) 1999-06-23 2002-04-30 Unilever Home & Personal Care Usa A Division Of Conopco, Inc. Bleaching detergent compositions
US6384007B1 (en) 1999-11-11 2002-05-07 Unilever Home & Personal Usa Division Of Conopco, Inc. Method and composition for enhancing the activity of an enzyme

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US5474576A (en) * 1992-01-31 1995-12-12 The Procter & Gamble Company Detergent compositions inhibiting dye transfer in washing
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EP0628624A1 (fr) 1993-06-09 1994-12-14 The Procter & Gamble Company Compositions détergentes contenant une protéase et des additifs pour empêcher le transfert de colorant
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EP0747469A1 (fr) 1995-06-08 1996-12-11 The Procter & Gamble Company Compositions de nettoyage contenant du chondroitinase
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US8114169B2 (en) 2006-08-25 2012-02-14 Advanced Enzyme Technologies Limited Compositions for biobleaching coupled with stone washing of indigo dyed denims and process thereof
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Also Published As

Publication number Publication date
NO904422D0 (no) 1990-10-12
FI905038A0 (fi) 1990-10-12
EP0424398B1 (fr) 1992-03-11
AU617811B2 (en) 1991-12-05
FI95596C (fi) 1996-02-26
NO904422L (no) 1990-10-12
JPH03505100A (ja) 1991-11-07
NO176404C (no) 1995-03-29
KR900700587A (ko) 1990-08-16
AU3551989A (en) 1989-11-03
DK212388D0 (da) 1988-04-15
KR960010589B1 (ko) 1996-08-06
JP2716233B2 (ja) 1998-02-18
NO176404B (no) 1994-12-19
FI95596B (fi) 1995-11-15
WO1989009813A1 (fr) 1989-10-19

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