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WO1992003529A1 - Composition detergente enzymatique et procede de stabilisation enzymatique - Google Patents

Composition detergente enzymatique et procede de stabilisation enzymatique Download PDF

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Publication number
WO1992003529A1
WO1992003529A1 PCT/DK1991/000243 DK9100243W WO9203529A1 WO 1992003529 A1 WO1992003529 A1 WO 1992003529A1 DK 9100243 W DK9100243 W DK 9100243W WO 9203529 A1 WO9203529 A1 WO 9203529A1
Authority
WO
WIPO (PCT)
Prior art keywords
protease
inhibitor
detergent
composition according
subtilisin
Prior art date
Application number
PCT/DK1991/000243
Other languages
English (en)
Inventor
Jan Møller MIKKELSEN
Lone Kierstein Hansen
Original Assignee
Novo Nordisk A/S
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
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Application filed by Novo Nordisk A/S filed Critical Novo Nordisk A/S
Priority to DE69101557T priority Critical patent/DE69101557T2/de
Priority to AT91915580T priority patent/ATE103632T1/de
Publication of WO1992003529A1 publication Critical patent/WO1992003529A1/fr

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
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • 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
    • C11D3/38663—Stabilised liquid enzyme compositions

Definitions

  • the present invention relates to a detergent composition comprising a protease and a second enzyme (which may be another protease or a non- proteolytic enzyme), to a method for stabilizing an enzyme in the presence of a protease and to an enzymatic detergent additive comprising a protease and a second enzyme.
  • a second enzyme which may be another protease or a non- proteolytic enzyme
  • proteases are widely used as ingredients in commercial detergents, including liquids. Two different proteases may be used together (US 4,511 ,490, WO 88/03946). Other enzyme types (i.e. non-proteolytic) may also be used in detergents, e.g. amylase, cellulase, lipase or peroxidase.
  • the stability problem is aggravated as the protease is liable to digest and deactivate the other enzyme (i.e. the other protease or the non-proteolytic enzyme).
  • WO 89/04361 discloses a detergent containing a protease and a lipase, where improved lipase stability is achieved by selecting a specified groups of lipases and a specified group of proteases.
  • the stability of an enzyme in a detergent containing a protease can be improved by incorporation of a reversible protease inhibitor of the peptide or protein type.
  • the invention provides a detergent composition comprising a protease and one or more other enzymes, characterized by further comprising a reversible protease inhibitor of the peptide or protein type.
  • the invention provides a method for stabilizing an enzyme in the presence of a protease, characterized by incorporating a protease inhibitor.
  • a further aspect of the invention provides an enzymatic detergent additive comprising a protease and one or more other enzymes in the form of a stabilized liquid or a non-dusting granulate, characterized by further comprising a reversible protease inhibitor of the peptide- or protein-type.
  • JP-A 62-269689 discloses improvement of the stability of a protease in a liquid detergent by incorporation of a protease inhibitor, but no other enzymes were present.
  • the protease used in the invention is preferably of microbial origin. It may be a serine protease, preferably an alkaline microbial protease or a trypsin- like protease.
  • alkaline proteases are subtilisins, especially those derived from Bacillus, e.g. subtilisin Novo, subtilisi ⁇ Carlsberg, subtilisin 309, subtilisin 147 and subtilisin 168 (both described in WO 89/06279) and mutant subtilins such as those described in WO 89/06279.
  • Examples of commercial Bacillus subtilisins are Alcalase ® , Savinase ® and Esperase ® , products of Novo Nordisk A/S.
  • trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO 89/06270.
  • the amount of protease in the detergent will typically be 0.2-40 ⁇ M, especially 1-20 ⁇ M (generally 5-1000 mg/l, especially 20-500 mg/l).
  • Other enzymes generally be 0.2-40 ⁇ M, especially 1-20 ⁇ M (generally 5-1000 mg/l, especially 20-500 mg/l).
  • the other enzyme(s) used in the invention may be another protease
  • non-proteolytic enzyme e.g. an amylase, a cellulase, a lipase or an oxidoreductase, such as a peroxidase.
  • the non- proteolytic enzyme is preferably of microbial origin, e.g. derived from a strain of
  • the amount of the other enzyme(s) in the detergent will typically be 0.2-40 ⁇ M, especially 1-20 ⁇ M (generally 5-1000 mg/l, especially 20-500 mg/l).
  • the inhibitor used in the invention may be any inhibitor of the peptide or protein type that reversibly inhibits the protease in question, e.g. those described in Lakowski, Jr. & Kato, Ann.Rev.Biochem. (1980) 49:593-626 and S. Murao et al., in Protein Protease Inhibitor - The Case of Streptomyces subtilisin Inhibitor (1985) at pp. 1-14. Examples are trypsin inhibitors of Family IV (described in the cited references) and subtilisin inhibitors of family III, VI and VII.
  • Streptomyces subtilisin inhibitor SSI
  • plasminostreptin from Streptomyces antifibrinolyticus barley subtilisin inhibitor Cl- 1 (e.g. described in Williamson et al., Plant Mol. Biol. 10, 1988, pp. 521 -535) and CI-2 (e.g. described in Williamson et al., Eur. J. Biochem. 165. 1987
  • SSI Streptomyces subtilisin inhibitor
  • Cl- 1 e.g. described in Williamson et al., Plant Mol. Biol. 10, 1988, pp. 521 -535) and CI-2 (e.g. described in Williamson
  • eglin C from leech e.g. described in Seem ⁇ ller et al., Hoppe-Seylers Z. Phvsiol. Chem. 361 , 1980, pp. 1841-1846
  • Vicia faba subtilisin inhibitor e.g. described in Svendsen et al., Carlsberq Res. Commun. 49, 1984, pp. 493-502
  • leupeptin inhibitor e.g. described in S. Kondo et al., J. Antibiot. 22, 1969, pp. 558-568.
  • the inhibitor may be a modified subtilisin inhibitor of Family VI with a weaker binding affinity for the protease.
  • a modified inhibitor may have one -or more of the following amino acid substitutions at the indicated positions (numbered from the reactive site of the inhibitor, P1 , P2 etc. are in the direction of the N-terminal and P'1 , P'2 etc. are in the direction of the C-terminal of the inhibitor molecule):
  • P3 Tyr, Glu, Ala, Arg, Pro, Ser, Lys or Trp
  • P2 Ser, Lys, Arg, Pro, Glu, Val, Tyr, Trp or Ala
  • P1 Arg, Tyr, Pro, Trp, Glu, Val, Ser, Lys or Ala
  • P'1 Gin, Ser, Thr, He or Pro
  • P'3 Glu, Gin, Asn, Val, Phe or Tyr.
  • a preferred modified inhibitor is CI-2 substituted with Arg, Pro or Glu at position P3, Lys or Arg at P2, and/or Glu, Arg or Pro at P1.
  • Modified inhibitors may be produced by known recombinant DNA techniques. Briefly, a DNA sequence (cDNA or a synthetic gene) encoding a known inhibitor is subjected to mutagenesis in order to replace the codon(s) for the amino acid(s) to be substituted with a new codon (codons) for the desired amino acid substitution (s). This may preferably be carried out by oligonucleotide- directed site-specific mutagenesis in bacteriophage M13 vectors (e.g. M.J. Zoller and M. Smith, Meth. Enzymol. 100 (1983) 468-500), in double-stranded DNA vectors (e.g. Y.
  • M13 vectors e.g. M.J. Zoller and M. Smith, Meth. Enzymol. 100 (1983) 468-500
  • double-stranded DNA vectors e.g. Y.
  • the mutant gene is subsequently expressed in a suitable host strain.
  • suitable hosts are bacteria (e.g. strains of Escherichia coli or Bacillus), fungi (e.g. strains of Saccharomyces cerevisiae or filamentous fungi like Aspergillus), plants such as tomato or potato or established human or animal cell lines.
  • the mutant gene has to be inserted in an expression plasmid with promoter and terminator DNA elements for the formation of translatable mutant inhibitor mRNA in vivo.
  • the plasmid is introduced into the host by genetic transformation. The choice of expression plasmid is dependent on the type of host strain used.
  • the expression of the mutant inhibitor may be done intracellularly or extracellularly.
  • the DNA sequence coding for the mutant inhibitor is fused in frame to a DNA sequence encoding a suitable peptide signalling secretion.
  • the secretion signal should preferably be cleaved off in vivo, resulting in secretion of the mature mutant inhibitor into the growth medium.
  • the amount of inhibitor preferably corresponds to a molar ratio of inhibitor reactive site to protease active site above 0.6, more preferably above 0.8 and most preferably above 1.
  • the ratio is generally below 10, usually below 5.
  • the type and amount of inhibitor is preferably chosen so as to provide at least 60% (e.g. at least 80%) inhibition in the detergent as such and below 10% inhibition when the detergent is diluted with water for use in washing, typically at a concentration of 0.3-10 g/l.
  • the detergent of the invention may be in any convenient form, e.g. powder, granules or liquid.
  • the invention is particularly applicable to the formulation of liquid detergents where enzyme stability problems are pronounced.
  • a liquid detergent may be aqueous, typically containing 20-70% water and 0-20% organic solvent (hereinafter, percentages by weight).
  • the detergent comprises surfactant which may be anionic, non- ionic, cationic, amphoteric or a mixture of these types.
  • the detergent will usually contain 5-30% anionic surfactant such as linear alkyl benzene sulphonate (l-AS), alpha-olefin sulphonate (AOS), alcohol ethoxy sulphate (AES) or soap. It may also contain 3-20% anionic surfactant such as nonyl phenol ethoxylate or alcohol ethoxylate.
  • the pH (measured in aqueous detergent solution) will usually be neutral or alkaline, e.g. 7-10.
  • the detergent may contain 1-40% of a detergent builder such as zeolite, phosphate, phosphonate, citrate, NTA, EDTA or DTPA, or it may be unbuilt (i.e. essentially free of a detergent builder). It may also contain other conventional detergent ingredients, e.g. fabric conditioners, foam boosters, bactericides, optical brighteners and perfumes.
  • a detergent builder such as zeolite, phosphate, phosphonate, citrate, NTA, EDTA or DTPA
  • a detergent builder such as zeolite, phosphate, phosphonate, citrate, NTA, EDTA or DTPA
  • other conventional detergent ingredients e.g. fabric conditioners, foam boosters, bactericides, optical brighteners and perfumes.
  • the protease, other enzyme(s) and inhibitor may be included in the detergent of the invention by separate addition or by adding the combined additive provided by the invention.
  • the additive will usually contain 0.2-8 mM protease (0.5-20%) and 0.2-8 mM (0.5-20%) of the second enzyme, and have an inhibitor/protease ratio as described above.
  • the detergent additive may be in liquid form for incorporation in a liquid detergent.
  • a liquid additive may contain 20-90% propylene glycol; 0.5-3% (as Ca) of a soluble calcium salt; 0-10% glycerol; minor amounts of short-chain fatty acids and carbohydrate; and water up to 100%.
  • Fig. 1 is a graph showing the residual activity (in %) after 13 days at room temperature of lipase in a detergent composition containing lipase and protease alone compared to a composition containing lipase, protease and Streptomyces subtilisin inhibitor;
  • Fig. 2 is a graph showing the residual activity (in %) after 13 days at room temperature of lipase in a detergent composition containing lipase and protease alone compared to a composition containing lipase, protease and barley subtilisin inhibitor CI-2;
  • Fig. 3 is a graph showing the residual activity (in %) after 43 hours at room temperature of lipase in the presence of protease with or without added leupeptin inhibitor; and Fig. 4 is a graph showing the residual activity (in %) after 10 days at room temperature of cellulase in the presence of protease with or without added Streptomyces subtilisin inhibitor; and
  • Fig. 5 is a graph showing the residual activity (in %) after 10 days at room temperature of cellulase in the presence of protease with or without added CI-2 inhibitor.
  • a concentrated liquid detergent was formulated as follows (% by weight of active substance):
  • a detergent according to the invention was prepared by addition of Streptomyces subtilisin inhibitor (SSI, 0.05 mg/ml, 4.5 ⁇ M) to a detergent of the composition: 52 (v/v) % of the above concentrated detergent in water containing 10 mg/ml (300 ⁇ M) Humicola lipase (LipolaseTM) and 0 1 mg mj (3 6 ⁇ M)
  • Another detergent was prepared by addition of inhibitor CI-2 (0.03 mg/ml, 3.3 ⁇ M) to a detergent of the composition 55 (v/v) % concentrated detergent in water containing 10 mg/ml (300 ⁇ M) Humicola lipase (LipolaseTM) and 0.1 mg/ml (3.6 ⁇ M) Savinase ® .
  • the lipase activity was measured at various times and expressed in % of initial lipase activity.
  • the protection of lipase from proteolytic degradation in the presence of a protease inhibitor was determined by adding 0.67 g/l leupeptin inhibitor to a mixture of 0.5 g/l Pseudomonas cepacia lipase and 2 g/l Fusarium protease in 50 mM Tris-HCI, pH 8.0, at 20°C and measuring the residual lipase activity (in %) after 43 hours. From the results shown in Fig. 3 it appears that there is very little degradation of the lipase in the presence of the leupeptin inhibitor, whereas the lipase is almost completely degraded when no inhibitor is added. The protease activity may be restored by dilution.
  • a concentrated liquid detergent was formulated as follows (% by weight of active substance):
  • a detergent according to the invention was prepared by addition of Streptomyces subtilisin inhibitor (SSI, 0.09 mg/ml, 7.7 ⁇ M) to a detergent (90% (w/w) of the above concentrated detergent in water) containing 0.12 mg/ml (3.3 ⁇ M) Humicola cellulase and 0.18 mg/ml ( ⁇ .7 ⁇ M) Savinase ® .
  • Another detergent was prepared by addition of inhibitor CI-2 (0.07 mg/ml, 7.8 ⁇ M) to a detergent (90% (w/w) of the above concentrated detergent in water) containing 0.12 mg/ml (3.3 ⁇ M) Humicola cellulase and 0.18 mg/ml (6.7 ⁇ M) Savinase ® .

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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)
  • Detergent Compositions (AREA)
  • Enzymes And Modification Thereof (AREA)

Abstract

L'invention se rapporte à une composition détergente comprenant une protéase et une ou plusieurs autres enzymes, et comprenant également un inhibiteur de protéase réversible du type peptidique ou protéique.
PCT/DK1991/000243 1990-08-24 1991-08-23 Composition detergente enzymatique et procede de stabilisation enzymatique WO1992003529A1 (fr)

Priority Applications (2)

Application Number Priority Date Filing Date Title
DE69101557T DE69101557T2 (de) 1990-08-24 1991-08-23 Enzymatische waschmittelzusammensetzung und verfahren zum stabilisieren der enzyme.
AT91915580T ATE103632T1 (de) 1990-08-24 1991-08-23 Enzymatische waschmittelzusammensetzung und verfahren zum stabilisieren der enzyme.

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
DK2042/90 1990-08-24
DK204290A DK204290D0 (da) 1990-08-24 1990-08-24 Enzymatisk detergentkomposition og fremgangsmaade til enzymstabilisering

Publications (1)

Publication Number Publication Date
WO1992003529A1 true WO1992003529A1 (fr) 1992-03-05

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Country Status (7)

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EP (1) EP0544777B1 (fr)
JP (1) JPH06500142A (fr)
AT (1) ATE103632T1 (fr)
DE (1) DE69101557T2 (fr)
DK (2) DK204290D0 (fr)
ES (1) ES2062812T3 (fr)
WO (1) WO1992003529A1 (fr)

Cited By (56)

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WO1993000418A1 (fr) * 1991-06-27 1993-01-07 Genencor International, Inc. Detergent liquide a enzymes stabilisees
WO1993020175A1 (fr) * 1992-03-31 1993-10-14 Novo Nordisk A/S Detergent contenant une protease et un inhibiteur de protease, et nouveaux inhibiteurs associes
EP0583534A1 (fr) * 1992-08-14 1994-02-23 The Procter & Gamble Company Compositions détergentes liquides contenant un aldehyde peptidique
EP0583535A1 (fr) * 1992-08-14 1994-02-23 The Procter & Gamble Company Compositions détergentes liquides contenant un cétopeptide trifluorométhylé
EP0549675B1 (fr) * 1990-09-18 1995-04-05 Novo Nordisk A/S Detergent contenant une protease ainsi qu'un inhibiteur et nouveaux inhibiteurs destines a etre utilises dans ce detergent
US5468414A (en) * 1991-04-30 1995-11-21 Panandiker; Rajan K. Built liquid detergents with boric-polyol complex to inhibit proteolytic enzyme
US5472628A (en) * 1991-04-30 1995-12-05 The Procter & Gamble Company Liquid detergents with an aryl acid for inhibition of proteolytic enzyme
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US5576283A (en) * 1992-08-14 1996-11-19 The Procter & Gamble Company Liquid detergents containing a peptide aldehyde
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WO1998013458A1 (fr) * 1996-09-24 1998-04-02 The Procter & Gamble Company Detergents liquides contenant un enzyme proteolytique et des inhibiteurs de protease
WO1998013461A1 (fr) * 1996-09-24 1998-04-02 The Procter & Gamble Company Compositions de detergents liquides pour lessive contenant une enzyme proteolytique et des inhibiteurs de protease
WO1998013460A1 (fr) * 1996-09-24 1998-04-02 The Procter & Gamble Company Detergents liquides contenant un enzyme proteolytique et des inhibiteurs de protease
WO1998013459A1 (fr) * 1996-09-24 1998-04-02 The Procter & Gamble Company Detergents liquides contenant un enzyme proteolytique, un aldehyde peptidique et des ions calcium
WO1998013462A1 (fr) * 1996-09-24 1998-04-02 The Procter & Gamble Company Detergents liquides contenant un enzyme proteolytique, un aldehyde peptidique et une source d'acide borique
AU695776B2 (en) * 1995-07-12 1998-08-20 Novozymes A/S Cleaning-in-place with a solution containing a protease and a lipase
US6071356A (en) * 1995-07-12 2000-06-06 Novo Nordisk Als Cleaning-in-place with a solution containing a protease and a lipase
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WO2001018165A1 (fr) * 1999-09-09 2001-03-15 The Procter & Gamble Company Composition detergente contenant une protease
WO2003041680A1 (fr) * 2001-11-13 2003-05-22 The Procter & Gamble Company Compositions topiques contenant des enzymes stabilisees a l'aide d'inhibiteurs
US6579698B1 (en) 1996-09-24 2003-06-17 The Procter & Gamble Company Stabilized proteinaceous protease inhibitors and variants thereof
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EP1700907A1 (fr) 2005-03-11 2006-09-13 Unilever N.V. Composition liquide de blanchiment
US7153820B2 (en) 2001-08-13 2006-12-26 Ecolab Inc. Solid detergent composition and method for solidifying a detergent composition
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US20100125047A1 (en) * 2008-11-14 2010-05-20 Neil Joseph Lant Composition comprising polymer and enzyme
WO2011003968A1 (fr) 2009-07-08 2011-01-13 Ab Enzymes Oy Protéase fongique et son utilisation
WO2011036153A1 (fr) * 2009-09-25 2011-03-31 Novozymes A/S Composition détergente
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US8603795B2 (en) 2009-04-30 2013-12-10 Ab Enzymes Oy Fungal protease and use thereof
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WO2015032447A1 (fr) 2013-09-09 2015-03-12 Ecolab Usa Inc. Détachage synergique grâce à une nouvelle combinaison de chélateurs
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EP3470516A1 (fr) 2012-09-10 2019-04-17 Ecolab USA Inc. Compositions pour laver la vaisselle à la main liquides et stables contenant des enzymes
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EP3666870A1 (fr) 2013-10-24 2020-06-17 Ecolab USA Inc. Compositions et méthodes d'élimination des salissures des surfaces
WO2021022045A1 (fr) 2019-07-31 2021-02-04 Ecolab Usa Inc. Compositions de détartrage sans équipement de protection individuelle
WO2024167695A1 (fr) 2023-02-08 2024-08-15 Danisco Us Inc. Compositions et procédés de production de globines hétérologues dans des cellules fongiques filamenteuses
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ES2062812T3 (es) 1994-12-16
ATE103632T1 (de) 1994-04-15
DK0544777T3 (da) 1994-08-22
JPH06500142A (ja) 1994-01-06
DE69101557D1 (de) 1994-05-05
EP0544777A1 (fr) 1993-06-09
EP0544777B1 (fr) 1994-03-30
DK204290D0 (da) 1990-08-24
DE69101557T2 (de) 1994-07-14

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