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EP2727989A2 - Procédé d'amélioration de la puissance de nettoyage d'un produit de lavage et de nettoyage - Google Patents

Procédé d'amélioration de la puissance de nettoyage d'un produit de lavage et de nettoyage Download PDF

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Publication number
EP2727989A2
EP2727989A2 EP14152970.1A EP14152970A EP2727989A2 EP 2727989 A2 EP2727989 A2 EP 2727989A2 EP 14152970 A EP14152970 A EP 14152970A EP 2727989 A2 EP2727989 A2 EP 2727989A2
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EP
European Patent Office
Prior art keywords
washing
daltons
cleaning
component
culture supernatant
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
EP14152970.1A
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German (de)
English (en)
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EP2727989B2 (fr
EP2727989A3 (fr
EP2727989B1 (fr
Inventor
Timothy O'connell
Petra Siegert
Stefan Evers
Johannes Bongaerts
Thomas Weber
Karl-Heinz Maurer
Cornelius Bessler
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Henkel AG and Co KGaA
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Henkel AG and Co KGaA
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Application filed by Henkel AG and Co KGaA filed Critical Henkel AG and Co KGaA
Priority to PL14152970.1T priority Critical patent/PL2727989T5/pl
Publication of EP2727989A2 publication Critical patent/EP2727989A2/fr
Publication of EP2727989A3 publication Critical patent/EP2727989A3/fr
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    • 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
    • C11D3/3869—Enzyme enhancers or mediators
    • 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
    • C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/02—Anionic compounds
    • C11D1/32—Protein hydrolysates; Fatty acid condensates thereof
    • 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
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/2003—Alcohols; Phenols
    • 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
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/2003—Alcohols; Phenols
    • C11D3/2006—Monohydric alcohols
    • C11D3/201—Monohydric alcohols linear
    • 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
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/2003—Alcohols; Phenols
    • C11D3/2041—Dihydric alcohols
    • 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
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/2003—Alcohols; Phenols
    • C11D3/2041—Dihydric alcohols
    • C11D3/2044—Dihydric alcohols linear
    • 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
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/2003—Alcohols; Phenols
    • C11D3/2065—Polyhydric alcohols
    • 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
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/2072—Aldehydes-ketones
    • C—CHEMISTRY; METALLURGY
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    • 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
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/2075—Carboxylic acids-salts thereof
    • C—CHEMISTRY; METALLURGY
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    • 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
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    • C11D3/2075—Carboxylic acids-salts thereof
    • C11D3/2079—Monocarboxylic acids-salts thereof
    • 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
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    • C11D3/2075—Carboxylic acids-salts thereof
    • C11D3/2082—Polycarboxylic acids-salts thereof
    • 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
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/2075—Carboxylic acids-salts thereof
    • C11D3/2086—Hydroxy carboxylic acids-salts thereof
    • 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
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/22—Carbohydrates or derivatives thereof
    • C11D3/221—Mono, di- or trisaccharides or derivatives thereof
    • 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
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/22—Carbohydrates or derivatives thereof
    • C11D3/222—Natural or synthetic polysaccharides, e.g. cellulose, starch, gum, alginic acid or cyclodextrin
    • 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
    • C11D3/33—Amino carboxylic acids
    • 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
    • C11D3/37—Polymers
    • C11D3/3703—Macromolecular compounds obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds
    • C11D3/3719—Polyamides or polyimides
    • 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
    • C11D3/37—Polymers
    • C11D3/3703—Macromolecular compounds obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds
    • C11D3/3723—Polyamines or polyalkyleneimines
    • 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
    • C11D3/37—Polymers
    • C11D3/3746—Macromolecular compounds obtained by reactions only involving carbon-to-carbon unsaturated bonds
    • C11D3/3753—Polyvinylalcohol; Ethers or esters thereof
    • 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
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    • C11D3/37—Polymers
    • C11D3/3746—Macromolecular compounds obtained by reactions only involving carbon-to-carbon unsaturated bonds
    • C11D3/3757—(Co)polymerised carboxylic acids, -anhydrides, -esters in solid and liquid compositions
    • 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
    • C11D3/37—Polymers
    • C11D3/3746—Macromolecular compounds obtained by reactions only involving carbon-to-carbon unsaturated bonds
    • C11D3/3769—(Co)polymerised monomers containing nitrogen, e.g. carbonamides, nitriles or amines
    • 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
    • C11D3/381—Microorganisms
    • 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
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    • 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
    • C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
    • 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
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    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
    • C—CHEMISTRY; METALLURGY
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    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
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    • 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

Definitions

  • the present application is directed to methods for improving the cleaning performance of a detergent or cleaning agent containing a hydrolytic enzyme.
  • enzymes in detergents and cleaners are well established in the art. They serve to extend the range of services of the funds concerned according to their specific activities. These include in particular hydrolytic enzymes such as proteases, amylases, lipases and cellulases. The first three hydrolyze proteins, starches and fats and thus contribute directly to soil removal. Cellulases are used in particular because of their tissue effect.
  • Another group of detergents and cleaning agents are oxidative enzymes, in particular oxidases, which, if appropriate, in combination with other components, preferably serve to bleach soiling or to generate the bleaching agents in situ.
  • enzymes which are subjected to constant optimization, further enzymes are constantly being made available for use in detergents and cleaners in order to be able to optimally address particular soiling, such as pectinases, ⁇ -glucanases, mannanases or other hemicellulases for hydrolysis, in particular more specific vegetable polymers.
  • proteases and in particular serine proteases, which include the subtilases. They cause the degradation of protein-containing stains on the items to be cleaned.
  • proteases of the subtilisin type (subtilases, subtilopeptidases, EC 3.4.21.62) are particularly important, which are attributed to the serine proteases due to the catalytically active amino acids. They act as nonspecific endopeptidases, that is, they hydrolyze any acid amide linkages that are internal to peptides or proteins. Their pH optimum is usually in the clearly alkaline range.
  • Subtilases Subtilisin-like Proteases "by R. Siezen, pages 75-95 in”
  • Subtilisin enzymes edited by R. Bott and C. Betzel, New York, 1996
  • Subtilases are naturally produced by microorganisms; Of these, in particular, the subtilisins formed and secreted by Bacillus species are to be mentioned as the most important group within the subtilases.
  • subtilisin-type proteases preferably used in detergents and cleaners are the subtilisins BPN 'and Carlsberg, the protease PB92, the subtilisins 147 and 309, the alkaline protease from Bacillus lentus, in particular from Bacillus lentus DSM 5483, subtilisin DY and the subtilases, but not the subtilisins in the narrower sense attributable enzymes thermitase, proteinase K and the proteases TW3 and TW7.
  • proteases are, for example, those under the trade names Durazym®, Relase®, Everlase®, Nafizym, Natalase®, Kannase® and Ovozyme® from Novozymes, which are available under the trade names, Purafect®, Purafect® OxP, Purafect® Prime and Properase ® from Genencor, sold under the trade name Protosol® by Advanced Biochemicals Ltd., Thane, India, under the trade name Wuxi® by Wuxi Snyder Bioproducts Ltd., China, under the trade names Proleather® and Protease P From Amano Pharmaceuticals Ltd., Nagoya, Japan, and that available under the name Proteinase K-16 from Kao Corp., Tokyo, Japan.
  • a disadvantage of these enzymes used in detergents and cleaning agents, in particular proteases, from the prior art is that they are especially at low temperatures, for example between 10 ° C and 40 ° C, in particular between 10 ° C and 30 ° C or even between 10 ° C and 25 ° C, have no satisfactory hydrolytic activity, in particular proteolytic activity, and therefore in particular in detergents and dishwashing detergents in this temperature range show no optimal cleaning performance.
  • cleaning performance is significantly improved if in these agents at least one hydrolytic enzyme (also referred to herein as component (a)) with one or more of the above i. to iv. cited substances or substance classes (also referred to herein as component (b)) is combined.
  • hydrolytic enzyme also referred to herein as component (a)
  • component (b) hydrolytic enzyme
  • cleaning performance is understood to mean the whitening performance of one or more soiling, in particular laundry soiling, which are sensitive to degradation by the particular hydrolytic enzyme, in particular for degradation by proteases.
  • both the washing or cleaning agent which comprises the hydrolytic enzyme, or the washing or cleaning liquor formed by this agent, and the hydrolytic enzyme itself have a respective cleaning performance.
  • the cleaning performance of the hydrolytic enzyme thus contributes to the cleaning performance of the agent or the washing or cleaning liquor formed by the agent.
  • component (b) The cleaning performance of detergents and cleaners based on the enzymatic activity used, in particular on the proteolytic activity, is improved by the addition of component (b).
  • component (a) and (b) With regard to the interaction of these components (a) and (b), a synergistic effect results, ie a better performance compared to the individual performances of the respective component in one-component systems (ie detergents or cleaners, each containing only the hydrolytic, in particular proteolytic enzyme, or the Component (b)) and also compared to the sum of the individual performances of components (a) and (b), ie the sum of two one-component systems, each having the component (a) and (b) alone.
  • hydrolytic enzyme (a), in particular protease, with a component (b) according to the invention represents a further possibility for improving the performance of detergents in terms of their cleaning performance, in particular their enzyme-based cleaning performance, especially with regard to their cleaning performance, which is caused by a contained protease to improve.
  • the washing or cleaning liquor is understood to be the use solution containing the washing or cleaning agent which acts on textiles or fabrics (wash liquor) or hard surfaces (cleaning liquor) and thus comes into contact with the soiling present on textiles or fabrics or hard surfaces .
  • the washing or cleaning liquor arises when the washing or cleaning process begins and the detergent or cleaning agent, for example, in a washing machine or other suitable container dissolved in water or diluted with water.
  • Preferred hydrolytic enzymes in the sense of component (a) include in particular proteases, amylases, in particular ⁇ -amylases, cellulases, lipases, hemicellulases, in particular pectinases, mannanases, ⁇ -glucanases, and mixtures thereof.
  • proteases in particular proteases, amylases, in particular ⁇ -amylases, cellulases, lipases, hemicellulases, in particular pectinases, mannanases, ⁇ -glucanases, and mixtures thereof.
  • proteases are particularly preferred.
  • These enzymes are basically of natural origin; Starting from the natural molecules, improved variants are available for use in detergents or cleaning agents, which are preferably used accordingly.
  • subtilisin type those of the subtilisin type are preferable.
  • subtilisins BPN 'and Carlsberg the protease PB92, the subtilisins 147 and 309, the alkaline protease from Bacillus lentus, subtilisin DY and the enzymes thermitase, proteinase K and the subtilases, but not the subtilisins in the narrower sense Proteases TW3 and TW7.
  • Subtilisin Carlsberg is available in a further developed form under the trade name Alcalase® from Novozymes A / S, Bagsv ⁇ rd, Denmark.
  • subtilisins 147 and 309 are sold under the trade names Esperase®, and Savinase® by the company Novozymes. From the protease from Bacillus lentus DSM 5483 derived under the name BLAP® protease variants derived.
  • proteases are, for example, those under the trade names Durazym®, Relase®, Everlase®, Nafizym®, Natalase®, Kannase® and Ovozyme® from Novozymes, available under the trade names, Purafect®, Purafect® OxP, Purafect® Prime, Excellase® and Properase® from Genencor, sold under the trade name Protosol® by Advanced Biochemicals Ltd., Thane, India sold under the trade name Wuxi® by Wuxi Snyder Bioproducts Ltd., China, under the trade names Proleather® and Protease P® by Amano Pharmaceuticals Ltd., Nagoya, Japan, and the product called Proteinase K-16 of enzymes available from Kao Corp., Tokyo, Japan. Particular preference is also given to using the proteases from Bacillus gibsonii and Bacillus pumilus, which are disclosed in the international patent applications WO2008 / 086916 and W02007 / 131656 ,
  • amylases which can be used according to the invention are the ⁇ -amylases from Bacillus licheniformis, B. amyloliquefaciens or B. stearothermophilus and their further developments improved for use in detergents or cleaners.
  • the B. licheniformis enzyme is available from Novozymes under the name Termamyl® and from Genencor under the name Purastar®ST. Further development products of this ⁇ -amylase are available from Novozymes under the trade name Duramyl® and Termamyl®ultra, from Genencor under the name Purastar®OxAm and from Daiwa Seiko Inc., Tokyo, Japan, as Keistase®. B.
  • amyloliquefaciens ⁇ -amylase is sold by Novozymes under the name BAN®, and variants derived from the B. stearothermophilus ⁇ -amylase under the names BSG® and Novamyl®, also from Novozymes. Furthermore, for this purpose, the ⁇ -amylase from Bacillus sp. A 7-7 (DSM 12368) and the cyclodextrin glucanotransferase (CGTase) from B. agaradherens (DSM 9948).
  • amylolytic enzymes belonging to the sequence space of ⁇ -amylases which can be used in the international patent application WO 03/002711 A2 is defined, and the ones in the application WO 03/054177 A2 to be discribed.
  • fusion products of said molecules can be used.
  • the further developments of the ⁇ -amylase from Aspergillus niger and A. oryzae available under the trade names Fungamyl® from Novozymes are suitable.
  • Further usable commercial products are, for example, the Amylase-LT® and Stainzyme® or Stainzyme ultra® or Stainzyme plus®, the latter also from Novozymes.
  • variants of these enzymes obtainable by point mutations can be used according to the invention.
  • lipases or cutinases which can be used according to the invention, which are contained in particular because of their triglyceride-cleaving activities, but also in order to generate in situ peracids from suitable precursors, are the lipases which are originally obtainable from Humicola lanuginosa (Thermomyces lanuginosus) or further developed, in particular those with the amino acid exchange D96L. They are, for example, from the company Novozymes under the Trade names Lipolase®, Lipolase® Ultra, LipoPrime®, Lipozyme® and Lipex®. Furthermore, for example, the cutinases can be used, which were originally isolated from Fusarium solani pisi and Humicola insolens.
  • Lipases which are likewise useful are sold by Amano under the names Lipase CE®, Lipase P®, Lipase B® or Lipase CES®, Lipase AKG®, Bacillis sp. Lipase®, Lipase AP®, Lipase M-AP® and Lipase AML®.
  • Lipases or cutinases can be used, the initial enzymes were originally isolated from Pseudomonas mendocina and Fusarium solanii.
  • Lipase® and Lipomax® are prepared by Meito Sangyo KK, Japan, under the name Lipase MY-30®, Lipase OF® and Lipase PL® to mention also the product Lumafast® from the company Genencor.
  • cellulases may be present as pure enzymes, as enzyme preparations or in the form of mixtures in which the individual components advantageously complement each other in terms of their various performance aspects.
  • performance aspects include, in particular, the contributions of the cellulase to the primary washing performance of the composition (cleaning performance), to the secondary washing performance of the composition (anti-redeposition effect or graying inhibition), to softening (fabric effect) or to the exercise of a "stone washed" effect.
  • cleaning performance the contributions of the cellulase to the primary washing performance of the composition
  • anti-redeposition effect or graying inhibition anti-redeposition effect or graying inhibition
  • fabric effect fabric effect
  • a useful fungal endoglucanase (EG) -rich cellulase preparation or its further developments is offered by Novozymes under the trade name Celluzyme®.
  • Endolase® and Carezyme® which are also available from Novozymes, are based on the 50 kD EG or the 43 kD EG from H. insolens DSM 1800. Further commercial products of this company are Cellusoft®, Renozyme® and Celluclean®. Also usable are, for example, the 20 kD-EG from Melanocarpus available from AB Enzymes, Finland, under the trade names Ecostone® and Biotouch®. Further commercial products of AB Enzymes are Econase® and Ecopulp®. Other suitable cellulases are from Bacillus sp. CBS 670.93 and CBS 669.93, those derived from Bacillus sp. CBS 670.93 from the company Genencor under the trade name Puradax® is available. Other commercial products of Genencor are "Genencor detergent cellulase L" and IndiAge®Neutra.
  • Suitable enzymes for this purpose are, for example, available under the names Gamanase® and Pektinex AR® from Novozymes, under the name Rohapec® B1L from AB Enzymes and under the name Pyrolase® from Diversa Corp., San Diego, CA, USA , The from Bacillus subtilis-derived ⁇ -glucanase is available under the name Cereflo® from Novozymes.
  • Hemicellulases which are particularly preferred according to the invention are mannanases which are sold, for example, under the trade names Mannaway® by the company Novozymes or Purabrite® by the company Genencor.
  • the enzymes may be formulated together with accompanying substances, for example from the fermentation or with stabilizers.
  • Agents used in a method according to the invention preferably contain enzymes in total amounts of 1 ⁇ 10 -8 to 5 percent by weight based on active protein.
  • the enzymes are from 0.001 to 5% by weight, more preferably from 0.01 to 5% by weight, even more preferably from 0.05 to 4% by weight and most preferably from 0.075 to 3.5% by weight. % contained in these agents, wherein each enzyme contained can be present in the stated amounts.
  • the protein concentration can be determined by known methods, for example the BCA method (bicinchoninic acid, 2,2'-biquinolyl-4,4'-dicarboxylic acid) or the biuret method ( Gornall AG, CS Bardawill and MM David, J. Biol. Chem., 177 (1948), pp. 751-766 ).
  • BCA method bicinchoninic acid, 2,2'-biquinolyl-4,4'-dicarboxylic acid
  • the biuret method Gornall AG, CS Bardawill and MM David, J. Biol. Chem., 177 (1948), pp. 751-766 .
  • the hydrolytic enzyme at least one of which is present in a detergent or cleaning agent used in the method according to the invention (namely as component (a)), supports the cleaning performance of the composition with respect to certain soils or stains.
  • a detergent or cleaning agent used in the method according to the invention namely as component (a)
  • an agent used in a method according to the invention contains a plurality of enzymes, wherein the enzymes may belong to the same or different enzyme classes.
  • the enzymes exhibit synergistic effects on their action against certain soils or stains, i. the enzymes contained in the middle composition mutually support each other in their cleaning performance.
  • the substances mentioned are preferably amino acids or polymers thereof or their salts or derivatives thereof, where both stereoisomers of the amino acids can be used, ie both D and L amino acids, also in combination, or corresponding polymers or derivatives.
  • a polyamino acid in this regard comprises at least two amino acid residues. Particularly preferred are glutamate, polyglutamate, lysine, glutamine, histidine, phenylalanine, tyrosine, alanine, leucine, isoleucine, methionine, proline, valine, gluramine, cysteine, trypptophan, threonine, serine, glycine, aspartate and asparagine.
  • Particularly preferred are poly-glutamic acid, including ⁇ -D-polyglutamic acid, L-polyglutamic acid and DL-polyglutamic acid, poly-aspartic acid, including ⁇ -D-polyaspartic acid and L-polyaspartic acid, poly-glutamine, including ⁇ -D-polyglutamine, L Polyglutamine and DL-polyglutamine, as well as poly-asparagine, including ⁇ -D-polyasparagine and L-polyasparagine.
  • An example of a particularly preferred polyaspartic acid is the compound available under the trade name Baypure DS 100 solid G (Lanxess company).
  • biosurfactants In the under ii. specified substances are biosurfactants. These are understood in the context of the invention substances that are formed by microorganisms and often also deposited. Like traditional surfactants, biosurfactants are surface-active substances that reduce the surface tension of liquids and thereby promote the mixing of aqueous (hydrophilic) and water-repellent (hydrophobic) phases. Preferred biosurfactants according to the invention belong, in particular, to the substance group of the lipids or lipid derivatives, in particular lipopeptides. They are therefore bioactive, peptidic substances that are formed by microorganisms.
  • peptide chains preferably consist of two to forty amino acids and may be linear, cyclic or branched.
  • ribosomally synthesized peptide chains they have as monomeric building blocks not only proteinogenic L-amino acids, but also D-amino acids as well as alpha-hydroxy and / or carboxylic acids of all kinds.
  • the amino acids are L- ⁇ - or D- ⁇ Amino acids, but also ⁇ -, ⁇ - or ⁇ -amino acids can be present, both in the D and in the L configuration.
  • the peptide chains may also have further chemical modifications, in particular they may be glycosylated, hydrolyzed, N-methylated or N-formylated. Frequently occurring structural elements are also thiazoline and / or oxazoline rings in different oxidation states.
  • Particularly preferred biosurfactants according to the invention are anionic lipopeptides and more preferably surfactin-like or lichenigen-like substances or surfactin or lichenin itself.
  • Surfactin-like or lichenigen-like substances are understood as meaning those which have either a similar chemical structure as surfactin or lichenyin and / or have a comparable with surfactin or Lichenysin effect.
  • Surfactin can be described in particular by the following formula: fatty acid-cyclo- [Glu-Leu-Leu-Val-Asp-Leu-Leu]. The structure of surfactin is also in FIG. 1 specified.
  • Lichenysine can be described in particular by the following formula: Fatty acid-cyclo [Gln-Leu-Leu-Val-Asp-Leu-Ile]. Since Lichenycin is often also referred to as Lichenisin, it is expressly pointed out at this point that according to the invention with the name Lichenysin both terms are included.
  • Biosurfactant type microorganism Trehalose lipids Arthrobacter paraffineus Corynebacterium sp. Mycobacterium sp. Rhodococcus erythropolis, Norcardia sp. rhamnolipids Pseudomonas aeruginosa Pseudomonas sp., Serratia rubidea sophorolipids Candida apicola, Candida bombicola Candida lipolytica Candida bogoriensis glycolipids Alcanivorax borkumensis Arthrobacter sp., Corynebacterium sp. R.
  • microbial metabolites In the under iii. specified substances are microbial metabolites. These are understood to mean substances which arise as intermediates or as degradation products of metabolic processes of the microorganism or as degradation products of nutrient medium through the microorganism. Microbial metabolites preferred according to the invention are present in the culture medium of a culture of the microorganism forming them. Therefore, they are particularly preferably secreted by the microorganism which forms them.
  • microbial metabolites which are particularly preferred according to the invention are diols, in particular 2,3-butanediol, acids, in particular acetate, lactate, pyruvate, 2-methylpropionate, 3-methylbutyrate, ⁇ -ketogluterate, propionate, butyrate, butyate, sugar, in particular levan, and as another particularly preferred microbial metabolite acetoin.
  • microbial metabolites may also be propanediol, glycol, glycerol, citrate, formate, ethanol, methanol or butanol.
  • component (b) is a preparation of a microbial culture supernatant containing at least 2.5% by weight of one of the substances i) to iii).
  • the culture medium of a microbial culture contains one of the substances i described above. and / or ii. and / or iii.
  • the culture supernatant obtained after the greatest possible separation of the cells or cell fragments containing at least one of these substances can therefore be used to enrich a washing or cleaning agent with the component (b).
  • the detergent or cleaning agent a preparation of such a microbial culture supernatant is added, the at least 2.5 wt .-% of one of the substances i.
  • the preparation contains at least 3, 3.5, 4, 4.5, 5, 5.5, 6, 6.5, 7, 7.5, 8, 8.5, 9, 9.5, 10, 12 , 14, 16, 18, 20, 22, 24, 26, 28, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85 and 90 wt .-% of one of the substances i. to iii.
  • the required amount is necessary for the provision of a sufficient minimum amount of the respective substance, without affecting the washing or cleaning agent in its washing performance due to the presence of too many other components of the microbial culture supernatant, in particular adversely affect.
  • component (b) is contained in the supernatant of a microbial culture. It may either have been actively produced or secreted by the microorganisms in the supernatant or have entered the supernatant due to cell lytic events in the culture. By customary routine measures, for example by fractionation, it is then possible to produce preparations of these culture supernatants which contain component (b) in sufficient quantity to allow use according to the invention.
  • a suitable preparation can therefore also be, for example, one or more fractions of a culture supernatant. If the culture supernatant already contains component (b) in sufficient quantity, the culture supernatant can also be added directly to the washing or cleaning agent. In this case, the preparation is the culture supernatant itself.
  • the natto or its non-bean content obtained with the aid of cultures of Bacillus subtilis natto can also be used according to the invention as component (b).
  • component (b) is added to the detergent or cleaning agent as a separate single substance, i. not as a component of another ingredient of the washing or cleaning agent.
  • component (b) is therefore free in the detergent, i. it is distributed in this and distributed as homogeneously as possible.
  • component (b) is preferably dissolved or dispersed in them.
  • the washing or cleaning agent particularly preferably does not contain component (b) as part of the dosage form of the hydrolytic enzyme (a), in particular not as a constituent of an enzyme granulate.
  • liquid or gel-shaped i. non-solid detergents or cleaners.
  • a preferred liquid detergent for such a washing system is composed as follows (all figures in weight percent): 0.3- 0.5% xanthan gum, 0.2-0.4% anti-foaming agent, 6-7% glycerol, 0.3-0.5% ethanol, 4-7% FAEOS (fatty alcohol ether sulfate), 24-28% nonionic surfactants, 1% boric acid, 1-2% sodium citrate (dihydrate), 2-4% soda, 14-16% coconut Fatty acids, 0.5% HEDP (1-hydroxyethane- (1,1-di-phosphonic acid)), 0-0.4% PVP (polyvinylpyrrolidone), 0-0.05% optical brightener, 0-0.001% dye, Rest demineralized water.
  • the dosage of the liquid detergent is between 4.5 and 5.5 grams per liter of wash liquor, for example, 4.9 grams per liter of wash liquor. Preference is given to washing in a pH range between pH 8 and pH 10.5, preferably between pH 8 and pH 9.
  • a preferred powdered detergent for such a washing system is composed as follows (all figures in weight percent): 10% linear alkylbenzenesulfonate (sodium salt), 1.5% C12-C18 fatty alcohol sulfate (sodium salt), 2.0% C12-C18 fatty alcohol with 7 EO, 20% sodium carbonate, 6.5% sodium bicarbonate, 4.0% amorphous sodium disilicate, 17 % Sodium carbonate peroxohydrate, 4.0% TAED, 3.0% polyacrylate, 1.0% carboxymethylcellulose, 1.0% phosphonate, 25% sodium sulfate, balance: optional foam inhibitors, optical brightener, fragrances and, if necessary, water ad 100%.
  • the dosage of the liquid detergent is between 6.0 and 7.0 grams per liter of wash liquor, for example, 6.7 grams per liter of wash liquor.
  • a liquid detergent is used.
  • the degree of whiteness i. the brightening of the stains, is preferably determined by optical measuring methods, preferably photometrically.
  • a suitable device for this purpose is for example the spectrometer Minolta CM508d.
  • the devices used for the measurement are previously calibrated with a white standard, preferably a supplied white standard.
  • the activity-like use ensures that, even if the ratio of active substance to total protein (the values of the specific activity) diverge, the respective enzymatic properties, for example the washing performance of certain soils, are compared. In general, a low specific activity can be compensated by adding a larger amount of protein.
  • Methods for the determination of the enzyme activities are familiar to the expert in the field of enzyme technology and are routinely used by him. For example, methods for the determination of protease activity are disclosed in U.S. Patent Nos. 4,936,866 and 4,347,866 Surfactants, Vol. 7 (1970), pp. 125-132 ,
  • the protease activity is preferably indicated in PE (protease units).
  • suitable protease activities are 5 or 10 PE (protease units) per ml wash liquor.
  • the enzymatic activity used is not equal to zero.
  • the synergistic cleaning performance is preferably based on a novel mechanism of action, ie there is no increase in enzyme activity per se in the classical sense, as would be measured in one of the following methods, based on proteases. Accordingly, a synergism according to the invention is also present in particular when an improved cleaning performance in the presence of components (a) and (b) is found compared to the sum of the cleaning powers of component (a) alone and component (b) alone, and the component ( b) in at least one of the subsequent test methods, preferably in both subsequent test methods, no effect with respect to increasing the hydrolytic activity of component (a), in particular with regard to increasing the hydrolytic activity of a protease, beyond the standard deviation due to measurement:
  • the protease activity is determined quantitatively by the release of the chromophore para-nitroaniline (pNA) from the substrate.
  • the substrate is: suc-L-Ala-L-Ala-L-Pro-L-Phe-p-Nitroanilide (substrate solution: 110 mM in DMSO).
  • the protease cleaves the substrate and releases pNA.
  • the release of pNA causes an increase in absorbance at 410 nm, the time course of which is a measure of enzymatic activity (see Del Mar et al., 1979).
  • the measurement is carried out at a temperature of 25 ° C, at pH 8.6 and a wavelength of 410 nm.
  • the measurement time is 5 min and the measurement interval 20s to 60s.
  • the use buffer (Tris-HCl pH 8.6) is used as a blank sample, 10 ⁇ L of the substrate solution are added to each cuvette, 1000 ⁇ L of buffer are added to each cuvette, 1-300 ⁇ l of buffer (s) are added Add component (b) (0.1, 0.2, 0.5 or 1% by weight in working buffer) to the cuvette and place 1-300 ⁇ l of the protease or blank sample in the cuvette The measurement is started by mixing the sample After mixing, the cuvettes are immediately transferred to the photometer and the measurement is started.An activation or stabilization of the protease can be quantified by means of the measurement data.
  • Tris-HCl pH 8.6 Tris-HCl pH 8.6
  • Protease activity is determined via the hydrolysis of casein and subsequent reaction of TCA-soluble peptides with Folin &Ciocalteu's phenol reagent. The absorbance of the resulting complex is measured at 660 nm and compared to a tyrosine standard. Reaction mixtures contain 3 ml of 0.8% (w / v) casein and 0.5 ml of a suitable enzyme dilution with or without the component (b) to be tested (concentration 0.1, 0.2, 0.5 or 1 wt. %), both in universal buffer 1 from Britton and Robinson, pH 9.5 (cf. J. Chem. Soc. 1931, p. 1451 ).
  • the mixtures are incubated for 30 minutes at 25 ° C, then the reaction is stopped by adding Stop Reagent (TCA). In control reactions, the stop reagent is added before enzyme addition with or without the substance to be tested. After 20 minutes at 25 ° C, the reaction mixtures are filtered through Whatman # 42 filter paper or centrifuged.
  • TCA Stop Reagent
  • the method is characterized in that component (b) is contained in a microbial culture supernatant, in particular in a bacterial or fungal culture supernatant, in particular in a culture supernatant of Bacillus sp. and in particular in a culture supernatant of Bacillus subtilis, Bacillus licheniformis, Bacillus pumilus, Bacillus aeolius or Bacillus subtilis natto. It has been found that culture supernatants of these microorganisms comprise at least one, preferably a plurality of substances of component (b) and thus can advantageously be used according to the invention.
  • microorganisms whose culture supernatants contain a component (b) according to the invention in this regard are selected from the group of the genera of Escherichia, Klebsiella, Bacillus, Staphylococcus, Corynebacterium, Arthrobacter, Streptomyces, Stenotrophomonas and Pseudomonas and in particular selected from the group of Escherichia coli, Klebsiella planticola, Bacillus licheniformis, Bacillus lentus, Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus alcalophilus, Bacillus globigu, Bacillus gibsonii, Bacillus pumilus, Staphylococcus carnosus, Corynebacterium glutamicum, Arthrobacter oxidans, Streptomyces lividans, Streptomyces coelicolor and Stenotrophomonas maltophilia.
  • a particularly advantageous synergistic cleaning performance also results from the fact that the substance used as component (b) is present in a certain concentration in the washing or cleaning liquor.
  • the process is accordingly characterized in that this component is present in the washing or cleaning liquor in a concentration of from 0.00025 to 0.6% by weight, in particular from 0.0003 to 0.5% by weight .-%.
  • This advantageous use concentration relates to the components i described above. and / or ii. and / or iii. and / or iv.
  • Detergents and cleaning agents which can be used in the process according to the invention include all conceivable types of detergents or cleaners, both concentrates and undiluted agents, for use on a commercial scale, in the washing machine or in hand washing or cleaning. These include detergents for textiles, carpets, or natural fibers, for which the term detergent is used. These include, for example, dishwashing detergents for dishwashers or manual dishwashing detergents or cleaners for hard surfaces such as metal, glass, porcelain, ceramics, tiles, stone, painted surfaces, plastics, wood or leather, for which the term detergent is used, ie in addition to manual and machine Dishwashing agents, for example, scouring agents, glass cleaners, toilet scenters, etc.
  • washing and cleaning agents in the invention also include washing aids which are added to the actual detergent in the manual or machine textile laundry to achieve a further effect.
  • laundry detergents and cleaners in the context of the invention also include textile pre-treatment and post-treatment agents, ie those agents with which the laundry item is brought into contact before the actual laundry, for example to dissolve stubborn soiling, and also agents which are in one of the actual Textile laundry downstream step to give the laundry further desirable properties such as comfortable grip, crease resistance or low static charge. Among the latter, i.a. calculated the fabric softener.
  • the detergents or cleaning agents which can be used in the process according to the invention can in addition to the active compounds used according to the invention - the components (a) and (b) - in principle all known and contain usual ingredients in such agents, wherein preferably at least one further ingredient is present in the agent.
  • the agents may in particular be builders, surface-active surfactants, bleaches based on organic and / or inorganic peroxygen compounds, bleach activators, water-miscible organic solvents, enzymes, sequestering agents, electrolytes, pH regulators and other auxiliaries such as optical brighteners, grayness inhibitors, foam regulators and colorants and fragrances, and combinations thereof.
  • a further combination of the active compounds according to the invention with one or more further ingredient (s) of the agents proves advantageous, since then a further improved cleaning performance can be achieved by further resulting synergisms.
  • the combination with a surfactant and / or a builder and / or a bleaching agent such a further synergism is achieved.
  • Such preferred further ingredients of the washing or cleaning agent are disclosed in the international publication WO 2009/021867 , whose disclosure is therefore expressly referred to or the disclosure thereof is therefore expressly incorporated into the present application.
  • the ingredients to be selected as well as the conditions under which the agent is used, such as temperature, pH, ionic strength, redox ratios or mechanical influences, should be optimized for the respective cleaning problem.
  • conventional temperatures for the use of detergents and cleaners in the ranges of 10 ° C over 40 ° C and 60 ° C up to 95 ° for mechanical means or in technical applications.
  • the ingredients of the respective agents are coordinated, in particular in such a way that synergies arise with regard to the cleaning performance.
  • synergies which are present in a temperature range between 10 ° C and 60 ° C, in particular in a temperature range of 10 ° C to 50 ° C, from 10 ° C to 40 ° C, from 10 ° C to 30 ° C. , from 15 ° C to 30 ° C from 10 ° C to 25 ° C, from 15 ° C to 25 ° C, and most preferably at 20 ° C.
  • an agent useful in the method of the invention further contains the hydrolytic enzyme in an amount of from 2 ⁇ g to 20 mg, preferably from 5 ⁇ g to 17.5 mg, more preferably from 20 ⁇ g to 15 mg and most preferably from 50 ⁇ g to 10 mg per g of the agent.
  • the hydrolytic enzyme contained in the agent in particular a protease, and / or other ingredients of the agent may be coated with a substance impermeable to the enzyme at room temperature or in the absence of water, which becomes permeable to the enzyme under conditions of use of the agent.
  • the washing or cleaning agent itself may be packaged in a container, preferably an air-permeable container, from which it is released shortly before use or during the washing process.
  • inventions of the present invention furthermore comprise all solid, powdery, liquid, gelatinous or paste-like administration forms of the agents which can be used in the method according to the invention, which if appropriate can also consist of several phases and can be present in compressed or uncompressed form.
  • the agent can be present as a free-flowing powder, in particular with a bulk density of 300 g / l to 1200 g / l, in particular 500 g / l to 900 g / l or 600 g / l to 850 g / l.
  • the solid dosage forms of the composition also include extrudates, granules, tablets or pouches.
  • the agent can also be liquid, gelatinous or pasty, for example in the form of a non-aqueous liquid detergent or a non-aqueous paste or in the form of an aqueous liquid detergent or a water-containing paste.
  • the agent may be present as a one-component system. Such means preferably consist of one phase. Alternatively, an agent can also consist of several phases. Such an agent is therefore divided into several components.
  • Detergents or cleaning agents which can be used in the process according to the invention may contain exclusively a hydrolytic enzyme, for example and in particular a protease. Alternatively, however, they may also contain further hydrolytic enzymes or other enzymes in a concentration which is expedient for the effectiveness of the agent, it being possible in principle to use all enzymes established for this purpose in the prior art.
  • Preferred enzymes which can be used as enzymes are all enzymes which can display catalytic activity in the composition, in particular proteases, amylases, cellulases, hemicellulases, mannanases, tannases, xylanases, xanthanases, ⁇ -glucosidases, carrageenases, oxidases, perhydrolases, oxidoreductases or lipases, and preferably mixtures thereof.
  • These enzymes are basically of natural origin; Starting from the natural molecules, improved variants are available for use in detergents and cleaners, which are preferably used accordingly.
  • Such a method is advantageous since, as described above, the cleaning performance of a washing or cleaning agent containing a corresponding hydrolytic enzyme is improved by the addition of a component as indicated.
  • the method is advantageous to remove from textiles or hard surfaces corresponding contaminants, especially proteinaceous impurities.
  • Embodiments of this subject invention include, for example, hand washing, manual removal of stains from textiles or from hard surfaces or machine processes.
  • Methods for cleaning textiles are generally distinguished by the fact that various cleaning-active substances are applied to the items to be cleaned in a plurality of process steps and washed off after the action time, or that the items to be cleaned are otherwise treated with a detergent or a solution of this agent. The same applies to methods for cleaning hard surfaces.
  • a hydrolytic enzyme i. Component (a)
  • a hydrolytic enzyme which naturally already possesses a hydrolytic activity and also unfolds these in media which otherwise have no cleaning power, such as, for example, in mere buffer
  • such a method can also consist merely in that apart from the added component (b) the only other Component a hydrolytic enzyme, ie Component (a) is applied, preferably in a buffer solution or in water.
  • All processes of the invention are preferably in a temperature range of 10 ° C to 60 ° C, in particular from 10 ° C to 50 ° C, from 10 ° C to 40 ° C, from 10 ° C to 30 ° C, from 15 ° C to 30 ° C from 10 ° C to 25 ° C and from 15 ° C to 25 ° C performed.
  • a synergistic interaction of the components (a) and (b) with regard to the cleaning performance is especially at these lower to middle washing temperatures or cleaning temperatures.
  • the assays were assembled into 48-well plates in 1 ml each of wash liquor as shown in Table 3 below. The incubation was carried out for 60 minutes at 40 ° C with shaking (about 600 revolutions per minute (rpm)).
  • Table 3 volumes solution 420 ⁇ l 161-966 mg of laundry detergent in 42 ml of water or buffer 30-530 ⁇ l 1-100 PE / ml protease 30-530 ⁇ l Prepared substance solution rest H 2 O Soiling ⁇ approx. 1cm
  • Proteases used were the alkaline protease from Bacillus lentus DSM 5483 ( WO 92/21760 ), the protease from Bacillus pumilus according to WO2007 / 131656 and the protease shown in FIG. 2 or SEQ ID NO. 3 of the international publication WO 03/057713 is disclosed.
  • component (b) polyglutamate (poly-glutamic acid), lysine, phenylalanine, tyrosine, alanine, leucine, proline, cysteine, threonine, serine, glycine, aspartate, asparagine, 2,3- Butanediol, pyruvate, propionate, butyrate, levan and surfactin.
  • Stock solutions of these substances were prepared with 0.00001-1.5 M substance or 0.0001-55% (weight) in water or buffer (phosphate 0.00001-1.5 M pH 6.5-8.0 or Tris 0.00001-1.5 M pH 7.5-9.0 or Soerensen buffer pH 7.5-9.0 or citrate buffer 0.00001-1.5 M pH 4.5-7.0 or acetate buffer 0 , 00001-1.5 M pH 2.5-5.5).
  • buffer phosphate 0.00001-1.5 M pH 6.5-8.0 or Tris 0.00001-1.5 M pH 7.5-9.0 or Soerensen buffer pH 7.5-9.0 or citrate buffer 0.00001-1.5 M pH 4.5-7.0 or acetate buffer 0 , 00001-1.5 M pH 2.5-5.5).
  • the washing performance was increased with bacterial or fungal fermenter supernatants and nutrient media (culture supernatants) or fractions from the purification of these fluids, especially with Bacillus fermenter and Bacillus culture media and fractions containing such substances.
  • component (b) Used as component (b) were therefore culture supernatants or dilutions of two different cultures of Bacillus sp. (Strain 1 or strain 2) as well as differently processed and / or fractionated preparations of the supernatants as indicated in each case.
  • the washing performance was achieved with surfactin or lichenycin or fermented supernatants from microorganisms producing surfactin, lichenigen or similar lipopeptide-type molecules.
  • surfactin-like or surfactin-like molecules were detected by mass spectroscopy.
  • Tables 16 to 19 below show the washings obtained. It is clear that the components used (b) cause a synergistic increase in the washing performance of those detergents containing a hydrolytic enzyme, namely a protease, ie component (a). In controls which do not contain a hydrolytic enzyme, these components (b) do not increase the washing performance, so that the increased washing performance is due to an advantageous synergistic interaction of components (a) and (b).
  • An inactivated hydrolytic enzyme (see Table 19) also results in no longer a synergistic cleaning performance, which is further evidence of the specific advantageous interaction of components (a) and (b).

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ES2753240T3 (es) 2020-04-07
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PL2313482T5 (pl) 2023-02-27
EP2313483B1 (fr) 2018-06-20
DE102008038479A1 (de) 2010-02-25
EP2727988A2 (fr) 2014-05-07
PL2727989T5 (pl) 2023-03-27
EP2727989B1 (fr) 2019-06-26
EP2313482A2 (fr) 2011-04-27
ES2744829T5 (es) 2022-10-19
ES2745761T3 (es) 2020-03-03
PL2727989T3 (pl) 2019-12-31
EP2727988A3 (fr) 2016-03-16
EP2727990A3 (fr) 2016-03-16
WO2010020475A3 (fr) 2010-06-17
EP2313483A2 (fr) 2011-04-27

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