EP2727989B2 - 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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EP2727989B2
EP2727989B2 EP14152970.1A EP14152970A EP2727989B2 EP 2727989 B2 EP2727989 B2 EP 2727989B2 EP 14152970 A EP14152970 A EP 14152970A EP 2727989 B2 EP2727989 B2 EP 2727989B2
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Prior art keywords
cleaning
washing
protease
agent
chr
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German (de)
English (en)
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EP2727989A3 (fr
EP2727989A2 (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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    • 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
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    • 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
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    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
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    • C11D3/2003—Alcohols; Phenols
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    • C11D3/16—Organic compounds
    • C11D3/20—Organic compounds containing oxygen
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    • C11D3/2086—Hydroxy carboxylic acids-salts thereof
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    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
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    • C11D3/22—Carbohydrates or derivatives thereof
    • C11D3/221—Mono, di- or trisaccharides or derivatives thereof
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    • 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
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    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
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    • C11D3/33—Amino carboxylic acids
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    • C11D3/3719—Polyamides or polyimides
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    • C11D3/3757—(Co)polymerised carboxylic acids, -anhydrides, -esters in solid and liquid compositions
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    • C11D3/37—Polymers
    • C11D3/3746—Macromolecular compounds obtained by reactions only involving carbon-to-carbon unsaturated bonds
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    • C11D3/16—Organic compounds
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    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
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    • 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
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    • C11D3/38645—Preparations containing enzymes, e.g. protease or amylase containing cellulase

Definitions

  • the present application is directed to the use of a microbial metabolite to increase the cleaning performance of a protease in a washing or cleaning process.
  • enzymes in detergents and cleaning agents serve to expand the range of services of the funds concerned according to their specific activities.
  • hydrolytic enzymes such as proteases, amylases, lipases and cellulases.
  • the first three hydrolyze proteins, starch and fats and thus contribute directly to dirt removal.
  • Cellulases are used in particular because of their tissue effect.
  • Another group of detergent and cleaning agent enzymes are oxidative enzymes, in particular oxidases, which optionally in combination with other components preferably serve to bleach soiling or to generate the bleaching agents in situ.
  • enzymes which are subject to continuous optimization
  • other enzymes are constantly being made available for use in detergents and cleaning agents, in order to be able to optimally deal with special soiling in particular, such as pectinases, ⁇ -glucanases, mannanases or other hemicellulases for hydrolysis, in particular special ones plant polymers.
  • proteases and in particular serine proteases which also include the subtilases. They break down proteinaceous soiling on the items to be cleaned.
  • proteases of the subtilisin type (subtilases, subtilopeptidases, EC 3.4.21.62) are particularly important, which are assigned to the serine proteases because of the catalytically active amino acids. They act as non-specific endopeptidases, which means they hydrolyze any acid amide bonds that are inside peptides or proteins. Their optimum pH is usually in the clearly alkaline range.
  • Subtilases: Subtilisin-like Proteases by R.
  • Subtilisin enzymes edited by R. Bott and C. Betzel, New York, 1996 .
  • Subtilases are naturally produced by microorganisms; among these, the subtilisins formed and secreted by Bacillus species should be mentioned in particular as the most important group within the subtilases.
  • subtilisin-type proteases preferably used in detergents and cleaning agents 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, and subtilisin DY the enzymes thermitase, proteinase K and the proteases TW3 and TW7, which can be assigned to the subtilases, but no longer to the subtilisins in the narrower sense.
  • proteases that can be used are, for example, those under the trade names Durazym® , Relase® , Everlase®, Nafizym , Natalase® , Kannase® and Ovozyme® from Novozymes, those under the trade names Purafect®, Purafect® OxP , Purafect® Prime and Properase ® from Genencor, sold under the trade name Protosol ® from Advanced Biochemicals Ltd., Thane, India, sold under the trade name Wuxi ® from Wuxi Snyder Bioproducts Ltd., China, sold under the trade names Proleather ® and Protease P ® from Amano Pharmaceuticals Ltd., Nagoya, Japan, and the enzyme available under the name Proteinase K-16 from Kao Corp., Tokyo, Japan.
  • the present invention is therefore based on the object of improving the cleaning performance (washing power) of detergents or cleaning agents with regard to soiling that is sensitive to degradation by proteases.
  • a further object of the invention is to improve the cleaning performance of proteases in detergents or cleaning agents or the wash liquor formed by the detergents or cleaning agents with regard to soiling that is sensitive to degradation by proteases, and in particular in a temperature range between 10°C and 50°C, between 10°C and 40°C and preferably between 10°C and 30°C or 10°C and 25°C.
  • the invention thus relates to the use of a microbial metabolite to increase the cleaning performance of a protease in a washing or cleaning process, characterized in that the microbial metabolite is selected from the group consisting of 2,3-butanediol, pyruvate, propionate, butyrate and levan .
  • cleaning performance of detergents or cleaning agents is significantly improved if in these agents at least one protease (herein also referred to as component (a) or hydrolytic enzyme (a)) with a microbial metabolite , selected from the group consisting of 2,3-butanediol, pyruvate, propionate and levan (also referred to herein as component (b)).
  • component (a) or hydrolytic enzyme (a) with a microbial metabolite , selected from the group consisting of 2,3-butanediol, pyruvate, propionate and levan
  • cleaning performance is understood to mean the lightening performance on one or more stains, in particular laundry stains, which are sensitive to degradation by proteases.
  • stains are blood-milk/ink on cotton, whole egg/pigment on cotton, chocolate-milk/ink on cotton, peanut oil-pigment/ink on polyester/cotton, grass on cotton or cocoa on cotton, especially such as indicated below.
  • both the washing or cleaning agent which comprises the protease, or the washing or cleaning liquor formed by this agent, and the protease itself have a respective cleaning performance.
  • the cleaning performance of the protease thus contributes to the cleaning performance of the agent or the washing or cleaning liquor formed by the agent.
  • the cleaning performance of detergents and cleaning agents, based on the proteolytic activity used, is improved by adding component (b).
  • component (a) and (b) With regard to the interaction of these components (a) and (b), there is a synergistic effect, i.e. better performance compared to the individual performance of the respective component in one-component systems (i.e. detergents or cleaning agents that only contain the proteolytic enzyme or contain component (b)) and also compared to the sum of the individual performances of components (a) and (b), i.e. the sum of two one-component systems each with component (a) and (b) alone.
  • the selected combination of (a) protease with a component (b) according to the invention thus represents a further possibility for improving the performance of detergents or cleaning agents with regard to their cleaning performance, in particular with regard to their cleaning performance, which is brought about by a protease present.
  • washing or cleaning liquor is understood to mean the working solution containing the washing or cleaning agent which acts on textiles or fabrics (washing 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 is usually formed when the washing or cleaning process begins and the washing or cleaning agent is dissolved in water or diluted with water, for example in a washing machine or in another suitable container.
  • subtilisin type those of the subtilisin type are preferred.
  • these are the subtilisins BPN' and Carlsberg, the protease PB92, the subtilisins 147 and 309, the alkaline protease from Bacillus lentus, subtilisin DY and the subtilases, but no longer the subtilisins in the narrower sense, thermitase, proteinase K and the enzymes proteases TW3 and TW7.
  • Subtilisin Carlsberg is available in a further developed form under the trade name Alcalase® from Novozymes A/S, Bagsvaerd, Denmark.
  • subtilisins 147 and 309 are marketed under the trade names Esperase® and Savinase® by the Novozymes company.
  • the protease variants listed under the name BLAP® are derived from the protease from Bacillus lentus DSM 5483.
  • proteases are, for example, those sold 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, Excellase ® and Properase ® from Genencor, sold under the trade name Protosol ® from Advanced Biochemicals Ltd., Thane, India, sold under the trade name Wuxi ® from Wuxi Snyder Bioproducts Ltd., China, sold under the trade names Proleather ® and Protease P ® from Amano Pharmaceuticals Ltd., Nagoya, Japan, and the enzyme available under the name Proteinase K-16 from Kao Corp., Tokyo, Japan.
  • the proteases from Bacillus gibsonii and Bacillus pumilus which are disclosed in the international patent applications, are also used with particular preference WO2008/086916 and WO2007/1
  • amylases examples include the ⁇ -amylases from Bacillus licheniformis, from B. amyloliquefaciens or from B. stearothermophilus, and further developments thereof which have been improved for use in detergents or cleaning agents.
  • the enzyme from B. licheniformis is available from Novozymes under the name Termamyl® and from Genencor under the name Purastar® ST. Further development products of this ⁇ -amylase are from the from Novozymes under the trade names Duramyl® and Termamyl® ultra, from Genencor under the name Purastar® OxAm and from Daiwa Seiko Inc., Tokyo, Japan, as Keistase® .
  • the ⁇ -amylase from B. amyloliquefaciens is marketed by the company Novozymes under the name BAN® , and variants derived from the ⁇ -amylase from B. stearothermophilus under the names BSG® and Novamyl® , also from the company 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 can be used, which belong to the sequence space of ⁇ -amylases 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 the molecules mentioned can also be used.
  • ⁇ -amylase from Aspergillus niger and A. oryzae available under the trade names Fungamyl® from Novozymes are also suitable.
  • Other commercial products that can be used are, for example, Amylase- LT® and Stainzyme® or Stainzyme ultra® or Stainzyme plus® , the latter also from Novozymes. Variants of these enzymes obtainable by point mutations can also be used according to the invention.
  • Examples of usable lipases or cutinases which are included in particular because of their triglyceride-cleaving activities, but also to generate peracids in situ from suitable precursors, are the lipases originally available from Humicola lanuginosa (Thermomyces lanuginosus), or further developed, in particular those with the amino acid substitution D96L. They are marketed, for example, by the Novozymes company 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 that can also be used are available from the Amano company 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 ® available.
  • the lipases or cutinases from Genencor can be used, the starting enzymes of which were originally isolated from Pseudomonas mendocina and Fusarium solanii.
  • Lipase® and Lipomax® originally marketed by Gist-Brocades and the enzymes marketed by Meito Sangyo KK, Japan, under the names Lipase MY- 30® , Lipase OF® and Lipase PL® Mention should also be made of the product Lumafast® from Genencor .
  • cellulases can be present as pure enzymes, as enzyme preparations or in the form of mixtures in which the individual components advantageously complement one another with regard to their various aspects of performance. These performance aspects include, in particular, the contributions of cellulase to the primary washing performance of the agent (cleaning performance), to the secondary washing performance of the agent (anti-redeposition effect or graying inhibition), to finishing (fabric effect) or to exerting a "stone washed" effect.
  • cleaning performance the contributions of cellulase to the primary washing performance of the agent
  • anti-redeposition effect or graying inhibition to finishing (fabric effect) or to exerting a "stone washed” effect.
  • a usable fungal cellulase preparation rich in endoglucanase (EG) or its further developments is offered by the company Novozymes under the trade name Celluzyme® .
  • Endolase® and Carezyme® which are also available from Novozymes, are based on the 50 kD EG and the 43 kD EG, respectively, from H. insolens DSM 1800.
  • Other commercial products from this company that can be used are Cellusoft® , Renozyme® and Celluclean® .
  • Also usable are, for example, the 20 kD EG from Melanocarpus, which are available from AB Enzymes, Finland, under the trade names Ecostone® and Biotouch® .
  • Other commercial products from AB Enzymes are Econase® and Ecopulp® .
  • Other suitable cellulases are from Bacillus sp. CBS 670.93 and CBS 669.93, wherein the Bacillus sp. CBS 670.93 is available from Genencor under the trade name Puradax®.
  • Other commercial products from Genencor are “Genencor detergent cellulase L” and IndiAge® Neutra.
  • Suitable enzymes in this regard are available, for example, 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 ⁇ -glucanase obtained from Bacillus subtilis is available under the name Cereflo® from Novozymes.
  • Hemicellulases that are particularly preferred according to the invention are mannanases, which are marketed, for example, under the trade names Mannaway(R) by the company Novozymes or Purabrite® by the company Genencor.
  • the enzymes can be packaged together with accompanying substances, for example from the fermentation or with stabilizers.
  • Agents used 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 preferably 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 particularly preferably from 0.075 to 3.5% by weight. -% contained in these funds, each contained enzyme may be present in the amounts mentioned.
  • the protein concentration can be determined using known methods, for example the BCA method (bicinchoninic acid; 2,2'-biquinolyl-4,4'-dicarboxylic acid) or the biuret method ( AG Gornall, CS Bardawill and MM David, J. Biol. Chem., 177 (1948), pp. 751-766 ) are determined.
  • BCA method bicinchoninic acid; 2,2'-biquinolyl-4,4'-dicarboxylic acid
  • the biuret method AG Gornall, CS Bardawill and MM David, J. Biol. Chem., 177 (1948), pp. 751-766
  • the protease used as component (a) and the optionally at least one further hydrolytic enzyme present in a washing or cleaning agent supports the cleaning performance of the agent with regard to specific soiling or stains.
  • a composition particularly preferably contains a plurality of enzymes, it being possible for the enzymes to belong to the same or different enzyme classes.
  • the enzymes particularly preferably show synergistic effects with regard to their action on certain soiling or stains, i.e. the enzymes contained in the agent composition support each other in their cleaning performance.
  • a protease (a) is combined with a component (b), i.e. at least one substance which, in conjunction with the protease (a) when the agent is used, brings about a synergistic cleaning performance and which is selected from a microbial metabolite (iii).
  • the agent may contain an (i) amino acid or polyamino acid or derivative thereof and/or a (ii) biosurfactant.
  • the substances specified under (i) are preferably amino acids or polymers thereof or their salts or their derivatives, it being possible to use both stereoisomers of the amino acids, ie both D- and L-amino acids, also in combination, or corresponding ones polymers or derivatives.
  • a polyamino acid comprises at least two amino acid residues. Glutamate, polyglutamate, lysine, glutamine, histidine, phenylalanine, tyrosine, alanine, leucine, isoleucine, methionine, proline, valine, glutamine, cysteine, tryptophan, threonine, serine, glycine, aspartate and asparagine are particularly preferred.
  • Polyglutamic acid including ⁇ -D-polyglutamic acid, L-polyglutamic acid and DL-polyglutamic acid
  • polyaspartic acid including ⁇ -D-polyaspartic acid and L-polyaspartic acid
  • polyglutamine including ⁇ -D-polyglutamine, L -polyglutamine and DL-polyglutamine
  • 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 are substances that are formed by microorganisms and are often also separated.
  • 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.
  • Biosurfactants preferred according to the invention belong primarily to the substance group of 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 can be linear, cyclic or branched.
  • monomeric building blocks are not only proteinogenic L-amino acids, but also D-amino acids and alpha-hydroxy and/or carboxylic acids of all kinds.
  • biosurfactants are anionic lipopeptides and more preferably surfactin-like or lichenysin-like substances or surfactin or lichenysin itself and/or which have an effect comparable to surfactin or lichenysin.
  • 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 figure 1 specified.
  • Lichenysin 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, the term lichenysin encompasses both terms.
  • 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.
  • Bacillus licheniformis surfactin Bacillus subtilis, Bacillus pumilus viscosine Pseudomonas fluorescens Ornithine, lysine peptides Thiobacillus thiooxidans Streptomyces sioyaensis Gluconobacter cerinus phospholipids Acinetobacter sp. sulfonylipids T. thioosidans Corynebacterium alkanolyticum fatty acids Capnocytophaga sp.
  • the substances specified under (iii) are microbial metabolites. These are understood to be substances which are formed by the microorganism as intermediate stages or as degradation products of metabolic processes of the microorganism or as degradation products of nutrient medium. According to the invention, preferred microbial metabolites are present in the culture medium of a culture of the microorganism forming them. They are therefore particularly preferably secreted by the microorganism that forms them. Microbial metabolites used according to the invention are 2,3-butanediol, pyruvate, propionate, butyrate.
  • Acetate, lactate, 2-methylpropionate, 3-methylbutyrate, ⁇ -ketogluterate, acetoin, propanediol, glycol, glycerol, citrate, formate, ethanol, methanol or butanol can be mentioned as further microbial metabolites.
  • Component (b) is preferably added to the detergent or cleaning agent as a separate individual substance, i.e. not as part of another ingredient in the detergent or cleaning agent.
  • Component (b) is therefore preferably freely present in the washing or cleaning agent, i.e. it is distributed in it 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 administration form of the hydrolytic enzyme (a), in particular not as part of an enzyme granulate.
  • Liquid or gel-like, i.e. non-solid, washing or cleaning agents are preferred according to the invention.
  • a preferred liquid detergent for such a washing system is composed as follows (all data in percent by weight): 0.3-0.5% xanthan gum, 0.2-0.4% anti-foam agent, 6-7% glycerin, 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, remainder demineralised water.
  • the dosage of the liquid detergent is preferably between 4.5 and 5.5 grams per liter of wash liquor, for example 4.9 grams per liter of wash liquor. Washing is preferably carried out 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 data in percent by weight): 10% linear alkyl benzene sulfonate (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 hydrogen carbonate, 4.0% amorphous sodium disilicate, 17% sodium carbonate peroxohydrate, 4.0% TAED, 3.0% polyacrylate, 1.0% carboxymethyl cellulose, 1.0% phosphonate, 25% sodium sulphate, remainder: optional foam inhibitors, optical brightener, fragrances and optionally water to 100%.
  • the dosage of the liquid detergent is preferably between 6.0 and 7.0 grams per liter of wash liquor, for example 6.7 grams per liter of wash liquor. Washing is preferably carried out in a pH value range between pH 9 and pH 11.
  • a liquid detergent is preferably used.
  • the degree of whiteness i.e. the lightening of the soiling, is preferably determined using optical measuring methods, preferably photometrically.
  • a suitable device for this is, for example, the Minolta CM508d spectrometer.
  • the devices used for the measurement are usually calibrated beforehand with a white standard, preferably a supplied white standard.
  • the respective enzymatic properties for example the washing performance on certain types of soiling, are compared.
  • a low specific activity can be compensated for by adding a larger amount of protein.
  • Methods for determining the enzyme activities are familiar to the person skilled in the field of enzyme technology and are routinely used by him. For example, methods for determining protease activity are disclosed in Surfactants, Vol. 7 (1970), pp. 125-132 .
  • the protease activity is preferably given in PE (protease units).
  • suitable protease activities are 5 or 10 PU (protease units) per ml of wash liquor.
  • the enzymatic activity used is not zero.
  • the synergistic cleaning performance is preferably based on a new mechanism of action, ie there is no increase in the enzyme activity per se in the classical sense, as would be measured in one of the following methods—relative to proteases. Accordingly, a synergism according to the invention is also present in particular when an improved cleaning performance is determined in the presence of components (a) and (b) compared to the sum of the cleaning performances of component (a) alone and component (b) alone, and component ( b) in at least one of the following test methods, preferably in both of the following test methods, no effect with regard to increasing the proteolytic activity of component (a) over the measurement-related standard deviation shows:
  • the protease activity is determined quantitatively via 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 the pNA causes an increase in absorbance at 410 nm, the time course of which is a measure of the enzymatic activity (cf. Del Mar et al., 1979).
  • the measurement is carried out at a temperature of 25°C, at pH 8.6 and at a wavelength of 410 nm.
  • the measurement time is 5 minutes and the measurement interval is 20s to 60s.
  • the working 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 a cuvette for each sample. 1-300 ⁇ l of the buffer or the Component (b) (0.1, 0.2, 0.5 or 1% by weight in working buffer) is added to the cuvette. 1-300 ⁇ l of the protease or the blank sample are added to 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. Activation or stabilization of the protease can be quantified using the measurement data.
  • 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 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).
  • TCA stop reagent
  • the stop reagent is added prior to enzyme addition, with or without the substance to be tested.
  • the reaction mixtures are filtered through Whatman #42 filter paper or centrifuged.
  • a particularly advantageous synergistic cleaning performance also results from the fact that the substance used as component (b) is present in the washing or cleaning liquor in a specific concentration, for example 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.
  • Washing and cleaning agents that can be used according to the invention include all conceivable types of washing and cleaning agents, both concentrates and agents to be used undiluted, for use on a commercial scale, in the washing machine or for hand washing or hand cleaning. These include, for example, detergents for textiles, carpets, or natural fibers, for which the term detergent is used. This also includes, for example, dishwashing detergents for dishwashers or manual dishwashing detergents or cleaners for hard surfaces such as metal, glass, porcelain, ceramics, tile, stone, painted surfaces, plastics, wood or leather, for which the term detergent is used, i.e. in addition to manual and machine Dishwashing detergents, for example, also scouring agents, glass cleaners, toilet deodorizers, etc.
  • detergents and cleaning agents within the scope of the invention also include washing aids that are added to the actual detergent in manual or machine washing in order to achieve a further effect.
  • detergents and cleaning agents within the scope of the invention also include textile pre-treatment and after-treatment agents, i.e. those agents with which the item of laundry is brought into contact before the actual wash, for example to loosen stubborn dirt, and also those agents which are in one of the actual Textile washing subsequent step give the laundry other desirable properties such as a pleasant feel, crease resistance or low static charge.
  • the latter means include fabric softeners.
  • the detergents or cleaning agents that can be used according to the invention which can be in the form of, in particular, powdered solids, in post-compacted particle form, as homogeneous solutions or suspensions, can in principle be all known and present in such Means contain usual ingredients, preferably at least one other ingredient is present in the agent.
  • the funds can in particular builder substances, 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, graying inhibitors, foam regulators and dyes and fragrances as well combinations thereof included.
  • a further combination of the active ingredients according to the invention with one or more other ingredient(s) of the agent has proven to be advantageous, since a further improved cleaning performance can then be achieved through further resulting synergisms.
  • a further synergism is achieved in particular through the combination with a surfactant and/or a builder substance and/or a bleaching agent.
  • Such preferred further ingredients of the washing or cleaning agent are disclosed in the international patent application WO 2009/021867 , to the disclosure of which reference is therefore expressly made or the disclosure of which is therefore expressly included in the present application.
  • the ingredients to be selected and the conditions under which the agent is used should be optimized for the cleaning problem in question.
  • normal temperatures for the use of detergents and cleaning agents are in the range of 10° C., over 40° C. and 60° C. up to 95° C. for mechanical agents or for technical applications.
  • the ingredients of the agents in question are preferably matched to one another, in particular in such a way that synergies result in terms of the cleaning performance.
  • Synergies that are present in a temperature range between 10°C and 60°C, in particular in a temperature range from 10°C to 50°C, from 10°C to 40°C, from 10°C to 30°C, are particularly preferred , 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 that can be used according to the invention also contains the hydrolytic enzyme in an amount of 2 mg to 20 mg, preferably 5 mg to 17.5 mg, particularly preferably 20 mg to 15 mg and very particularly preferably 50 mg to 10 mg per g of the means
  • the hydrolytic enzyme contained in the agent, in particular a protease, and/or other ingredients of the agent can be coated with a substance which is impermeable to the enzyme at room temperature or in the absence of water and which becomes permeable to the enzyme under conditions of use of the agent.
  • Such an embodiment of the invention is thus characterized in that the hydrolytic enzyme is coated with a substance which is impermeable to the enzyme at room temperature or in the absence of water.
  • the washing or cleaning agent itself can also 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 also include all solid, powdery, liquid, gel-like or pasty forms of administration of the agents that can be used according to the invention, which can optionally also consist of several phases and can be in compressed or non-compressed form.
  • the agent can be in the form of 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 agent also include extrudates, granules, tablets or pouches.
  • the agent can also be liquid, gel-like 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 can be in the form of a one-component system. Such means preferably consist of one phase.
  • a remedy can also consist of several phases. Such a remedy is therefore divided into several components.
  • Detergents or cleaning agents that can be used according to the invention can contain only one protease. Alternatively, however, they can also contain further hydrolytic enzymes or other enzymes in a concentration suitable for the effectiveness of the agent, it being possible in principle to use all enzymes established in the prior art for these purposes.
  • All enzymes which can develop a catalytic activity in the agent can preferably be used as further enzymes, in particular proteases, amylases, cellulases, hemicellulases, mannanases, tannases, xylanases, xanthanases, ® -glucosidases, carrageenases, oxidases, perhydrolases, oxidoreductases or lipases, and preferably mixtures thereof.
  • proteases amylases, cellulases, hemicellulases, mannanases, tannases, xylanases, xanthanases, ® -glucosidases, carrageenases, oxidases, perhydrolases, oxidoreductases or lipases, and preferably mixtures thereof.
  • proteases amylases
  • cellulases hemicellulases
  • mannanases tannases
  • Such a method is advantageous since, as described above, the cleaning performance of a washing or cleaning agent which contains a protease is improved by the addition of a component as indicated.
  • the method is therefore advantageous for removing such contamination, in particular protein-containing contamination, from textiles or from hard surfaces.
  • Embodiments are, for example, hand washing, manual removal of stains from textiles or hard surfaces, or mechanical processes.
  • Processes for cleaning textiles are generally characterized in that various cleaning-active substances are applied to the items to be cleaned in several process steps and washed off after the exposure time, or that the items to be cleaned are treated in some other way with a detergent or a solution of this agent. The same applies to processes for cleaning hard surfaces.
  • a protease i.e. component (a)
  • a protease i.e. component (a)
  • a protease i.e. component (a)
  • a buffer solution or in water preferably in a buffer solution or in water.
  • All the methods described here are preferably carried out in a temperature range from 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.
  • a synergistic interaction of components (a) and (b) with regard to the cleaning performance is particularly present at these lower to medium washing temperatures or cleaning temperatures.
  • components (a) and (b) work together advantageously, in particular synergistically, so that not only the cleaning performance of a detergent or cleaning agent (or the washing liquor formed from this agent) is improved, but also the cleaning performance of the protease even.
  • test batches were assembled in 48-well plates in 1 ml wash liquor each as indicated in Table 3 below. The incubation took place for 60 minutes at 40° C. with shaking (about 600 revolutions per minute (rpm)).
  • Table 3 volumes solution 420 ⁇ l 161-966 mg laundry detergent in 42 ml water or buffer 30-530 ⁇ l 1-100 PU/ml protease 30-530 ⁇ l Prepared substance solution rest H2O Soiling ⁇ approx. 1cm
  • the soiling was rinsed, dried and fixed three times and the degree of whiteness of the washed textiles was measured in comparison to a whiteness standard (d/8, 8mm, SCI/SCE), which had been normalized to 100% (determination of the L value) .
  • the measurement was carried out using a colorimeter (Minolta Cm508d) with an illuminant setting of 10°/D65. The results obtained are given as percentage performance, the difference in the remission values of the basic detergent without substance or enzymes and that with protease being normalized to 100%.
  • 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 disclosure document WO 03/057713 is revealed.
  • Stock solutions of these substances were prepared at 0.00001-1.5 M substance or 0.0001-55% (wt) 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.

Claims (2)

  1. Utilisation d'un métabolite microbien permettant d'améliorer le pouvoir nettoyant d'une protéase dans un processus de lavage ou de nettoyage, caractérisée en ce que le métabolite microbien est choisi dans le groupe constitué par le 2,3-butanediol, le pyruvate, le propionate, le butyrate et la lévane.
  2. Utilisation selon la revendication 1, caractérisée en ce que le métabolite microbien présente une masse moléculaire (MW) de 150 à 5 × 106 daltons, en particulier de 200 à 1 × 106daltons, de 220 à 0,75 × 106 daltons et en particulier de 400 à 0,5 × 106 daltons.
EP14152970.1A 2008-08-20 2009-07-10 Procédé d'amélioration de la puissance de nettoyage d'un produit de lavage et de nettoyage Active EP2727989B2 (fr)

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DE102008038479A DE102008038479A1 (de) 2008-08-20 2008-08-20 Wasch- oder Reinigungsmittel mit gesteigerter Waschkraft
EP09780407.4A EP2313482B2 (fr) 2008-08-20 2009-07-10 Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant
PCT/EP2009/058789 WO2010020475A2 (fr) 2008-08-20 2009-07-10 Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant

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EP14152970.1A Active EP2727989B2 (fr) 2008-08-20 2009-07-10 Procédé d'amélioration de la puissance de nettoyage d'un produit de lavage et de nettoyage
EP09780407.4A Active EP2313482B2 (fr) 2008-08-20 2009-07-10 Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant
EP14152968.5A Active EP2727988B1 (fr) 2008-08-20 2009-07-10 Procédé d'amélioration de la puissance de nettoyage d'un produit de lavage ou de nettoyage
EP09780409.0A Revoked EP2313483B1 (fr) 2008-08-20 2009-07-10 Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant

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EP14152968.5A Active EP2727988B1 (fr) 2008-08-20 2009-07-10 Procédé d'amélioration de la puissance de nettoyage d'un produit de lavage ou de nettoyage
EP09780409.0A Revoked EP2313483B1 (fr) 2008-08-20 2009-07-10 Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant

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EP (5) EP2727990A3 (fr)
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WO2010020475A3 (fr) 2010-06-17
EP2727988A3 (fr) 2016-03-16
EP2727988A2 (fr) 2014-05-07
PL2727988T3 (pl) 2020-02-28
ES2744829T5 (es) 2022-10-19
WO2010020476A3 (fr) 2010-06-17
US20110136720A1 (en) 2011-06-09
ES2745761T3 (es) 2020-03-03
PL2313482T3 (pl) 2019-11-29
EP2313482B2 (fr) 2022-07-27
EP2727989A3 (fr) 2016-03-16
EP2313482B1 (fr) 2019-06-12
EP2727990A2 (fr) 2014-05-07
US20110201536A1 (en) 2011-08-18
PL2727989T3 (pl) 2019-12-31
WO2010020476A2 (fr) 2010-02-25
EP2727990A3 (fr) 2016-03-16
EP2727988B1 (fr) 2019-09-04
EP2313482A2 (fr) 2011-04-27
ES2744829T3 (es) 2020-02-26
ES2753240T3 (es) 2020-04-07
EP2313483B1 (fr) 2018-06-20
EP2727989A2 (fr) 2014-05-07
EP2313483A2 (fr) 2011-04-27
EP2727989B1 (fr) 2019-06-26
PL2313482T5 (pl) 2023-02-27
WO2010020475A2 (fr) 2010-02-25
ES2745761T5 (es) 2023-03-09
PL2727989T5 (pl) 2023-03-27
DE102008038479A1 (de) 2010-02-25

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