EP2313482B1 - Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant - Google Patents

Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant Download PDF

Info

Publication number
EP2313482B1
EP2313482B1 EP09780407.4A EP09780407A EP2313482B1 EP 2313482 B1 EP2313482 B1 EP 2313482B1 EP 09780407 A EP09780407 A EP 09780407A EP 2313482 B1 EP2313482 B1 EP 2313482B1
Authority
EP
European Patent Office
Prior art keywords
agent
daltons
cleaning
washing
protease
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.)
Active
Application number
EP09780407.4A
Other languages
German (de)
English (en)
Other versions
EP2313482B2 (fr
EP2313482A2 (fr
Inventor
Timothy O'connell
Petra Siegert
Stefan Evers
Johannes Bongaerts
Thomas Weber
Karl-Heinz Maurer
Cornelius Bessler
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Henkel AG and Co KGaA
Original Assignee
Henkel AG and Co KGaA
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Family has litigation
First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=41059950&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=EP2313482(B1) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.
Priority to PL14152968T priority Critical patent/PL2727988T3/pl
Priority to EP14152970.1A priority patent/EP2727989B2/fr
Priority to EP14152968.5A priority patent/EP2727988B1/fr
Priority to PL14152970.1T priority patent/PL2727989T5/pl
Priority to PL09780407.4T priority patent/PL2313482T5/pl
Application filed by Henkel AG and Co KGaA filed Critical Henkel AG and Co KGaA
Publication of EP2313482A2 publication Critical patent/EP2313482A2/fr
Publication of EP2313482B1 publication Critical patent/EP2313482B1/fr
Application granted granted Critical
Publication of EP2313482B2 publication Critical patent/EP2313482B2/fr
Active legal-status Critical Current
Anticipated expiration legal-status Critical

Links

Images

Classifications

    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • 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
    • 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
    • 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
    • C11D3/2079—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
    • 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
    • C11D3/2082—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
    • C11D3/16—Organic compounds
    • 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
    • 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
    • C11D3/38627—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
    • 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
    • C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38645—Preparations containing enzymes, e.g. protease or amylase containing cellulase

Definitions

  • the present application is directed to methods of improving the cleaning performance of a detergent containing a protease.
  • enzymes in detergents and cleaners 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 washing and cleaning agent enzymes are oxidative enzymes, in particular oxidases, which, if appropriate, in combination with other components, are preferably used to bleach soiling or to produce 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 enzymes thermitase, proteinase K and the proteases TW3 and TW7, which are assigned to the subtilases but no longer to the subtilisins in the narrower sense.
  • 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 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 the enzyme available under the name Proteinase K-16 from Kao Corp., Tokyo, Japan.
  • a disadvantage of this prior art proteases preferably used in detergents and cleaners is that they are particularly 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 proteolytic activity and therefore, especially in detergents and dishwashing detergents in this temperature range show no optimal cleaning performance.
  • DE 1942236 A1 and DE 1964792 A1 Detergents containing a protease and a simple amino acid are known DE 2060485 A1 a dishwashing detergent with trypsin or chymotrypsin and certain amino acids and from WO 98/17770 A1 a detergent with polymers and proteases.
  • WO 96/22352 A1 is concerned with improving the storage stability of polyamino acid compounds in detergents, by the polyamino acid and a protein (white egg albumin), for example, in an agglomerate or the like. is present, wherein the detergent may also contain a protease.
  • the present invention is therefore based on the object to improve the cleaning performance (detergency) of detergents or cleaners, especially with regard to soiling, which are 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 of the wash liquor formed by the detergents or cleaners, in particular with regard to soiling, which are sensitive to degradation by proteases and in particular in one Temperature range between 10 ° C and 50 ° C, between 10 ° C and 40 ° C and preferably between 10 ° C and 30 ° C and 10 ° C and 25 ° C.
  • the invention thus relates to a process for improving the cleaning performance of a washing or cleaning agent comprising a protease, characterized in that the washing or cleaning agent, a component is added, which causes a synergistic cleaning performance in conjunction with the protease when using the agent and which is a polyamino acid, wherein the component is present in the agent from 0.018 to 0.2% by weight, in particular from 0.04 to 0.1% by weight, and wherein the washing or cleaning agent comprises the protease 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 composition.
  • cleaning performance of detergents or cleaners is improved significantly if in these agents at least one protease (also referred to herein as component (a) or hydrolytic enzyme (a)) is reacted with a polyamino acid ( Also referred to herein as component (b)) is combined.
  • protease also referred to herein as component (a) or hydrolytic enzyme (a)
  • component (b) polyamino acid
  • cleaning performance is understood to mean the whitening performance of one or more soiling, in particular laundry soiling, which are sensitive to degradation by proteases.
  • both the washing or cleaning agent comprising 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 the addition of component (b).
  • component (b) With regard to the interaction of these components (a) and (b), there is a synergistic effect, ie better performance compared to the individual performances of the respective component in one-component systems (ie detergents containing only the proteolytic enzyme or the component (b)) and also with respect to the sum of the individual powers of the components (a) and (b), ie the sum of two one-component systems each having the components (a) and (b) alone.
  • the selected combination of (a) protease with a component (b) according to the invention represents a further possibility for improving the performance of detergents with regard to their cleaning performance, in particular with regard to their cleaning performance caused by a protease contained.
  • the washing or cleaning liquor is understood to mean 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.
  • subtilisin type examples thereof are the 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, Bagsvaerd, 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, which are 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, 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 the enzyme available under the name Proteinase K-16 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 WO2007 / 131656 ,
  • amylases examples include the ⁇ -amylases from Bacillus licheniformis, B. amyloliquefaciens or B. stearothermophilus and their use in washing or Detergents improved developments.
  • 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 names 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 are contained in particular because of their Triglyceridspaltenden activities, but also to generate from suitable precursors in situ peracids are the lipacases originally from Humicola lanuginosa (Thermomyces lanuginosus), or further developed, in particular those with the amino acid exchange D96L. They are sold, for example, by 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.
  • Other important commercial products are the preparations M1 Lipase.RTM. And Lipomax.RTM.
  • Lipase MY-30® Lipase OF®
  • Lipase PL® Lipase PL® to mention also the product Lumafast® from the company Genencor.
  • cellulases can be used as pure enzymes, as enzyme preparations or in the form of mixtures in which the individual components can be advantageously treated with respect to their properties complement various performance aspects, be present. These 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 cleaning performance
  • 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 the company 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 ⁇ -glucanase obtained from Bacillus subtilis 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. Preferred are the enzymes from 0.001 to 5 wt .-%, more preferably from 0.01 to 5 wt .-%, still more preferably from 0.05 to 4 wt .-% and particularly preferably from 0.075 to 3.5 wt .-% 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 protease used as component (a) and optionally at least one further hydrolytic enzyme present in a detergent or cleaning agent used in the method according to the invention supports the cleaning performance of the composition with respect to certain soils or stains.
  • 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.
  • a protease (a) is combined therewith with a component (b), i. at least one substance which in combination with the protease (a) effects a synergistic cleaning performance when the agent is used and which is selected from a (i) polyamino acid.
  • the agent may contain, in addition to the polyamino acid (i), a biosurfactant (ii) and / or a microbial metabolite (iii).
  • the substances mentioned under (i) are polyamino acids, their salts or their derivatives, where both stereoisomers of the amino acids can be used, that is to say 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. Most preferably it is polyglutamate.
  • 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 -Polyglutamin 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 are understood in the context of the invention substances that are formed by microorganisms and often also deposited.
  • 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, respectively ⁇ -amino acids, but also ⁇ -, ⁇ - or ⁇ -amino acids can be present, both in D and in L configuration.
  • the peptide chains can also undergo 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.
  • the substances mentioned under (iii) 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, sugar, in particular levan, and also others particularly preferred microbial metabolite acetoin.
  • microbial metabolites may also be propanediol, glycol, glycerol, citrate, formate, ethanol, methanol or butanol.
  • Component (b) is preferably added to the detergent or cleaning agent as a separate individual substance, ie not as a component of a further ingredient of the detergent or cleaning agent.
  • the component (b) is therefore preferably free in the washing or cleaning agent, ie it is distributed in this and distributed as homogeneously as possible.
  • the component (b) is preferably dissolved or dispersed in these.
  • 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 Dosing of the liquid detergent between 4.5 and 5.5 grams per liter of wash liquor, for example, 4.9 grams per liter of wash liquor.
  • 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% carboxymethyl cellulose, 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 determining protease activity are disclosed in Tenside, Vol. 7 (1970), pp. 125-132 , The protease activity is preferably indicated in PE (protease units). For example, suitable protease activities are 5 or 10 PE (protease units) per ml wash liquor. However, 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 greater than the sum of the cleaning powers of component (a) alone and component (b) alone and component (b) in at least one of the subsequent test methods, preferably in both subsequent test methods, has no effect in terms of increasing the proteolytic activity of component (a) beyond the measurement-related standard deviation:
  • 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 substances optionally used in addition to the polyamino acid used as component (b) are present in certain concentrations in the washing or cleaning agent.
  • the method is characterized in that the biosurfactant is present in the agent from 0.001% to 25% by weight, in particular from 0.005 to 10% by weight, and / or the microbial metabolite is present in the agent 0.018 to 0.2 wt .-%, in particular from 0.04 to 0.1 wt .-%.
  • 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 .-%.
  • 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.
  • dishwashing detergents or manual dishwashing detergents or hard surface cleaners such as metal, glass, porcelain, ceramic, tile, stone, painted surfaces, plastics, wood or leather for which the term detergent is used, in addition to manual and automatic dishwashing detergents, are also included
  • the detergents and cleaning agents in the invention also include laundry 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.
  • the fabric softeners are calculated.
  • the detergents or cleaning agents which can be used in the process according to the invention which can be in the form of homogeneous solutions or suspensions, in particular in powdered solids, 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, 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 dyes and perfumes and Combinations of these included.
  • 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.
  • ingredients to be selected as well as the conditions under which the agent is used should be optimized for the particular 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.
  • the hydrolytic enzyme contained in the agent in particular a protease, and / or further ingredients of the agent may be enveloped with a substance impermeable to the enzyme at room temperature or in the absence of water, which under application conditions of the agent is permeable to the substance Enzyme becomes.
  • a substance impermeable to the enzyme at room temperature or in the absence of water which under application conditions of the agent is permeable to the substance Enzyme becomes.
  • 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 only one 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 because, as described above, the cleaning performance of a washing or cleaning agent containing a protease 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 for example, the Hand wash, the manual removal of stains from textiles or 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 protease i. Component (a)
  • a protease which naturally already possesses a proteolytic 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 protease, 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.
  • Another object of the invention is the use of a component which is a polyamino acid to achieve a synergistic cleaning performance in conjunction with a protease, wherein the component is present in the agent from 0.018 to 0.2 wt .-%, in particular from 0.04 to 0.1 wt .-% and wherein the detergent or cleaning agent, the protease in an amount of 2 micrograms to 20 mg, preferably from 5 micrograms to 17.5 mg, more preferably from 20 micrograms to 15 milligrams, and most preferably from 50 ⁇ g to 10 mg per g of the agent.
  • the use is accordingly characterized in that the agent additionally contains a biosurfactant in an amount of 0.001% to 25% by weight, in particular of 0.005 to 10% by weight, and / or a microbial metabolite in an amount of 0.018 to 0.2 wt .-%, in particular from 0.04 to 0.1 wt .-%.
  • a biosurfactant in an amount of 0.001% to 25% by weight, in particular of 0.005 to 10% by weight
  • / or a microbial metabolite in an amount of 0.018 to 0.2 wt .-%, in particular from 0.04 to 0.1 wt .-%.
  • Another object of the invention is the use of a component which is a polyamino acid for increasing the cleaning performance of a protease in a washing or cleaning process, wherein the component is present in the agent from 0.018 to 0.2 wt .-%, in particular from 0, 04 to 0.1 wt .-% and wherein the washing or cleaning agent, the protease in an amount of 2 micrograms to 20 mg, preferably from 5 micrograms to 17.5 mg, more preferably from 20 micrograms to 15 mg, and most preferably from 50 ⁇ g to 10 mg per g of the agent.
  • the components (a) and (b) work together advantageously, in particular synergistically, so that not only the cleaning performance of a washing or cleaning agent (or the wash liquor formed by this agent) is improved, but also the cleaning performance of the protease
  • a washing or cleaning agent or the wash liquor formed by this agent
  • the cleaning performance of the protease The facts, objects and embodiments described for washing or cleaning processes according to the invention are also applicable to this subject of the invention. Therefore, reference is made at this point expressly to the disclosure in the appropriate place with the statement that this disclosure also applies to the above inventive use.
  • 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.
  • polyglutamate poly-glutamic acid
  • Stock solutions of this substance 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).

Claims (14)

  1. Procédé d'amélioration du pouvoir nettoyant d'un agent de lavage ou nettoyant, comprenant une protéase, caractérisé en ce qu'un composant est ajouté à l'agent de lavage ou nettoyant, ledit composant agissant sur un pouvoir nettoyant synergique en coopération avec la protéase lors de l'application de l'agent et étant un polyaminoacide, dans lequel le composant est présent dans l'agent à raison de 0,018 à 0,2 poids, en particulier de 0,04 à 0,1 % en poids et l'agent de lavage ou nettoyant contenant la protéase en une quantité de 2 µg à 20 mg, de préférence de 5 µg à 17,5 mg, en particulier de 20 µg à 15 mg et de manière tout particulièrement préférée de 50 µg à 10 mg par gramme de l'agent.
  2. Procédé selon la revendication 1, caractérisé en ce que l'agent contient en outre un agent tensioactif biologique et/ou un métabolite microbien.
  3. Procédé selon la revendication 1 ou 2, caractérisé en ce que le composant présente une masse moléculaire (MW) de 150 à 5 x 106 daltons, en particulier de 200 à 1 x 106 daltons, de 220 à 0,75 x 106 daltons et en particulier de 400 à 0,5 x 106 daltons, l'agent tensioactif biologique présente une masse moléculaire (MW) de 500 à 3 000 daltons, en particulier de 600 à 2 500 daltons, de 700 à 2 250 daltons et en particulier de 800 à 2 000 daltons et/ou le métabolite microbien présente une masse moléculaire (MW) de 150 à 5 x 106 daltons, en particulier de 200 à 1x106 daltons, de 220 à 0,75 x 106 daltons et en particulier de 400 à 0,5 x 106 daltons.
  4. Procédé selon l'une des revendications 1 à 3, caractérisé en ce que l'agent tensioactif biologique est présent dans l'agent à raison de 0,001 % à 25 % en poids, en particulier de 0,005 à 10 % en poids et/ou le métabolite microbien est présent dans l'agent à raison de 0,018 à 0,2 % en poids, en particulier de 0,04 à 0,1 % en poids.
  5. Procédé selon l'une des revendications 1 à 4, caractérisé en ce que le composant est présent dans l'agent de lavage ou nettoyant à une concentration de 0,00025 à 0,6 % en poids, en particulier de 0,0003 à 0,5 % en poids.
  6. Procédé selon l'une des revendications 1 à 5, caractérisé en ce que la protéase est enrobée d'une substance imperméable à l'enzyme à température ambiante ou en l'absence d'eau dans l'agent de lavage ou de nettoyage.
  7. Procédé selon l'une des revendications 1 à 6, caractérisé en ce que le agent de lavage ou nettoyant est présente
    (a) sous forme solide, en particulier comme une poudre fluide présentant une densité apparente de 300 g/l à 1 200 g/l, en particulier de 500 g/l à 900 g/, ou
    (b) sous forme pâteuse ou liquide, et/ou
    (c) sous forme d'un système monocomposant, ou
    (d) est divisé en plusieurs composants.
  8. Procédé de lavage ou de nettoyage comprenant les étapes
    (a) la fourniture d'une solution de lavage ou nettoyante comprenant un agent de lavage ou nettoyant qui
    i. contient une protéase et
    ii. un composant qui agit sur un pouvoir nettoyant synergique en coopération avec la protéase lors de l'application du agent et qui est un polyaminoacide ;
    (b) la mise en contact d'un textile ou d'une surface dure avec la solution de lavage ou de nettoyage selon (a),
    dans lequel le composant est présent dans l'agent à raison de 0,018 à 0,2 % en poids, en particulier de 0,04 à 0,1 % en poids et l'agent de lavage ou nettoyant contient la protéase en une quantité de 2 µg à 20 mg, de préférence de 5 µg à 17,5 mg, en particulier de 20 µg à 15 mg et de manière tout particulièrement préférée de 50 µg à 10 mg par gramme de l'agent.
  9. Procédé selon l'une des revendications 1 à 8, caractérisé en ce qu'il est mis en oeuvre dans une plage de température de 10 °C à 60 °C, en particulier de 10 °C à 50 °C, de 10 °C à 40 °C, de 10 °C à 30 °C, de 15 °C à 30 °C, de 10 °C à 25 °C et de 15 °C à 25 °C.
  10. Utilisation d'un composant, qui est un polyaminoacide, pour obtenir un pouvoir nettoyant synergique en coopération avec une protéase, dans lequel le composant est présent dans l'agent à raison de 0,018 à 0,2 poids, en particulier de 0,04 à 0,1 % en poids, et l'agent de lavage ou nettoyant contenant la protéase en une quantité de 2 µg à 20 mg, de préférence de 5 µg à 17,5 mg, en particulier de 20 µg à 15 mg et de manière tout particulièrement préférée de 50 µg à 10 mg par gramme de l'agent.
  11. Utilisation selon la revendication 10, caractérisée en ce que l'agent contient en outre un agent tensioactif biologique et/ou un métabolite microbien.
  12. Utilisation selon la revendication 10 ou 11, caractérisée en ce que l'agent tensioactif biologique est présent dans l'agent à raison de 0,001 % à 25 % en poids, en particulier de 0,005 à 10 % en poids et/ou le métabolite microbien est présent dans l'agent à raison de 0,018 à 0,2 % en poids, en particulier de 0,04 à 0,1 % en poids.
  13. Utilisation d'un composant, qui est un polyaminoacide, pour améliorer le pouvoir nettoyant synergique d'une protéase dans un processus de lavage ou de nettoyage, dans lequel le composant est présent dans l'agent à raison de 0,018 à 0,2 poids, en particulier de 0,04 à 0,1 % en poids, et l'agent de lavage ou nettoyant contient la protéase en une quantité de 2 µg à 20 mg, de préférence de 5 µg à 17,5 mg, en particulier de 20 µg à 15 mg et de manière tout particulièrement préférée de 50 µg à 10 mg par gramme de l'agent.
  14. Utilisation selon l'une des revendications 10 à 13, caractérisée en ce que le composant présente une masse moléculaire (MW) de 150 à 5 x 106 daltons, en particulier de 200 à 1 x 106 daltons, de 220 à 0,75 x 106 daltons et en particulier de 400 à 0,5 x 106 daltons, l'agent tensioactif biologique présente une masse moléculaire (MW) de 500 à 3 000 daltons, en particulier de 600 à 2 500 daltons, de 700 à 2 250 daltons et en particulier de 800 à 2 000 daltons et/ou le métabolite microbien présente une masse moléculaire (MW) de 150 à 5 x 106 daltons, en particulier de 200 à 1 x 106 daltons, 220 à 0,75 x 106 daltons et en particulier de 400 à 0,5 x 106 daltons.
EP09780407.4A 2008-08-20 2009-07-10 Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant Active EP2313482B2 (fr)

Priority Applications (5)

Application Number Priority Date Filing Date Title
EP14152970.1A EP2727989B2 (fr) 2008-08-20 2009-07-10 Procédé d'amélioration de la puissance de nettoyage d'un produit de lavage et de nettoyage
EP14152968.5A EP2727988B1 (fr) 2008-08-20 2009-07-10 Procédé d'amélioration de la puissance de nettoyage d'un produit de lavage ou de nettoyage
PL14152970.1T PL2727989T5 (pl) 2008-08-20 2009-07-10 Sposób polepszenia skuteczności czyszczenia środka piorącego lub czyszczącego
PL09780407.4T PL2313482T5 (pl) 2008-08-20 2009-07-10 Sposób polepszenia skuteczności czyszczenia środka piorącego lub czyszczącego
PL14152968T PL2727988T3 (pl) 2008-08-20 2009-07-10 Sposób polepszenia skuteczności czyszczenia środka piorącego lub czyszczącego

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
DE102008038479A DE102008038479A1 (de) 2008-08-20 2008-08-20 Wasch- oder Reinigungsmittel mit gesteigerter Waschkraft
PCT/EP2009/058789 WO2010020475A2 (fr) 2008-08-20 2009-07-10 Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant

Related Child Applications (4)

Application Number Title Priority Date Filing Date
EP14152968.5A Division EP2727988B1 (fr) 2008-08-20 2009-07-10 Procédé d'amélioration de la puissance de nettoyage d'un produit de lavage ou de nettoyage
EP14152968.5A Division-Into EP2727988B1 (fr) 2008-08-20 2009-07-10 Procédé d'amélioration de la puissance de nettoyage d'un produit de lavage ou de nettoyage
EP14152970.1A Division EP2727989B2 (fr) 2008-08-20 2009-07-10 Procédé d'amélioration de la puissance de nettoyage d'un produit de lavage et de nettoyage
EP14152970.1A Division-Into EP2727989B2 (fr) 2008-08-20 2009-07-10 Procédé d'amélioration de la puissance de nettoyage d'un produit de lavage et de nettoyage

Publications (3)

Publication Number Publication Date
EP2313482A2 EP2313482A2 (fr) 2011-04-27
EP2313482B1 true EP2313482B1 (fr) 2019-06-12
EP2313482B2 EP2313482B2 (fr) 2022-07-27

Family

ID=41059950

Family Applications (5)

Application Number Title Priority Date Filing Date
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
EP14152971.9A Ceased EP2727990A3 (fr) 2008-08-20 2009-07-10 Procédé d'amélioration de la puissance de nettoyage d'un produit de lavage ou de nettoyage
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
EP09780407.4A Active EP2313482B2 (fr) 2008-08-20 2009-07-10 Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant
EP09780409.0A Revoked EP2313483B1 (fr) 2008-08-20 2009-07-10 Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant

Family Applications Before (3)

Application Number Title Priority Date Filing Date
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
EP14152971.9A Ceased EP2727990A3 (fr) 2008-08-20 2009-07-10 Procédé d'amélioration de la puissance de nettoyage d'un produit de lavage ou de nettoyage
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

Family Applications After (1)

Application Number Title Priority Date Filing Date
EP09780409.0A Revoked EP2313483B1 (fr) 2008-08-20 2009-07-10 Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant

Country Status (6)

Country Link
US (2) US20110136720A1 (fr)
EP (5) EP2727989B2 (fr)
DE (1) DE102008038479A1 (fr)
ES (3) ES2745761T5 (fr)
PL (3) PL2313482T5 (fr)
WO (2) WO2010020475A2 (fr)

Families Citing this family (31)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE102008038479A1 (de) 2008-08-20 2010-02-25 Henkel Ag & Co. Kgaa Wasch- oder Reinigungsmittel mit gesteigerter Waschkraft
US8816537B2 (en) 2010-01-18 2014-08-26 Toyota Jidosha Kabushiki Kaisha Contactless electric power receiving apparatus, contactless electric power transmitting apparatus, contactless electric power feeding system, and vehicle
ES2609023T3 (es) 2010-07-22 2017-04-18 Unilever N.V. Composiciones detergentes que comprenden biotensioactivo y enzima
DE102012206571A1 (de) 2012-04-20 2013-10-24 Henkel Ag & Co. Kgaa Lagerstabiles Wasch- oder Reinigungsmittel mit gesteigerter Reinigungsleistung
CN113201519A (zh) 2012-05-07 2021-08-03 诺维信公司 具有黄原胶降解活性的多肽以及编码其的核苷酸
DE102012220103A1 (de) 2012-11-05 2014-05-08 Henkel Ag & Co. Kgaa Die Primärwaschkraft verbessernde Tensidkombination
WO2014200657A1 (fr) 2013-06-13 2014-12-18 Danisco Us Inc. Alpha-amylase provenant destreptomyces xiamenensis
WO2014200658A1 (fr) 2013-06-13 2014-12-18 Danisco Us Inc. Alpha-amylase issue de promicromonospora vindobonensis
WO2014200656A1 (fr) 2013-06-13 2014-12-18 Danisco Us Inc. Alpha-amylase provenant de streptomyces umbrinus
WO2014204596A1 (fr) 2013-06-17 2014-12-24 Danisco Us Inc. Alpha-amylase issue d'un membre de la famille des bacillaceae
DE102013215824A1 (de) * 2013-08-09 2015-02-12 Henkel Ag & Co. Kgaa Wasch- oder Reinigungsmittel mit immobilisierter Enzymkomponente
US20160186102A1 (en) 2013-10-03 2016-06-30 Danisco Us Inc. Alpha-amylases from exiguobacterium, and methods of use, thereof
EP3060659B1 (fr) 2013-10-03 2019-05-29 Danisco US Inc. Alpha-amylases de exiguobacterium, methodes et utilisation
JP2016538412A (ja) 2013-11-11 2016-12-08 エコラボ ユーエスエー インコーポレイティド 強化されたスケール制御及び汚れ分散性を有する高アルカリ性物品洗浄洗剤
KR102131173B1 (ko) 2013-11-11 2020-07-07 에코랍 유에스에이 인코퍼레이티드 다용도의 효소 세정제 및 사용 용액을 안정화시키는 방법
MX2016006489A (es) 2013-11-20 2016-08-03 Danisco Us Inc Alfa-amilasas variantes que tienen susceptibilidad reducida a la escision por proteasas y metodos de uso.
EP3105256A1 (fr) * 2014-02-14 2016-12-21 E. I. du Pont de Nemours and Company Poly-alpha-1,3-1,6-glucanes utilisables en vue de la modification de la viscosité
EP3070155A1 (fr) * 2015-03-18 2016-09-21 Evonik Degussa GmbH Composition comprenant des peptidases et biotenseurs
DE102015211640B4 (de) 2015-06-24 2017-09-21 Organon eG Frankfurt Stoff zum mikrobiologischen Behandeln von Gegenständen oder deren Oberflächen
AR105803A1 (es) * 2015-08-28 2017-11-08 Unilever Nv Composiciones de lavado mejoradas
US10183087B2 (en) * 2015-11-10 2019-01-22 American Sterilizer Company Cleaning and disinfecting composition
CA3018866C (fr) 2016-03-31 2024-03-26 Gojo Industries, Inc. Composition de desinfectant comprenant un principe actif probiotique/prebiotique
WO2017173240A1 (fr) 2016-03-31 2017-10-05 Gojo Industries, Inc. Composition nettoyante stimulant les peptides antimicrobiens
WO2017173190A2 (fr) 2016-04-01 2017-10-05 Danisco Us Inc. Alpha-amylases, compositions et procédés
WO2017173324A2 (fr) 2016-04-01 2017-10-05 Danisco Us Inc. Alpha-amylases, compositions et procédés
CA3043748A1 (fr) 2016-11-23 2018-05-31 Gojo Industries, Inc. Composition desinfectante comprenant une substance active probiotique/prebiotique
CN110072985B (zh) * 2016-12-15 2021-04-20 高露洁-棕榄公司 在精细织物液体洗涤剂中使用柠檬酸和亚氨基二琥珀酸盐的织物色彩保护
EP3658658A4 (fr) * 2017-07-24 2021-04-28 Rhodia Operations Composition détergente contenant des enzymes
DE102018214093A1 (de) 2018-08-21 2020-02-27 Henkel Ag & Co. Kgaa Wasch- oder Reinigungsmittel mit gesteigerter Proteaseleistung
BR112022005889A2 (pt) * 2019-09-29 2022-06-21 Novozymes As Usos de desoxirribonuclease em composição detergente
WO2023275191A1 (fr) 2021-06-29 2023-01-05 Christeyns Additif amélioré contenant une enzyme et formulations de lessive détergente

Citations (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US1011108A (en) 1909-09-23 1911-12-05 Christian M Bowman Attachment for engravers' blocks.
WO2002042408A2 (fr) 2000-11-27 2002-05-30 The Procter & Gamble Company Produits detergents, procedes et fabrication
US6944108B2 (en) 2002-02-07 2005-09-13 Shinano Kenshi Kabushiki Kaisha Method for controlling the rotation of optical disk based on disk shapes
WO2009087526A1 (fr) 2008-01-04 2009-07-16 The Procter & Gamble Company Utilisation d'une cellulase pour conférer des avantages d'élimination des salissures à du coton pendant un procédé de blanchissage ultérieur
EP2100947A1 (fr) 2008-03-14 2009-09-16 The Procter and Gamble Company Composition détergente de lave-vaisselle automatique
EP2100948A1 (fr) 2008-03-14 2009-09-16 The Procter and Gamble Company Composition détergente de lave-vaisselle automatique
WO2009112992A1 (fr) 2008-03-14 2009-09-17 The Procter & Gamble Company Composition détergente pour lave-vaisselle

Family Cites Families (71)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US3948838A (en) * 1968-07-25 1976-04-06 Burlington Industries, Inc. Soil release composition
DE1942236A1 (de) * 1969-08-20 1971-03-04 Henkel & Cie Gmbh Eiweissloesende Wasch-,Waschhilfs- und Reinigungsmittel
DE1964792A1 (de) * 1969-12-24 1971-07-01 Henkel & Cie Gmbh Eiweissloesende Wasch-,Waschhilfs- und Reinigungsmittel
JPS5014651B1 (fr) * 1969-12-30 1975-05-29
DE2038103A1 (de) * 1970-07-31 1972-02-10 Henkel & Cie Gmbh Waessrige Reinigungsmittelkonzentrate mit einem Gehalt an stabilisierten Enzymen
CH540335A (de) * 1970-09-28 1973-08-15 Kronwitter & Co Flüssiges biologisches Wasch-, Reinigungs- und Geschirrspülmittel
AT330930B (de) 1973-04-13 1976-07-26 Henkel & Cie Gmbh Verfahren zur herstellung von festen, schuttfahigen wasch- oder reinigungsmitteln mit einem gehalt an calcium bindenden substanzen
DE2709476A1 (de) * 1976-03-08 1977-09-15 Procter & Gamble Europ Fluessiges, enzymhaltiges wasch- und reinigungsmittel
US4305837A (en) 1980-10-30 1981-12-15 The Procter & Gamble Company Stabilized aqueous enzyme composition
CA1334389C (fr) * 1986-03-26 1995-02-14 Ernest H. Brumbaugh Composition anti-taches pour lave-vaisselle
JPS6363796A (ja) 1986-09-03 1988-03-22 花王株式会社 洗浄剤組成物
JP2562624B2 (ja) * 1986-11-07 1996-12-11 昭和電工株式会社 水溶性マイクロカプセルおよび液体洗剤組成物
JPS63183999A (ja) 1987-01-26 1988-07-29 花王株式会社 洗浄剤組成物
DE3723873A1 (de) 1987-07-18 1989-01-26 Henkel Kgaa Verwendung von hydroxyalkylpolyethylenglykolethern in klarspuelmitteln fuer die maschinelle geschirreinigung
US6287841B1 (en) 1988-02-11 2001-09-11 Genencor International, Inc. High alkaline serine protease
DE3942617A1 (de) * 1989-12-22 1991-06-27 Henkel Kgaa Stabilisatoren fuer waessrige fluessigwaschmittel
US5308530A (en) 1990-11-21 1994-05-03 Lever Brothers Company, Division Of Conopco, Inc. Detergent compositions containing polycarboxylates and calcium-sensitive enzymes
US5340735A (en) 1991-05-29 1994-08-23 Cognis, Inc. Bacillus lentus alkaline protease variants with increased stability
US5545344A (en) * 1991-05-31 1996-08-13 Colgate-Palmolive Co. Nonaqueous liquid, improved automatic dishwashing composition containing enzymes
US5468411A (en) * 1991-05-31 1995-11-21 Colgate Palmolive Co. Powdered automatic dishwashing composition containing enzymes
US5879920A (en) * 1991-10-07 1999-03-09 Genencor International, Inc. Coated enzyme-containing granule
US5559089A (en) * 1992-03-12 1996-09-24 The Procter & Gamble Company Low-dosage automatic dishwashing detergent with monopersulfate and enzymes
EP0636170B1 (fr) * 1992-04-13 1997-08-06 The Procter & Gamble Company Composition thixotrope liquide contenant des enzymes, pour le lavage automatique de la vaisselle
AU669900B2 (en) * 1992-07-20 1996-06-27 Colgate-Palmolive Company, The Stabilized built aqueous liquid softergent compositions
DE69217934T2 (de) * 1992-08-14 1997-09-04 Procter & Gamble Peptidaldehydhaltige flüssige Waschmittel
WO1994025556A1 (fr) 1993-04-27 1994-11-10 The Procter & Gamble Company Compositions de detergent liquide ou granulaire pour lave-vaisselle
US5691295A (en) * 1995-01-17 1997-11-25 Cognis Gesellschaft Fuer Biotechnologie Mbh Detergent compositions
JPH09512298A (ja) * 1994-04-22 1997-12-09 ザ、プロクター、エンド、ギャンブル、カンパニー アミラーゼを含有する粒状洗剤組成物
WO1996000277A1 (fr) * 1994-06-23 1996-01-04 Unilever N.V. Compositions pour le lavage de la vaisselle
JP2849041B2 (ja) 1994-06-30 1999-01-20 ザ、プロクター、エンド、ギャンブル、カンパニー 洗剤組成物
US5858117A (en) * 1994-08-31 1999-01-12 Ecolab Inc. Proteolytic enzyme cleaner
GB9501112D0 (en) * 1995-01-20 1995-03-08 Procter & Gamble Detergent compositions comprising stabilised polyamino acid compounds
US5576282A (en) 1995-09-11 1996-11-19 The Procter & Gamble Company Color-safe bleach boosters, compositions and laundry methods employing same
US5945394A (en) * 1995-09-18 1999-08-31 Stepan Company Heavy duty liquid detergent compositions comprising salts of α-sulfonated fatty acid methyl esters and use of α-sulphonated fatty acid salts to inhibit redeposition of soil on fabric
US6165970A (en) * 1996-03-29 2000-12-26 The Procter & Gamble Company Detergent composition comprising acrylic acid-based polymer and amino tricarboxylic acid-based compound
AU724338B2 (en) * 1996-04-24 2000-09-21 Unilever Plc Synthetic bar composition comprising alkoxylated surfactants
US6121226A (en) * 1996-05-03 2000-09-19 The Procter & Gamble Company Compositions comprising cotton soil release polymers and protease enzymes
US5858948A (en) * 1996-05-03 1999-01-12 Procter & Gamble Company Liquid laundry detergent compositions comprising cotton soil release polymers and protease enzymes
CN1238001A (zh) * 1996-09-24 1999-12-08 普罗格特-甘布尔公司 含有蛋白水解酶、肽醛和钙离子的液体洗涤剂
US5919697A (en) * 1996-10-18 1999-07-06 Novo Nordisk A/S Color clarification methods
US6436342B1 (en) * 1996-11-13 2002-08-20 The Procter & Gamble Company Sprayable disinfecting compositions and processes for disinfecting surfaces therewith
US6218351B1 (en) * 1998-03-06 2001-04-17 The Procter & Gamble Compnay Bleach compositions
CN1285868A (zh) 1998-01-13 2001-02-28 宝洁公司 具有改善的溶解作用的颗粒组合物
JP3403332B2 (ja) * 1998-05-12 2003-05-06 花王株式会社 洗浄剤組成物
US6268329B1 (en) * 1998-06-30 2001-07-31 Nouozymes A/S Enzyme containing granule
ATE368765T1 (de) * 1998-09-30 2007-08-15 Unilever Nv Wäschebehandlung
ES2243163T3 (es) 1999-03-17 2005-12-01 Kao Corporation Composicion detergente.
MY120271A (en) * 1999-05-19 2005-09-30 Colgate Palmolive Co Laundry detergent composition containing high level of protease enzyme
GB9914622D0 (en) * 1999-06-23 1999-08-25 Reckitt & Colman Inc Improvements in or relating to organic compositions
US6331512B1 (en) * 1999-09-29 2001-12-18 Amway Corporation Phosphate-free automatic dishwashing detergent
DE19953057A1 (de) 1999-11-03 2001-05-10 Henkel Kgaa Enzymhaltige höherviskose Flüssigwaschmittel
DE10027634A1 (de) * 2000-06-06 2001-12-13 Basf Ag Verwendung von kationisch modifizierten, teilchenförmigen, hydrophoben Polymeren als Zusatz zu Spül- oder Pflegemitteln für Textilien und als Zusatz zu Waschmitteln
US20020183226A1 (en) * 2001-02-28 2002-12-05 Chandrika Kasturi Liquid detergent composition exhibiting enhanced alpha-amylase enzyme stability
ES2295359T3 (es) * 2001-06-22 2008-04-16 Genencor International, Inc. Granulos de alta resistencia al impacto.
JP2003013093A (ja) * 2001-06-27 2003-01-15 Saraya Kk 低泡性洗浄剤組成物
DE10131441A1 (de) 2001-06-29 2003-01-30 Henkel Kgaa Eine neue Gruppe von alpha-Amylasen sowie ein Verfahren zur Identifizierung und Gewinnung neuer alpha-Amylasen
DE10163748A1 (de) 2001-12-21 2003-07-17 Henkel Kgaa Neue Glykosylhydrolasen
CA2795814A1 (fr) 2001-12-31 2003-07-17 Genencor International, Inc. Proteases produisant une reponse immunogene modifiee et leurs procedes de production et d'utilisation
US7557076B2 (en) 2002-06-06 2009-07-07 The Procter & Gamble Company Organic catalyst with enhanced enzyme compatibility
CA2502303C (fr) * 2002-11-04 2010-08-17 The Procter & Gamble Company Detergent a lessive liquide
ES2283997T3 (es) 2003-03-24 2007-11-01 Ciba Specialty Chemicals Holding Inc. Composiciones detergentes.
US7300913B2 (en) * 2004-10-15 2007-11-27 Naturell Clean, Inc. Systems and methods for cleaning materials
US7556654B1 (en) * 2004-10-15 2009-07-07 Naturell Methods for cleaning materials
DE102006022224A1 (de) 2006-05-11 2007-11-15 Henkel Kgaa Subtilisin aus Bacillus pumilus und Wasch- und Reinigungsmittel enthaltend dieses neue Subtilisin
EP1867708B1 (fr) 2006-06-16 2017-05-03 The Procter and Gamble Company Compositions de lavage
DE102007029643A1 (de) 2006-09-08 2009-01-15 Henkel Ag & Co. Kgaa Reinigungsmittel
DE102007003143A1 (de) 2007-01-16 2008-07-17 Henkel Kgaa Neue Alkalische Protease aus Bacillus gibsonii und Wasch- und Reinigungsmittel enthaltend diese neue Alkalische Protease
DE102007038031A1 (de) 2007-08-10 2009-06-04 Henkel Ag & Co. Kgaa Mittel enthaltend Proteasen
EP2083067A1 (fr) * 2008-01-25 2009-07-29 Basf Aktiengesellschaft Utilisation de complexants organiques et/ou de liaisons contenant des groupes d'acides de carbone polymères dans une composition de produit de lavage ou de nettoyage
DE102008038479A1 (de) 2008-08-20 2010-02-25 Henkel Ag & Co. Kgaa Wasch- oder Reinigungsmittel mit gesteigerter Waschkraft
WO2019048486A1 (fr) 2017-09-05 2019-03-14 Henkel Ag & Co. Kgaa Variantes de protéases à performances améliorées

Patent Citations (9)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US1011108A (en) 1909-09-23 1911-12-05 Christian M Bowman Attachment for engravers' blocks.
WO2002042408A2 (fr) 2000-11-27 2002-05-30 The Procter & Gamble Company Produits detergents, procedes et fabrication
US6944108B2 (en) 2002-02-07 2005-09-13 Shinano Kenshi Kabushiki Kaisha Method for controlling the rotation of optical disk based on disk shapes
WO2009087526A1 (fr) 2008-01-04 2009-07-16 The Procter & Gamble Company Utilisation d'une cellulase pour conférer des avantages d'élimination des salissures à du coton pendant un procédé de blanchissage ultérieur
EP2100947A1 (fr) 2008-03-14 2009-09-16 The Procter and Gamble Company Composition détergente de lave-vaisselle automatique
EP2100948A1 (fr) 2008-03-14 2009-09-16 The Procter and Gamble Company Composition détergente de lave-vaisselle automatique
WO2009112994A1 (fr) 2008-03-14 2009-09-17 The Procter & Gamble Company Composition détergente pour lave-vaisselle
WO2009112992A1 (fr) 2008-03-14 2009-09-17 The Procter & Gamble Company Composition détergente pour lave-vaisselle
WO2009112993A1 (fr) 2008-03-14 2009-09-17 The Procter & Gamble Company Composition détergente pour lave-vaisselle

Non-Patent Citations (2)

* Cited by examiner, † Cited by third party
Title
HERMANN G. HAUTHAL, G. WAGNER: "HOUSEHOLD CLEANING, CARE AND MAINTENANCE PRODUCTS", 2003, VERLAG FUR CHEMISCHE INDUSTRIE, article "2.4 Enzymes", pages: 1pp, 2, 7-12, 80, XP055676344
STRAATHOF A J J, ADLERCREUTZ P.: "APPLIED BIOCATALYSIS", 2005, HARWOOD ACADEMIC PRESS, ISBN: 90-5823-024-4, article TRAMPER ET AL.: "Enzymes as processing aids and final products", pages: 62, 75 - 81, XP055257798

Also Published As

Publication number Publication date
EP2727989B2 (fr) 2022-12-21
EP2727988B1 (fr) 2019-09-04
WO2010020476A2 (fr) 2010-02-25
PL2313482T3 (pl) 2019-11-29
US20110201536A1 (en) 2011-08-18
ES2753240T3 (es) 2020-04-07
ES2745761T5 (es) 2023-03-09
EP2313483B1 (fr) 2018-06-20
PL2313482T5 (pl) 2023-02-27
EP2727989A3 (fr) 2016-03-16
ES2745761T3 (es) 2020-03-03
ES2744829T3 (es) 2020-02-26
EP2727989A2 (fr) 2014-05-07
ES2744829T5 (es) 2022-10-19
DE102008038479A1 (de) 2010-02-25
WO2010020475A2 (fr) 2010-02-25
WO2010020475A3 (fr) 2010-06-17
EP2727988A3 (fr) 2016-03-16
EP2727990A3 (fr) 2016-03-16
PL2727988T3 (pl) 2020-02-28
EP2313483A2 (fr) 2011-04-27
PL2727989T5 (pl) 2023-03-27
WO2010020476A3 (fr) 2010-06-17
EP2727990A2 (fr) 2014-05-07
EP2727988A2 (fr) 2014-05-07
EP2313482B2 (fr) 2022-07-27
PL2727989T3 (pl) 2019-12-31
EP2727989B1 (fr) 2019-06-26
US20110136720A1 (en) 2011-06-09
EP2313482A2 (fr) 2011-04-27

Similar Documents

Publication Publication Date Title
EP2313482B1 (fr) Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant
EP2115111B1 (fr) Dérivés de benzophénone ou d'anilide d'acide benzoïque portant des groupes carboxyle servant de stabilisateurs d'enzymes
EP2188360A1 (fr) Composés polycycliques comme stabilisateurs d'enzymes
WO2012019844A2 (fr) Préparation tensioactive liquide stabilisée contenant une enzyme
EP2220204A1 (fr) Détergents contenant des enzymes stabilisées
WO2013037609A2 (fr) Procédé d'adaptation d'une enzyme hydrolytique à un constituant stabilisant ladite enzyme hydrolytique
JP2001522784A (ja) ラッカーゼの抗菌活性
WO2006131503A2 (fr) Detergents comprenant des systemes d'adjuvant et de blanchiment enzymatiques
DE102013202772A1 (de) Wasch- oder Reinigungsmittel mit verbesserter Reinigungsleistung
EP2655587B1 (fr) Préparation tensioactive liquide contenant de la lipase et du phophonate
EP2640818B1 (fr) Préparation liquide d'agents tensioactifs stabilisée et contenant des enzymes
WO2023232193A1 (fr) Détergents et produits de nettoyage à stabilité enzymatique améliorée
WO2023232194A1 (fr) Détergents et agents de nettoyage à stabilité enzymatique améliorée
WO2023232192A1 (fr) Produits de lavage et de nettoyage à stabilité enzymatique améliorée
EP2598622A2 (fr) Préparation tensioactive liquide stabilisée contenant une enzyme

Legal Events

Date Code Title Description
PUAI Public reference made under article 153(3) epc to a published international application that has entered the european phase

Free format text: ORIGINAL CODE: 0009012

17P Request for examination filed

Effective date: 20110118

AK Designated contracting states

Kind code of ref document: A2

Designated state(s): AT BE BG CH CY CZ DE DK EE ES FI FR GB GR HR HU IE IS IT LI LT LU LV MC MK MT NL NO PL PT RO SE SI SK SM TR

AX Request for extension of the european patent

Extension state: AL BA RS

DAX Request for extension of the european patent (deleted)
17Q First examination report despatched

Effective date: 20120202

STAA Information on the status of an ep patent application or granted ep patent

Free format text: STATUS: EXAMINATION IS IN PROGRESS

GRAP Despatch of communication of intention to grant a patent

Free format text: ORIGINAL CODE: EPIDOSNIGR1

STAA Information on the status of an ep patent application or granted ep patent

Free format text: STATUS: GRANT OF PATENT IS INTENDED

INTG Intention to grant announced

Effective date: 20190122

GRAS Grant fee paid

Free format text: ORIGINAL CODE: EPIDOSNIGR3

GRAA (expected) grant

Free format text: ORIGINAL CODE: 0009210

STAA Information on the status of an ep patent application or granted ep patent

Free format text: STATUS: THE PATENT HAS BEEN GRANTED

AK Designated contracting states

Kind code of ref document: B1

Designated state(s): AT BE BG CH CY CZ DE DK EE ES FI FR GB GR HR HU IE IS IT LI LT LU LV MC MK MT NL NO PL PT RO SE SI SK SM TR

REG Reference to a national code

Ref country code: GB

Ref legal event code: FG4D

Free format text: NOT ENGLISH

REG Reference to a national code

Ref country code: CH

Ref legal event code: EP

REG Reference to a national code

Ref country code: AT

Ref legal event code: REF

Ref document number: 1142561

Country of ref document: AT

Kind code of ref document: T

Effective date: 20190615

REG Reference to a national code

Ref country code: DE

Ref legal event code: R096

Ref document number: 502009015829

Country of ref document: DE

REG Reference to a national code

Ref country code: IE

Ref legal event code: FG4D

Free format text: LANGUAGE OF EP DOCUMENT: GERMAN

REG Reference to a national code

Ref country code: NL

Ref legal event code: MP

Effective date: 20190612

REG Reference to a national code

Ref country code: LT

Ref legal event code: MG4D

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: FI

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190612

Ref country code: NO

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190912

Ref country code: HR

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190612

Ref country code: LT

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190612

Ref country code: SE

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190612

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: LV

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190612

Ref country code: BG

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190912

Ref country code: GR

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190913

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: RO

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190612

Ref country code: CZ

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190612

Ref country code: PT

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20191014

Ref country code: SK

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190612

Ref country code: NL

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190612

Ref country code: EE

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190612

REG Reference to a national code

Ref country code: ES

Ref legal event code: FG2A

Ref document number: 2744829

Country of ref document: ES

Kind code of ref document: T3

Effective date: 20200226

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: SM

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190612

Ref country code: IS

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20191012

REG Reference to a national code

Ref country code: CH

Ref legal event code: PL

REG Reference to a national code

Ref country code: DE

Ref legal event code: R026

Ref document number: 502009015829

Country of ref document: DE

PLBI Opposition filed

Free format text: ORIGINAL CODE: 0009260

PLAX Notice of opposition and request to file observation + time limit sent

Free format text: ORIGINAL CODE: EPIDOSNOBS2

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: MC

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190612

Ref country code: TR

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190612

REG Reference to a national code

Ref country code: BE

Ref legal event code: MM

Effective date: 20190731

26 Opposition filed

Opponent name: THE PROCTER & GAMBLE COMPANY

Effective date: 20200312

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: DK

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190612

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: LI

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20190731

Ref country code: CH

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20190731

Ref country code: LU

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20190710

Ref country code: IS

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20200224

Ref country code: BE

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20190731

Ref country code: SI

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190612

PLBB Reply of patent proprietor to notice(s) of opposition received

Free format text: ORIGINAL CODE: EPIDOSNOBS3

PG2D Information on lapse in contracting state deleted

Ref country code: IS

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: IE

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20190710

Ref country code: IS

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20191112

REG Reference to a national code

Ref country code: AT

Ref legal event code: MM01

Ref document number: 1142561

Country of ref document: AT

Kind code of ref document: T

Effective date: 20190710

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: AT

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20190710

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: CY

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190612

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: MT

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190612

Ref country code: HU

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT; INVALID AB INITIO

Effective date: 20090710

PLAB Opposition data, opponent's data or that of the opponent's representative modified

Free format text: ORIGINAL CODE: 0009299OPPO

R26 Opposition filed (corrected)

Opponent name: THE PROCTER & GAMBLE COMPANY

Effective date: 20200312

APBM Appeal reference recorded

Free format text: ORIGINAL CODE: EPIDOSNREFNO

APBP Date of receipt of notice of appeal recorded

Free format text: ORIGINAL CODE: EPIDOSNNOA2O

APAH Appeal reference modified

Free format text: ORIGINAL CODE: EPIDOSCREFNO

APBU Appeal procedure closed

Free format text: ORIGINAL CODE: EPIDOSNNOA9O

REG Reference to a national code

Ref country code: CH

Ref legal event code: PK

Free format text: BERICHTIGUNGEN

RIC2 Information provided on ipc code assigned after grant

Ipc: C11D 3/37 20060101ALI20220510BHEP

Ipc: C11D 3/386 20060101AFI20220510BHEP

PUAH Patent maintained in amended form

Free format text: ORIGINAL CODE: 0009272

STAA Information on the status of an ep patent application or granted ep patent

Free format text: STATUS: PATENT MAINTAINED AS AMENDED

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: MK

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20190612

REG Reference to a national code

Ref country code: FR

Ref legal event code: PLFP

Year of fee payment: 14

GRAT Correction requested after decision to grant or after decision to maintain patent in amended form

Free format text: ORIGINAL CODE: EPIDOSNCDEC

27A Patent maintained in amended form

Effective date: 20220727

AK Designated contracting states

Kind code of ref document: B2

Designated state(s): AT BE BG CH CY CZ DE DK EE ES FI FR GB GR HR HU IE IS IT LI LT LU LV MC MK MT NL NO PL PT RO SE SI SK SM TR

REG Reference to a national code

Ref country code: DE

Ref legal event code: R102

Ref document number: 502009015829

Country of ref document: DE

REG Reference to a national code

Ref country code: ES

Ref legal event code: DC2A

Ref document number: 2744829

Country of ref document: ES

Kind code of ref document: T5

Effective date: 20221019

P01 Opt-out of the competence of the unified patent court (upc) registered

Effective date: 20230705

PGFP Annual fee paid to national office [announced via postgrant information from national office to epo]

Ref country code: PL

Payment date: 20230630

Year of fee payment: 15

PGFP Annual fee paid to national office [announced via postgrant information from national office to epo]

Ref country code: IT

Payment date: 20230724

Year of fee payment: 15

Ref country code: GB

Payment date: 20230720

Year of fee payment: 15

Ref country code: ES

Payment date: 20230926

Year of fee payment: 15

PGFP Annual fee paid to national office [announced via postgrant information from national office to epo]

Ref country code: FR

Payment date: 20230725

Year of fee payment: 15

Ref country code: DE

Payment date: 20230719

Year of fee payment: 15