EP2727989B1 - Procédé d'amélioration de la puissance de nettoyage d'un produit de lavage et de nettoyage - Google Patents
Procédé d'amélioration de la puissance de nettoyage d'un produit de lavage et de nettoyage Download PDFInfo
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- EP2727989B1 EP2727989B1 EP14152970.1A EP14152970A EP2727989B1 EP 2727989 B1 EP2727989 B1 EP 2727989B1 EP 14152970 A EP14152970 A EP 14152970A EP 2727989 B1 EP2727989 B1 EP 2727989B1
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- washing
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- protease
- agent
- daltons
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- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
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- C11D3/2003—Alcohols; Phenols
- C11D3/2041—Dihydric alcohols
- C11D3/2044—Dihydric alcohols linear
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- C11D3/22—Carbohydrates or derivatives thereof
- C11D3/222—Natural or synthetic polysaccharides, e.g. cellulose, starch, gum, alginic acid or cyclodextrin
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- C11D3/3719—Polyamides or polyimides
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- C11D3/3723—Polyamines or polyalkyleneimines
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- C11D3/3746—Macromolecular compounds obtained by reactions only involving carbon-to-carbon unsaturated bonds
- C11D3/3753—Polyvinylalcohol; Ethers or esters thereof
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- C11D3/3757—(Co)polymerised carboxylic acids, -anhydrides, -esters in solid and liquid compositions
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- C11D3/3769—(Co)polymerised monomers containing nitrogen, e.g. carbonamides, nitriles or amines
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- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
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- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/381—Microorganisms
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- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
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- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
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- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
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- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
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- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
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- C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
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- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
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- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38645—Preparations containing enzymes, e.g. protease or amylase containing cellulase
Definitions
- the present application is directed to methods of enhancing the activity of a protease in a detergent or cleaning agent 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, including, in particular, the subtilisins formed and secreted by Bacillus species as the most important group within the subtilases.
- subtilisin-type proteases preferably used in detergents and cleaners are the subtilisins BPN 'and Carlsberg, the protease PB92, the subtilisins 147 and 309, the alkaline protease from Bacillus lentus, in particular from Bacillus lentus DSM 5483, subtilisin DY and the subtilases, but not the subtilisins in the narrower sense attributable enzymes thermitase, proteinase K and the proteases TW3 and TW7.
- proteases are, for example, those under the trade names Durazym®, Relase®, Everlase®, Nafizym, Natalase®, Kannase® and Ovozyme® from Novozymes, which are available under the trade names, Purafect®, Purafect® OxP, Purafect® Prime and Properase ® from Genencor, sold under the trade name Protosol® by Advanced Biochemicals Ltd., Thane, India, under the trade name Wuxi® by Wuxi Snyder Bioproducts Ltd., China, under the trade names Proleather® and Protease P From Amano Pharmaceuticals Ltd., Nagoya, Japan, and that available under the name Proteinase K-16 from Kao Corp., Tokyo, Japan.
- a disadvantage of 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.
- the present invention is therefore based on the object to improve the cleaning performance (washing power) of detergents or cleaning agents 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 washing or cleaning agents or the wash liquor formed by the washing or cleaning agents with regard to soiling which are sensitive to degradation by proteases, and in particular in a temperature range between 10 ° C and 50 ° C, between 10 ° C and 40 ° C and preferably between 10 ° C and 30 ° C and 10 ° C and 25 ° C.
- the invention thus relates to a method for increasing the activity of a protease in a washing or cleaning agent, characterized in that the washing or Detergent is added to a microbial metabolite which, in conjunction with the protease, provides a synergistic cleaning performance using the agent, the microbial metabolite being selected from the group consisting of 2,3-butanediol, pyruvate, propionate, butyrate and levan.
- cleaning performance of detergents or cleaners is significantly improved if these agents contain at least one protease (also referred to herein as component (a) or hydrolytic enzyme (a)) with a microbial metabolite , selected from the group consisting of 2,3-butanediol, pyruvate, propionate and levan (also referred to herein as component (b)).
- protease also referred to herein as component (a) or hydrolytic enzyme (a)
- a microbial metabolite selected from the group consisting of 2,3-butanediol, pyruvate, propionate and levan
- 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), a synergistic effect, i. a better performance compared to the individual performances of the respective component in one-component systems (ie detergents containing only the proteolytic enzyme or component (b) respectively) and also to the sum of the individual performances of the components (a ) and (b), ie the sum of two one-component systems each with 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 washing or cleaning agent, for example, in a washing machine or in another 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 which can be used are the ⁇ -amylases from Bacillus licheniformis, B. amyloliquefaciens or B. stearothermophilus and their further developments improved for use in detergents or cleaners.
- the B. licheniformis enzyme is available from Novozymes under the name Termamyl® and from Genencor under the name Purastar®ST. Further development products of this ⁇ -amylase are available from Novozymes under the trade 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 B. stearothermophilus ⁇ -amylase the name BSG® and Novamyl®, also from the company Novozymes. Furthermore, for this purpose, the ⁇ -amylase from Bacillus sp. A 7-7 (DSM 12368) and the cyclodextrin glucanotransferase (CGTase) from B. agaradherens (DSM 9948).
- amylolytic enzymes 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.
- Examples of useful lipases or cutinases which are contained in particular because of their triglyceride-cleaving activities, but also to generate from suitable precursors in situ peracids, are those originally from Humicola lanuginosa (Thermomyces lanuginosus) available, or further developed lipases, especially 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 may be present as pure enzymes, as enzyme preparations or in the form of mixtures in which the individual components advantageously complement each other in terms of their various performance aspects.
- 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 to softening
- 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.
- Other usable 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.
- the enzymes are from 0.001 to 5% by weight, more preferably from 0.01 to 5% by weight, even more preferably from 0.05 to 4% by weight and most preferably from 0.075 to 3.5% by weight. % contained in these agents, wherein each enzyme contained can be present in the stated amounts.
- the protein concentration can be determined by known methods, for example the BCA method (bicinchoninic acid, 2,2'-biquinolyl-4,4'-dicarboxylic acid) or the biuret method ( Gornall AG, CS Bardawill and MM David, J. Biol. Chem., 177 (1948), pp. 751-766 ).
- BCA method bicinchoninic acid, 2,2'-biquinolyl-4,4'-dicarboxylic acid
- the biuret method Gornall AG, CS Bardawill and MM David, J. Biol. Chem., 177 (1948), pp. 751-766 .
- the 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 acting synergistically in conjunction with the protease (a) when the agent is used, selected from a microbial metabolite (iii).
- the agent may contain, in addition to the microbial metabolite (iii), an (i) amino acid or polyamino acid or its derivative and / or a (ii) biosurfactant.
- the substances mentioned under (i) are preferably amino acids or polymers thereof or their salts or derivatives thereof, wherein both stereoisomers of the amino acids can be used, ie both D and L amino acids, also in combination, or corresponding Polymers or derivatives.
- a polyamino acid in this regard comprises at least two amino acid residues. Particularly preferred are glutamate, polyglutamate, lysine, glutamine, histidine, phenylalanine, tyrosine, alanine, leucine, isoleucine, methionine, proline, valine, glutamine, cysteine, tryptophan, threonine, serine, glycine, aspartate and asparagine.
- Particularly preferred are poly-glutamic acid, including ⁇ -D-polyglutamic acid, L-polyglutamic acid and DL-polyglutamic acid, poly-aspartic acid, including ⁇ -D-polyaspartic acid and L-polyaspartic acid, poly-glutamine, including ⁇ -D-polyglutamine, L Polyglutamine and DL-polyglutamine, as well as poly-asparagine, including ⁇ -D-polyasparagine and L-polyasparagine.
- An example of a particularly preferred polyaspartic acid is the compound available under the trade name Baypure DS 100 solid G (Lanxess company).
- biosurfactants 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- ⁇ -resp.
- D- ⁇ -amino acids however, also ⁇ , ⁇ or ⁇ -amino acids can be present, both in D and in L configuration.
- the peptide chains may also have further chemical modifications, in particular they may be glycosylated, hydrolyzed, N-methylated or N-formylated. Frequently occurring structural elements are also thiazoline and / or oxazoline rings in different oxidation states.
- Particularly preferred biosurfactants according to the invention are anionic lipopeptides and more preferably surfactin-like or lichenigen-like substances or surfactin or lichenin itself.
- Surfactin-like or lichenigen-like substances are understood as meaning those which have either a similar chemical structure as surfactin or lichenyin and / or have a comparable with surfactin or Lichenysin effect.
- Surfactin can be described in particular by the following formula: fatty acid-cyclo- [Glu-Leu-Leu-Val-Asp-Leu-Leu]. The structure of surfactin is also in FIG. 1 specified.
- Lichenysine can be described in particular by the following formula: fatty acid-cyclo- [Gln-Leu-Leu-Val-Asp-Leu-Ile]. Because Lichenycin is often called Lichenisin is expressly noted at this point that according to the invention with the name Lichenysin both names 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 used according to the invention are 2,3-butanediol, pyruvate, propionate, butyrate ,.
- microbial metabolites which may be mentioned are acetate, lactate, 2-methylpropionate, 3-methylbutyrate, ⁇ -ketogluterate, acetoin, propanediol, glycol, glycerol, citrate, formate, ethanol, methanol or butanol.
- component (b) is added to the detergent or cleaning agent as a separate single substance, i. not as a component of another ingredient of the washing or cleaning agent.
- component (b) is therefore free in the detergent, i. it is distributed in this and distributed as homogeneously as possible.
- component (b) is preferably dissolved or dispersed in them.
- the washing or cleaning agent particularly preferably does not contain component (b) as part of the dosage form of the hydrolytic enzyme (a), in particular not as a constituent of an enzyme granulate.
- liquid or gel-shaped i. non-solid detergents or cleaners.
- a preferred liquid detergent for such a washing system is composed as follows (all figures in weight percent): 0.3- 0.5% xanthan gum, 0.2-0.4% anti-foaming agent, 6-7% glycerol, 0.3-0.5% ethanol, 4-7% FAEOS (fatty alcohol ether sulfate), 24-28% nonionic surfactants, 1% boric acid, 1-2% sodium citrate (dihydrate), 2-4% soda, 14-16% coconut Fatty acids, 0.5% HEDP (1-hydroxyethane- (1,1-di-phosphonic acid)), 0-0.4% PVP (polyvinylpyrrolidone), 0-0.05% optical brightener, 0-0.001% dye, Rest demineralized water.
- the dosage of the liquid detergent is between 4.5 and 5.5 grams per liter of wash liquor, for example, 4.9 grams per liter of wash liquor. Preference is given to washing in a pH range between pH 8 and pH 10.5, preferably between pH 8 and pH 9.
- a preferred powdered detergent for such a washing system is composed as follows (all figures in weight percent): 10% linear alkylbenzenesulfonate (sodium salt), 1.5% C12-C18 fatty alcohol sulfate (sodium salt), 2.0% C12-C18 fatty alcohol with 7 EO, 20% sodium carbonate, 6.5% sodium bicarbonate, 4.0% amorphous sodium disilicate, 17% sodium carbonate peroxohydrate, 4.0% TAED, 3.0% polyacrylate, 1.0% 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 the determination of protease activity are disclosed in U.S. Patent Nos. 4,936,866 and 4,347,866 Surfactants, Vol. 7 (1970), pp. 125-132 ,
- the protease activity is preferably indicated in PE (protease units).
- suitable protease activities are 5 or 10 PE (protease units) per ml wash liquor.
- the enzymatic activity used is not equal to zero.
- the synergistic cleaning performance is based on a novel mechanism of action, i. There is no increase in the enzyme activity per se in the classical sense, as they would - in terms of proteases - would be measured in one of the following methods. Accordingly, a synergism according to the invention is also present in particular when an improved cleaning performance in the presence of components (a) and (b) is found compared to the sum of the cleaning powers of component (a) alone and component (b) alone, and the component ( b) in at least one of the subsequent test methods, preferably in both subsequent test methods, shows no effect with regard to the increase in 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 and 1000 ⁇ L of buffer are added to each cuvette per sample 1-300 ⁇ l of the buffer or component (b) (0.1, 0.2, 0.5 or 1% by weight in working buffer) are added to the cuvette, 1-300 ⁇ l of the protease or After the 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
- 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. These include, for example, dishwashing detergents for dishwashers or manual dishwashing detergents or cleaners for hard surfaces such as metal, glass, porcelain, ceramics, tiles, stone, painted surfaces, plastics, wood or leather, for which the term detergent is used, ie in addition to manual and machine Dishwashing agents, for example, scouring agents, glass cleaner, toilet scenters, etc.
- the washing 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.
- the ingredients to be selected as well as the conditions under which the agent is used, such as temperature, pH, ionic strength, redox ratios or mechanical influences, should be optimized for the 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.
- Particularly preferred are synergies which are present in a temperature range between 10 ° C and 60 ° C, in particular in a temperature range of 10 ° C to 50 ° C, from 10 ° C to 40 ° C, from 10 ° C to 30 ° C. , from 15 ° C to 30 ° C from 10 ° C to 25 ° C, from 15 ° C to 25 ° C, and most preferably at 20 ° C.
- an agent useful in the method of the invention further contains the hydrolytic enzyme in an amount of from 2 ⁇ g to 20 mg, preferably from 5 ⁇ g to 17.5 mg, more preferably from 20 ⁇ g to 15 mg and most preferably from 50 ⁇ g to 10 mg per g of the agent.
- the hydrolytic enzyme contained in the agent in particular a protease, and / or other ingredients of the agent may be coated with a substance impermeable to the enzyme at room temperature or in the absence of water, which becomes permeable to the enzyme under conditions of use of the agent.
- the hydrolytic enzyme is at room temperature or in the absence of water for the enzyme impermeable substance is enveloped.
- 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, .beta.-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 include, for example, hand washing, manual removal of stains from textiles or from hard surfaces or machine processes.
- Methods for cleaning textiles are generally distinguished by the fact that various cleaning-active substances are applied to the items to be cleaned in a plurality of process steps and washed off after the action time, or that the items to be cleaned are otherwise treated with a detergent or a solution of this agent. The same applies to methods for cleaning hard surfaces.
- a 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 microbial metabolite to enhance the cleaning performance of a protease in a washing or cleaning process, wherein the microbial metabolite is selected from the group consisting of 2,3-butanediol, pyruvate, propionate, butyrate and levan.
- 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 even.
- 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.
- Stock solutions of these substances were prepared with 0.00001-1.5 M substance or 0.0001-55% (weight) in water or buffer (phosphate 0.00001-1.5 M pH 6.5-8.0 or Tris 0.00001-1.5 M pH 7.5-9.0 or Soerensen buffer pH 7.5-9.0 or citrate buffer 0.00001-1.5 M pH 4.5-7.0 or acetate buffer 0 , 00001-1.5 M pH 2.5-5.5).
- buffer phosphate 0.00001-1.5 M pH 6.5-8.0 or Tris 0.00001-1.5 M pH 7.5-9.0 or Soerensen buffer pH 7.5-9.0 or citrate buffer 0.00001-1.5 M pH 4.5-7.0 or acetate buffer 0 , 00001-1.5 M pH 2.5-5.5).
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Claims (8)
- Procédé permettant d'accroître l'activité d'une protéase dans un produit détergent ou de nettoyage, caractérisé en ce qu'un métabolite microbien, qui agit en coopération avec la protéase sur un pouvoir nettoyant synergique lors de l'application du produit, est ajouté au produit détergent ou de nettoyage, le métabolite microbien étant choisi dans le groupe constitué par le 2,3-butanediol, le pyruvate, le propionate, le butyrate et le lévane.
- Procédé selon la revendication 1, caractérisé en ce que le métabolite microbien 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.
- Procédé selon l'une des revendications 1 ou 2, caractérisé en ce que le métabolite microbien est présent dans le produit à raison de 0,018 à 0,2 % en poids, en particulier de 0,04 à 0,1 % en poids.
- Procédé selon l'une des revendications 1 à 3, caractérisé en ce que le métabolite microbien est présent dans le liquide détergent ou de nettoyage à une concentration de 0,00025 à 0,6 % en poids, en particulier de 0,0003 à 0,5 % en poids.
- Procédé selon l'une des revendications 1 à 4, caractérisé en ce que le produit détergent ou de nettoyage contient la protéase en une quantité de 2 µg à 20 mg, de préférence de 5 µg à 17,5 mg, plus particulièrement de 20 µg à 15 mg et plus préférablement de 50 µg à 10 mg par g du détergent, et/ou en ce que la protéase contenue dans le produit détergent ou de nettoyage est enrobée d'une substance imperméable à l'enzyme à température ambiante ou en l'absence d'eau.
- Procédé selon l'une des revendications 1 à 5, caractérisé en ce que le produit détergent ou de nettoyage se présente(a) sous forme solide, en particulier comme une poudre fluide présentant une densité apparente de 300 à 1 200 g/l, en particulier de 500 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.
- Utilisation d'un métabolite microbien permettant d'améliorer le pouvoir nettoyant d'une protéase dans un processus de lavage ou de nettoyage, caractérisée en ce que le métabolite microbien est choisi dans le groupe constitué par le 2,3-butanediol, le pyruvate, le propionate, le butyrate et lévane.
- Utilisation selon la revendication 7, caractérisée en ce que le métabolite microbien 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.
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PL14152970.1T PL2727989T5 (pl) | 2008-08-20 | 2009-07-10 | Sposób polepszenia skuteczności czyszczenia środka piorącego lub czyszczącego |
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DE102008038479A DE102008038479A1 (de) | 2008-08-20 | 2008-08-20 | Wasch- oder Reinigungsmittel mit gesteigerter Waschkraft |
EP09780407.4A EP2313482B2 (fr) | 2008-08-20 | 2009-07-10 | Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant |
PCT/EP2009/058789 WO2010020475A2 (fr) | 2008-08-20 | 2009-07-10 | Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant |
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EP09780407.4A Division EP2313482B2 (fr) | 2008-08-20 | 2009-07-10 | Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant |
EP09780407.4A Division-Into EP2313482B2 (fr) | 2008-08-20 | 2009-07-10 | Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant |
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EP2727989A2 EP2727989A2 (fr) | 2014-05-07 |
EP2727989A3 EP2727989A3 (fr) | 2016-03-16 |
EP2727989B1 true EP2727989B1 (fr) | 2019-06-26 |
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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 |
EP09780409.0A Revoked EP2313483B1 (fr) | 2008-08-20 | 2009-07-10 | Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant |
EP14152970.1A Active EP2727989B2 (fr) | 2008-08-20 | 2009-07-10 | Procédé d'amélioration de la puissance de nettoyage d'un produit de lavage et de nettoyage |
EP09780407.4A Active EP2313482B2 (fr) | 2008-08-20 | 2009-07-10 | Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant |
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EP14152968.5A Active EP2727988B1 (fr) | 2008-08-20 | 2009-07-10 | Procédé d'amélioration de la puissance de nettoyage d'un produit de lavage ou de nettoyage |
EP09780409.0A Revoked EP2313483B1 (fr) | 2008-08-20 | 2009-07-10 | Procédé pour améliorer le pouvoir de nettoyage d'un produit détergent ou nettoyant |
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US (2) | US20110136720A1 (fr) |
EP (5) | EP2727990A3 (fr) |
DE (1) | DE102008038479A1 (fr) |
ES (3) | ES2744829T5 (fr) |
PL (3) | PL2727989T5 (fr) |
WO (2) | WO2010020475A2 (fr) |
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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 |
WO2012010405A1 (fr) | 2010-07-22 | 2012-01-26 | Unilever Plc | Compositions de détergent comprenant un biosurfactant et une enzyme |
DE102012206571A1 (de) | 2012-04-20 | 2013-10-24 | Henkel Ag & Co. Kgaa | Lagerstabiles Wasch- oder Reinigungsmittel mit gesteigerter Reinigungsleistung |
US9458441B2 (en) | 2012-05-07 | 2016-10-04 | Novozymes A/S | Polypeptides having xanthan degrading activity and polynucleotides encoding same |
DE102012220103A1 (de) | 2012-11-05 | 2014-05-08 | Henkel Ag & Co. Kgaa | Die Primärwaschkraft verbessernde Tensidkombination |
WO2014200658A1 (fr) | 2013-06-13 | 2014-12-18 | Danisco Us Inc. | Alpha-amylase issue de promicromonospora vindobonensis |
WO2014200657A1 (fr) | 2013-06-13 | 2014-12-18 | Danisco Us Inc. | Alpha-amylase provenant destreptomyces xiamenensis |
WO2014200656A1 (fr) | 2013-06-13 | 2014-12-18 | Danisco Us Inc. | Alpha-amylase provenant de streptomyces umbrinus |
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2008
- 2008-08-20 DE DE102008038479A patent/DE102008038479A1/de not_active Withdrawn
-
2009
- 2009-07-10 EP EP14152971.9A patent/EP2727990A3/fr not_active Ceased
- 2009-07-10 ES ES09780407T patent/ES2744829T5/es active Active
- 2009-07-10 EP EP14152968.5A patent/EP2727988B1/fr active Active
- 2009-07-10 WO PCT/EP2009/058789 patent/WO2010020475A2/fr active Application Filing
- 2009-07-10 ES ES14152970T patent/ES2745761T5/es active Active
- 2009-07-10 ES ES14152968T patent/ES2753240T3/es active Active
- 2009-07-10 PL PL14152970.1T patent/PL2727989T5/pl unknown
- 2009-07-10 WO PCT/EP2009/058791 patent/WO2010020476A2/fr active Application Filing
- 2009-07-10 PL PL09780407.4T patent/PL2313482T5/pl unknown
- 2009-07-10 EP EP09780409.0A patent/EP2313483B1/fr not_active Revoked
- 2009-07-10 PL PL14152968T patent/PL2727988T3/pl unknown
- 2009-07-10 EP EP14152970.1A patent/EP2727989B2/fr active Active
- 2009-07-10 EP EP09780407.4A patent/EP2313482B2/fr active Active
-
2011
- 2011-02-14 US US13/026,344 patent/US20110136720A1/en not_active Abandoned
- 2011-02-14 US US13/026,491 patent/US20110201536A1/en not_active Abandoned
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DE19953057A1 (de) | 1999-11-03 | 2001-05-10 | Henkel Kgaa | Enzymhaltige höherviskose Flüssigwaschmittel |
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Also Published As
Publication number | Publication date |
---|---|
EP2727988A3 (fr) | 2016-03-16 |
EP2727990A3 (fr) | 2016-03-16 |
ES2753240T3 (es) | 2020-04-07 |
PL2727988T3 (pl) | 2020-02-28 |
PL2313482T5 (pl) | 2023-02-27 |
EP2727989A3 (fr) | 2016-03-16 |
ES2744829T5 (es) | 2022-10-19 |
EP2313482B1 (fr) | 2019-06-12 |
WO2010020476A3 (fr) | 2010-06-17 |
US20110136720A1 (en) | 2011-06-09 |
PL2727989T5 (pl) | 2023-03-27 |
ES2744829T3 (es) | 2020-02-26 |
WO2010020475A2 (fr) | 2010-02-25 |
PL2727989T3 (pl) | 2019-12-31 |
US20110201536A1 (en) | 2011-08-18 |
EP2727989A2 (fr) | 2014-05-07 |
ES2745761T3 (es) | 2020-03-03 |
EP2727990A2 (fr) | 2014-05-07 |
EP2313483A2 (fr) | 2011-04-27 |
EP2727988A2 (fr) | 2014-05-07 |
ES2745761T5 (es) | 2023-03-09 |
PL2313482T3 (pl) | 2019-11-29 |
WO2010020475A3 (fr) | 2010-06-17 |
EP2313482A2 (fr) | 2011-04-27 |
EP2313483B1 (fr) | 2018-06-20 |
DE102008038479A1 (de) | 2010-02-25 |
EP2313482B2 (fr) | 2022-07-27 |
EP2727988B1 (fr) | 2019-09-04 |
EP2727989B2 (fr) | 2022-12-21 |
WO2010020476A2 (fr) | 2010-02-25 |
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