EP2838983A1 - Détergent ou produit de nettoyage stable au stockage, à performance de nettoyage accrue - Google Patents

Détergent ou produit de nettoyage stable au stockage, à performance de nettoyage accrue

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Publication number
EP2838983A1
EP2838983A1 EP13715693.1A EP13715693A EP2838983A1 EP 2838983 A1 EP2838983 A1 EP 2838983A1 EP 13715693 A EP13715693 A EP 13715693A EP 2838983 A1 EP2838983 A1 EP 2838983A1
Authority
EP
European Patent Office
Prior art keywords
acid
amino acid
protease
washing
cleaning
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Granted
Application number
EP13715693.1A
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German (de)
English (en)
Other versions
EP2838983B1 (fr
Inventor
Inga Kerstin Vockenroth
Benoit Luneau
Eva-Maria Wikker
Dustin ULLMANN
Marc-Steffen Schiedel
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Henkel AG and Co KGaA
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Henkel AG and Co KGaA
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Publication of EP2838983A1 publication Critical patent/EP2838983A1/fr
Application granted granted Critical
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Active legal-status Critical Current
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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
    • C11D3/36—Organic compounds containing phosphorus
    • 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
    • C11D3/36—Organic compounds containing phosphorus
    • C11D3/364—Organic compounds containing phosphorus containing nitrogen
    • 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
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase

Definitions

  • the invention is in the field of detergents and cleaners.
  • the invention particularly relates to protease-containing detergents and cleaners which enhance performance
  • Combinations of active ingredients and also proposes methods in which such agents are used.
  • the invention further relates to uses of such agents and proposes methods for increasing the cleaning performance by the addition of defined active ingredients.
  • subtilisin-like proteases based on the homology analysis of more than 170 amino acid sequences of serine proteases previously referred to as subtilisin-like proteases.
  • Subtilisin originally referred to serine proteases formed by Gram-positive bacteria or fungi.
  • subtilisins according to Siezen et al. a subset of subtilases.
  • Subtilases act as nonspecific endopeptidases by hydrolyzing any acid amide linkages that reside within peptides or proteins. Their pH optimum is usually in the clearly alkaline range.
  • the present invention is therefore based on the object of improving the cleaning performance (washing power) of protease-containing detergents or cleaners, in particular with regard to protease-sensitive soiling.
  • both active ingredients makes it possible to use the polymer in a lower concentration. This makes it possible to dispense with higher polymer concentrations, for example greater than 3 wt .-%, the The protease-enhancing ("boosting") effect of the polymer already occurs at a lower level in the presence of the complexing agent
  • inventive agent by an advantageous stability and an advantageous, especially enhanced, proteolytic cleaning performance.
  • An agent according to the invention accordingly has an advantageous cleaning performance on protease-sensitive soiling.
  • Such an agent therefore allows a satisfactory or improved removal of at least one, preferably of several protease-sensitive stains on textiles and / or hard surfaces, for example crockery.
  • such a cleaning performance occurs with regard to at least one protease-sensitive soiling, especially at low levels
  • Washing liquor is understood as meaning the use solution containing the washing or cleaning agent, which acts on textiles or fabric or hard surfaces and thus comes into contact with the soiling present on textiles or fabrics or hard surfaces.
  • the wash liquor is formed when the washing or cleaning process begins and the washing or cleaning agent is dissolved, for example in a dishwasher, a washing machine or other suitable container and / or diluted with water.
  • a hydrophilic monomer selected from the group consisting of acrylic acid and its salts (H1), methacrylic acid and its salts (H2), maleic acid and its salts (H3), fumaric acid and their salts (H4), maleic anhydride (H5), crotonic acid and its salts (H6), itaconic acid and its salts (H7), dimethylacrylic acid and its salts (H8), vinylacetic acid and its salts (H9), glutaconic acid and its salts (H10 ), Carboxyethylacrylic acid and its salts (H1 1), and mixtures thereof (H12), and from 0 to 50 mole percent, preferably 0 to 20 mole percent, of a lipophilic monomer selected from the group consisting of acrylic ester (L1) and methacrylic acid ester ( L2) of the formula wherein R- ⁇ is H or CH 3 and R 2 is a linear or
  • R- ⁇ H or CH 3 and R 2 is a linear or branched alkyl radical of Ci to C 20 , preferably of C 3 to Ci 2 , is.
  • Particularly preferred polymers are composed as follows:
  • the polymer or copolymer comprises from 50 to 100 mole percent, preferably from 80 to 100 mole percent, of a hydrophilic monomer and / or from 0 to 50 mole percent, preferably from 0 to 20 mole percent, of a lipophilic monomer.
  • Acusol 445N polyacrylic acid, sodium salt, MW 4500 g / mol, Dow Chemical
  • Sokalan CP10 modified polyacrylic acid, sodium salt, MW 4000 g / mol, BASF
  • Sokalan CP 42 modified polycarboxylate, BASF
  • Sokalan CP 12S poly (maleic-co-acrylic acid), MW 3000 g / mol, BASF
  • Sokalan PA 15 polyacrylic acid, sodium salt, MW 1200 g / mol, BASF
  • polymer 3 poly (acrylic acid-co-n-butyl acrylate), MW 6800 g / mol, acrylic acid / butyl acrylate 88/12,
  • Acusol 590 polyacrylate copolymer; Ha
  • the complexing agent is a phosphonate. This is in one
  • Composition according to the invention in an amount of 1 to 5 wt .-%, preferably from 1 to 4 wt .-%, from 1, 2 to 3 wt .-% or from 1, 5 to 2 wt .-%, present.
  • Phosphonates are salts and organic compounds, especially esters, of phosphonic acid.
  • complex-forming organic P-substituted phosphonates which have a phosphorus-carbon bond phosphorus-organic
  • the complex-forming phosphonates include, in addition to the 1-hydroxyethane-1, 1-diphosphonic acid a number of different compounds such as
  • Tetrasodium salt alkaline (pH 9) reacts.
  • Preferred aminoalkanephosphonates are ethylenediamine tetramethylenephosphonate (EDTMP), diethylenetriaminepentamethylenephosphonate (DTPMP) and their higher homologs. They are preferably in the form of neutral sodium salts, eg. B. as hexasodium salt of EDTMP or as hepta- and octa sodium salt of DTPMP used.
  • EDTMP ethylenediamine tetramethylenephosphonate
  • DTPMP diethylenetriaminepentamethylenephosphonate
  • They are preferably in the form of neutral sodium salts, eg. B. as hexasodium salt of EDTMP or as hepta- and octa sodium salt of DTPMP used.
  • a complexing agent is from the class of
  • the aminoalkanephosphonates also have a pronounced
  • washing or cleaning agent contains one or more phosphonate (s) from the group
  • ETMP ethylenediaminetetra (methylenephosphonic acid)
  • DTPMP diethylenetriamine penta (methylenephosphonic acid)
  • HDTMP hexamethylenediaminetetra (methylenephosphonic acid)
  • NTMP nitrilotri (methylenephosphonic acid)
  • HEDP 1-hydroxyethane-1, 1-diphosphonic acid
  • DTPMP diethylenetriamine penta
  • the washing or cleaning agents according to the invention may contain two or more different phosphonates.
  • the washing or cleaning agent is therefore characterized in that the complexing agent is a phosphonate, which is preferably present in an amount of from 1 to 3% by weight, more preferably from 1.5 to 2% by weight, in the composition.
  • the ratio of polymer to complexing agent in the washing or cleaning agent 3 is 1 to 1 to 3 and increasingly preferably 2.5 to 1 to 1 to 2.5, 2 to 1 to 1 to 2, 1 , 5 to 1 to 1 to 1, 5, 1, 33 to 1 to 1 to 1, 33 and most preferably 1 to 1.
  • Such ratios lead to particularly advantageous forms of synergistic interaction of polymer and complexing agent. These ratios refer to the phosphonate contained as a complexing agent.
  • the washing or cleaning agent is characterized in that it further comprises a further complexing agent, preferably citrate.
  • a further complexing agent comprises as complexing agent accordingly the phosphonate as explained above and additionally a further complexing agent.
  • the further complexing agent is present in the composition in an amount of from 1 to 6 wt%, more preferably from 2 to 5 wt%, and most preferably from 2 to 3 wt%.
  • the further complexing agent is particularly preferably citrate.
  • a very particularly preferred agent thus comprises a combination of phosphonate and citrate, in particular from 1 to 5 wt .-% phosphonate and from 1 to 6 wt .-% citrate, most preferably from 1, 5 to 2 wt .-% phosphonate and from 2 to 3% by weight of citrate.
  • a protease contained in a washing or cleaning agent according to the invention has a proteolytic activity, that is, it is capable of hydrolysing peptide bonds of a polypeptide or protein. It is therefore an enzyme which catalyzes the hydrolysis of peptide bonds and thereby is able to cleave peptides or proteins. It is especially a subtilase and most preferably a subtilisin.
  • the protease contained in a washing or cleaning agent according to the invention preferably comprises an amino acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. 1 indicated
  • 2 at least 70% and more preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82% of the total amino acid sequence. , 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90.0%, 90.5%, 91, 0%, 91, 5%, 92.0%, 92.5%, 93.0%, 93.5%, 94.0%, 94.5%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0%, 98.5%, 99.0%, 99.5% and 100% is identical.
  • SEQ ID NO. Figure 1 is the sequence of the mature (mature) alkaline protease from Bacillus lentus DSM 5483, which is disclosed in International Patent Application WO 92/21760, the disclosure of which is incorporated herein by reference.
  • SEQ ID NO. Figure 2 is the sequence of the mature (mature) protease from Bacillus amyloliquefaciens ( ⁇ ' ).
  • proteases are:
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. 1 indicated
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. 1 indicated
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. 1 indicated
  • Amino acid sequence over its total length to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85% , 86%, 87%, 88%, 89%, 90.0%, 90.5%, 91, 0%, 91, 5%, 92.0%, 92.5%, 93.0%, 93, 5%, 94.0%, 94.5%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0%, 98, 5% and 98.8% is identical, and in the count according to SEQ ID NO. 1 the
  • Amino acid sequence over its total length to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85% , 86%, 87%, 88%, 89%, 90.0%, 90.5%, 91, 0%, 91, 5%, 92.0%, 92.5%, 93.0%, 93, 5%, 94.0%, 94.5%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0%, 98, 5% and 98.8% is identical, and in the count according to SEQ ID NO. 1 the
  • Amino acid sequence over its total length to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85% , 86%, 87%, 88%, 89%, 90.0%, 90.5%, 91, 0%, 91, 5%, 92.0%, 92.5%, 93.0%, 93, 5%, 94.0%, 94.5%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0%, 98, 5% and 98.8% is identical, and in the count according to SEQ ID NO. 1 the
  • Amino acid substitution R99E in combination with the amino acid substitutions V4I and V199I, in particular a protease according to SEQ ID NO. 1 with the amino acid substitutions V4I, R99E and V199I.
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. 1 indicated
  • Amino acid sequence over its total length to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85% , 86%, 87%, 88%, 89%, 90.0%, 90.5%, 91, 0%, 91, 5%, 92.0%, 92.5%, 93.0%, 93, 5%, 94.0%, 94.5%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0%, 98, 5% and 98.8% is identical, and in the count according to SEQ ID NO. 1 the
  • Amino acid substitution R99D in combination with the amino acid substitutions S3T and V4I, in particular a protease according to SEQ ID NO. 1 with the amino acid substitutions S3T, V4I and R99D.
  • Amino acid sequence over its total length to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85% , 86%, 87%, 88%, 89%, 90.0%, 90.5%, 91%, 91, 5%, 92.0%, 92.5%, 93.0%, 93.5% , 94.0%, 94.5%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0%, 98.5% and 98.8% is identical, and in the count according to SEQ ID NO. 1 the
  • Amino acid substitution R99D in combination with the amino acid substitutions S3T and V199I, in particular a protease according to SEQ ID NO. 1 with the amino acid substitutions S3T, R99D and V199I.
  • Amino acid sequence over its total length to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85% , 86%, 87%, 88%, 89%, 90.0%, 90.5%, 91, 0%, 91, 5%, 92.0%, 92.5%, 93.0%, 93, 5%, 94.0%, 94.5%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0%, 98, 5% and 98.8% is identical, and in the count according to SEQ ID NO. 1 the
  • Amino acid substitution R99D in combination with the amino acid substitutions V4I and V199I, in particular a protease according to SEQ ID NO. 1 with the amino acid substitutions V4I, R99D and V199I.
  • Amino acid sequence over its total length to at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85% , 86%, 87%, 88%, 89%, 90.0%, 90.5%, 91, 0%, 91, 5%, 92.0%, 92.5%, 93.0%, 93, 5%, 94.0%, 94.5%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0% and 98.5% is identical, and in the count according to SEQ ID NO. 1 the
  • Amino acid sequence corresponding to that shown in SEQ ID NO. 1 at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, of their total length. 85%, 86%, 87%, 88%, 89%, 90.0%, 90.5%, 91, 0%, 91, 5%, 92.0%, 92.5%, 93.0%, 93.5%, 94.0%, 94.5%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0% and 98.5% is identical, and in the count according to SEQ ID NO.
  • proteases as described above, in particular those which are based on SEQ ID NO. 1, which is further at position 21 1 in the count according to SEQ ID NO. 1 have the amino acid leucine (L).
  • proteases are:
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. 2 specified
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. 2 specified
  • compositions may also contain betaines and / or cationic surfactants, which, if present, are preferably used in amounts of from 0.5% by weight to 7% by weight.
  • esterquats discussed below are particularly preferred.
  • active ingredient used preferably in amounts of up to 25 wt .-%, in particular up to 15 wt .-% and particularly preferably from 5 wt .-% to 15 wt .-%, each based on the total agent, present, in particular percarbonate is used.
  • the bleach activators may have been coated and / or granulated in a known manner with coating substances in order to avoid the interaction with the per compounds, granulated tetraacetylethylenediamine having mean particle sizes of from 0.01 mm to 0.8 mm, granulated 1, with the aid of carboxymethylcellulose. 5-diacetyl-2,4-dioxohexahydro-1,3,5-triazine, and / or in particulate form, trialkylammonium acetonitrile is particularly preferred.
  • Such bleach activators are preferably contained in detergents in amounts of up to 8% by weight, in particular from 2% by weight to 6% by weight, based in each case on the total agent.
  • the agents may contain other ingredients customary in detergents or cleaners.
  • These optional constituents include, in particular, enzymes, enzyme stabilizers, complexing agents for heavy metals, for example aminopolycarboxylic acids, aminohydroxypolycarboxylic acids, polyphosphonic acids and / or aminopolyphosphonic acids, foam inhibitors, for example organopolysiloxanes or paraffins, solvents and optical brighteners, for example stilbene disulfonic acid derivatives.
  • Such a further enzyme is in the middle advantageously each in an amount of 1 x 10 "-8 to 5 weight percent based on active protein.
  • Each additional enzyme is increasingly preferred in an amount of 1 x 10" 7 wt -3 %, from 0.00001-1% by weight, from 0.00005-0.5% by weight, from 0.0001 to 0, 1% by weight and particularly preferably from 0.0001 to 0.05% by weight .-% in agents according to the invention, based on active protein.
  • the said reference relates to proteases, the principle of titration of the active sites being transferable to other hydrolases).
  • the enzymes show synergistic cleaning performance certain soils or stains, ie the enzymes contained in the middle composition assist each other in their cleaning performance.
  • Amylases which can be synthesized according to the invention are, for example, the a-amylases from Bacillus licheniformis, from Bacillus amyloliquefaciens or from Bacillus stearothermophilus and in particular also improved for use in detergents or cleaners
  • the Bacillus amyloliquefaciens ⁇ -amylase is sold by Novozymes under the name BAN®, and variants derived from the Bacillus stearothermophilus ⁇ -amylase under the names BSG® and Novamyl®, also from the company Novozymes. Furthermore, the a-amylase from Bacillus sp. A 7-7 (DSM 12368) and cyclodextrin glucanotransferase (CGTase) from Bacillus agaradherens (DSM 9948). Likewise, fusion products of all the molecules mentioned can be used. In addition, the further developments of the ⁇ -amylase from Aspergillus niger and A.
  • amylases which can be synthesized according to the invention are preferably ⁇ -amylases.
  • Lipase® and Lipomax® preparations originally marketed by Gist-Brocades and the enzymes marketed by Meito Sangyo KK, Japan under the name Lipase MY-30®, Lipase OF® and Lipase PL®, also the product Lumafast® from Genencor.
  • cellulases may be included, depending on the purpose as pure enzymes, as
  • These aspects of performance include, in particular, contributions to primary washing,
  • Celluzyme® is offered. Endolase® and Carezyme®, also available from Novozymes, are based on the 50 kD EG or 43 kD EG from Humicola insolens DSM 1800. Further commercial products of this company are Cellusoft®, Renozyme® and Celluclean®. Continue to be used, for example
  • mannanases for example, mannanases, xanthan lyases, xanthanases, xyloglucanases, xylanases, pullulanases, pectin-splitting enzymes and ⁇ -glucanases.
  • 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.
  • pectin-destroying enzymes in the context of the present invention are also counted enzymes with the designations pectinase, pectate lyase, pectin esterase, pectin methoxylase, pectin methoxylase, pectin methyl esterase, pectase, pectin methyl esterase, pectin esterase, pectin-pectin hydrolase, pectin-polymerase, endopolygalacturonase, pectolase, pectin hydrolase, pectin-polygalacturonase, Endo-polygalacturonase, poly-a-1, 4-galacturonide glycanohydrolase, endogalacturonase, endo-D-galacturonase, galacturan 1, 4-a-galacturonidase, exopolygalacturonase, poly (galacturonate) hydrolase, exo-
  • enzymes suitable for this purpose are, for example, under the name Gamanase®, Pektinex AR®, X-Pect® or Pectaway® from Novozymes, under the name Rohapect UF®, Rohapect TPL®, Rohapect PTE100®, Rohapect MPE®, Rohapect MA plus HC, Rohapect DA12L®, Rohapect 10L®, Rohapect B1 L® from AB Enzymes, and available under the name Pyrolase® from Diversa Corp., San Diego, CA, USA.
  • Oxidoreductases for example oxidases, oxygenases, catalases (which react as peroxidase at low H 2 O 2 concentrations), peroxidases, such as halo, chloro, bromo, lignin, glucose or manganese peroxidases, can also be used to increase the bleaching effect.
  • Dioxygenases or laccases may be included. Suitable commercial products Denilite 1 and 2 of the company Novozymes are mentioned.
  • Suitable commercial products Denilite 1 and 2 of the company Novozymes are mentioned.
  • systems for enzymatic perhydrolysis which can be used advantageously, reference is made to the applications WO 98/45398 A1, WO 2005/056782 A2 and WO 2004/058961 A1.
  • a combined enzymatic bleaching system comprising an oxidase and a perhydrolase describes the application WO 2005/124012.
  • the enzyme stabilizer is preferably in a concentration of 0.000001 to 10 wt .-% and increasingly preferably from 0.00001 to 5 wt .-%, from 0.0001 to 2.5 wt .-%, from 0.001 to 2 wt. %, from 0.01 to 1.5% by weight, and from 0.1 to 1% by weight in the composition.
  • Suitable foam inhibitors include long-chain soaps, especially behenine, fatty acid amides, paraffins, waxes, microcrystalline waxes, organopolysiloxanes, and mixtures thereof which, in addition, are microfine, optionally silanated or otherwise
  • hydrophobized silica may contain.
  • foam inhibitors are preferably bound to granular, water-soluble carrier substances.
  • polyester-active soil release polymers that can be used in addition to the essential ingredients of the invention include copolyesters of dicarboxylic acids, for example adipic acid, phthalic acid or terephthalic acid, diols, for example ethylene glycol or propylene glycol, and polydiols, for example, polyethylene glycol or polypropylene glycol.
  • dicarboxylic acids for example adipic acid, phthalic acid or terephthalic acid
  • diols for example ethylene glycol or propylene glycol
  • polydiols for example, polyethylene glycol or polypropylene glycol.
  • Preferred soil release polymers include those compounds which are formally accessible by esterification of two monomeric moieties, the first monomer being a dicarboxylic acid HOOC-Ph-COOH and the second monomer being a diol HO- (CHR-) a OH, also known as a polymeric diol H ⁇ O ⁇ CHRn - ⁇ OH may be present.
  • Ph represents an o-, m- or p-phenylene radical which has 1 to 4 substituents selected from
  • Alkyl radicals having 1 to 22 C atoms, sulfonic acid groups, carboxyl groups and mixtures thereof, R can be hydrogen, an alkyl radical having 1 to 22 C atoms and mixtures thereof, a is a number from 2 to 6 and b is a number from 1 to 300.
  • the molar ratio of monomer diol units to polymer diol units is preferably 100: 1 to 1: 100, in particular 10: 1 to 1:10.
  • the degree of polymerization b is preferably in the range from 4 to 200, in particular from 12 to 140.
  • acids having at least two carboxyl groups may be included in the soil release-capable polyester.
  • these include, for example, alkylene and alkenylene dicarboxylic acids such as malonic acid, succinic acid, fumaric acid, maleic acid, glutaric acid, adipic acid, pimelic acid, suberic acid, azelaic acid and sebacic acid.
  • Preferred diols HO- (CHR-) a OH include those in which R is hydrogen and a is a number from 2 to 6, and those in which a is 2 and R is hydrogen and the alkyl radicals have from 1 to 10 , in particular 1 to 3 C-atoms is selected.
  • R is hydrogen and a is a number from 2 to 6
  • a is 2 and R is hydrogen and the alkyl radicals have from 1 to 10 , in particular 1 to 3 C-atoms is selected.
  • those of the formula HO-CH 2 - CHR -OH, in which R has the abovementioned meaning are particularly preferred.
  • diol components are ethylene glycol, 1, 2-propylene glycol, 1, 3-propylene glycol, 1, 4-butanediol, 1, 5-pentanediol, 1, 6-hexanediol, 1, 8-octanediol, 1, 2-decanediol, 1, 2-dodecanediol and neopentyl glycol.
  • Particularly preferred among the polymeric diols is polyethylene glycol having a middle one
  • polyesters as described above may also be end-capped, alkyl groups having from 1 to 22 carbon atoms and esters of monocarboxylic acids being suitable as end groups.
  • esters of monocarboxylic acids being suitable as end groups.
  • End groups can be based on alkyl, alkenyl and aryl monocarboxylic acids having 5 to 32 C atoms, in particular 5 to 18 C atoms. These include valeric acid, caproic acid, enanthic acid, caprylic acid, pelargonic acid, capric acid, undecanoic acid, undecenoic acid, lauric acid, lauroleinic acid, tridecanoic acid, myristic acid, myristoleic acid, pentadecanoic acid, palmitic acid, stearic acid, petroselinic acid, petroselaidic acid, oleic acid, linoleic acid, linolaidic acid, linolenic acid, levostearic acid , Arachidic acid, gadoleic acid, arachidonic acid, behenic acid, Erucic acid, brassidic acid, clupanodonic acid, lignoceric acid, cerotic acid, melissic acid, benzo
  • the end groups may also be based on hydroxymonocarboxylic acids having from 5 to 22 carbon atoms, including, for example, hydroxyvaleric acid, hydroxycaproic acid, ricinoleic acid, the hydrogenation product of which include hydroxystearic acid and o-, m- and p-hydroxybenzoic acid.
  • the hydroxymonocarboxylic acids may in turn be linked to one another via their hydroxyl group and their carboxyl group and thus be present several times in an end group.
  • the number of hydroxy-monocarboxylic acid units per end group is in the range from 1 to 50, in particular from 1 to 10.
  • the soil release polymers are preferably water-soluble, the term "water-soluble” being understood to mean a solubility of at least 0.01 g, preferably at least 0.1 g of the polymer per liter of water at room temperature and pH 8.
  • Preferably used polymers have these conditions However, a solubility of at least 1 g per liter, in particular at least 10 g per liter.
  • compositions according to the invention presents no difficulties and can be carried out in a known manner, for example by spray-drying or granulation, enzymes and possibly other thermally sensitive ingredients such as, for example, bleaching agents optionally being added separately later.
  • inventive compositions having an increased bulk density in particular in the range from 650 g / l to 950 g / l, a process comprising an extrusion step is preferred.
  • Rotary presses pressed with compressive forces in the range of about 50 to 100 kN, preferably at 60 to 70 kN. Particularly in the case of multilayer tablets, it may be advantageous if at least one layer is pre-compressed. This is preferably carried out at pressing forces between 5 and 20 kN, in particular at 10 to 15 kN. This gives fracture-resistant and yet sufficiently rapidly soluble tablets under application conditions with breaking and bending strengths of normally 100 to 200 N, but preferably more than 150 N.
  • a tablet produced in this way has a weight of from 10 g to 50 g, in particular from 15 g to 40 g.
  • the spatial form of the tablets is arbitrary and can be round, oval or angular, with intermediate forms are also possible. Corners and edges are advantageously rounded. Round tablets preferably have a diameter of 30 mm to 40 mm. In particular, the size of square or cuboid shaped tablets, which predominantly over the
  • Dosing device for example, the dishwasher are introduced, is dependent on the geometry and the volume of this metering device.
  • Exemplary preferred embodiments have a base area of (20 to 30 mm) x (34 to 40 mm), in particular of 26x36 mm or 24x38 mm.
  • an agent according to the invention is enclosed by a water-soluble film.
  • the film comprises a polyvinyl alcohol (PVA) or consists of polyvinyl alcohol (PVA).
  • a further subject of the invention is the use of a washing or cleaning agent according to the invention for the removal of stains, in particular protease-sensitive stains, on textiles or hard surfaces, i. for cleaning textiles or hard surfaces.
  • stains in particular protease-sensitive stains
  • agents according to the invention can, in particular due to the combination of protease, polymer and complexing agent, advantageously be used to suit textiles or hard surfaces
  • Embodiments of this subject invention include, for example, hand washing, manual removal of stains from fabrics or hard surfaces, or use in conjunction with a machine process. All aspects, objects, and embodiments described for washing or cleaning compositions of the present invention are also directed to this subject matter applicable. Therefore, reference is made at this point expressly to the disclosure in the appropriate place with the statement that this disclosure also for the above inventive
  • a further subject of the invention is a process for the cleaning of textiles or of hard surfaces, wherein in at least one process step an inventive washing or cleaning agent is used.
  • This includes both manual and mechanical processes, with mechanical processes being preferred on account of their more precise controllability, for example with regard to the quantities and reaction times used.
  • 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 or dilution of this agent , The same applies to processes for cleaning all other materials than textiles, especially hard surfaces.
  • washing or cleaning methods can be enriched in at least one of the method steps to the application of a washing or cleaning agent according to the invention and then represent embodiments of the present invention.
  • All facts, objects and embodiments described for washing or cleaning agents according to the invention are also applicable to this subject 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 method.
  • the process is characterized in that the protease in the wash liquor in a concentration of 1 x 10 "0 -0.2 wt .-%, from 0.000001-0, 12 wt .-%, of 0, 000005-0.04 wt .-%, from 0.00001 to 0.03 wt .-% and particularly preferably from 0.00005 to 0.02 wt .-% is present, wherein the statements are based on active protein in the wash liquor.
  • the method is characterized in that it is carried out at a temperature between 10 ° C and 60 ° C, preferably between 20 ° C and 50 ° C and more preferably between 30 ° C and 50 ° C.
  • liquid detergents A to H according to the invention are shown (all data in% by weight):
  • Optical brightener 0, 1 0.2 0.2 0.2 0.2 0.2 0.2 0.2 0.2
  • Formulation A was used as base formulation. It was admixed with 1.5% by weight of a complex-forming phosphonate (DTPMP) and with 1, 5% by weight or 3% by weight of one of the following polymers:
  • DTPMP complex-forming phosphonate
  • Acusol 445N poly (acrylic acid), sodium salt, MW 4500g / mol, Dow Chemical)
  • Sokalan CP10 modified polyacrylic acid, sodium salt, MW 4000 g / mol, BASF
  • Sokalan CP 42 Modified Polycarboxylate, BASF
  • Sokalan CP 12S poly (maleic acid-co-acrylic acid), sodium salt, MW 3000 g / mol, BASF)
  • Sokalan PA 15 polyacrylic acid, sodium salt, MW 1200 g / mol, BASF
  • Polymer 3 (poly (acrylic acid-co-n-butyl acrylate); MW 6800 g / mol; acrylic acid / n-butyl acrylate 88/12
  • protease-sensitive stain used was the standard stain "blood on cotton" Product No. 1 11, available from Eidgenössische Material- und Anlagen (EMPA) Testmaterialien AG, St. Gallen, Switzerland
  • Protease was a protease according to SEQ ID NO 2 with the amino acid substitution Y217L in the count according to SEQ ID NO 2.
  • the washing temperature was 20 ° C. and 40 ° C.
  • the detergent dosage was 75 ml detergent per 17 l water
  • the water hardness was 2.5 mmol / l Ca: Mg 3: 1
  • washing time 60 minutes Each batch was determined 6-fold.
  • Formulation A was again used as the base formulation. As in Example 1, it was admixed with 1.5% by weight of a complex-forming phosphonate (DTPMP) and with 1. 5% by weight or 3% by weight of one of the following polymers:
  • DTPMP complex-forming phosphonate
  • Acusol 445N polyacrylic acid, sodium salt, MW 4500g / mol, Dow Chemical
  • Sokalan CP 42 Modified Polycarboxylate, BASF
  • Polymer 3 (poly (acrylic acid-co-n-butyl acrylate); MW 6800 g / mol; acrylic acid / n-butyl acrylate 88/12 mol%)

Abstract

La performance de nettoyage de détergents ou de produits de nettoyage contenant des protéases doit être améliorée pour des salissures sensibles aux protéases. Ce résultat est atteint grâce à un détergent ou à un produit de nettoyage contenant des protéases, comprenant un polymère et un agent complexant, dans lequel le polymère se présente, dans le produit, à raison d'une quantité de 0,25 à 2% en poids, et l'agent complexant, à raison d'une quantité de 1 à 5% en poids, et l'agent complexant est un phosphonate.
EP13715693.1A 2012-04-20 2013-04-12 Composition détergente stable au stockage, à performance detergente accrue Active EP2838983B1 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
DE102012206571A DE102012206571A1 (de) 2012-04-20 2012-04-20 Lagerstabiles Wasch- oder Reinigungsmittel mit gesteigerter Reinigungsleistung
PCT/EP2013/057648 WO2013156396A1 (fr) 2012-04-20 2013-04-12 Détergent ou produit de nettoyage stable au stockage, à performance de nettoyage accrue

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EP2838983A1 true EP2838983A1 (fr) 2015-02-25
EP2838983B1 EP2838983B1 (fr) 2018-12-19

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CN109563452B (zh) 2016-09-07 2021-11-30 埃科莱布美国股份有限公司 含有由膦酸稳定的酶的洗涤剂组合物
MX2022015224A (es) 2020-06-10 2023-01-05 Chemetall Gmbh Composiciones de decapado acuosas y su uso.
US20230220560A1 (en) 2020-06-10 2023-07-13 Chemetall Gmbh Aqueous Pickling Compositions and Their Use

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EP2838983B1 (fr) 2018-12-19
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