EP2838983B1 - Composition détergente stable au stockage, à performance detergente accrue - Google Patents

Composition détergente stable au stockage, à performance detergente accrue Download PDF

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Publication number
EP2838983B1
EP2838983B1 EP13715693.1A EP13715693A EP2838983B1 EP 2838983 B1 EP2838983 B1 EP 2838983B1 EP 13715693 A EP13715693 A EP 13715693A EP 2838983 B1 EP2838983 B1 EP 2838983B1
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Prior art keywords
acid
washing
protease
amino acid
polymer
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German (de)
English (en)
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EP2838983A1 (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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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. More particularly, the invention relates to protease-containing detergents and cleaners containing performance-enhancing combinations of active ingredients, and further 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.
  • enzymes in detergents and cleaners is well established in the art. They serve to extend the range of services of the funds concerned according to their specific activities. These include in particular hydrolytic enzymes such as proteases, amylases, lipases and cellulases.
  • subtilases The enzymes that are the longest-established and contained in virtually all modern, high-performance detergents and cleaners are proteases, and in particular serine proteases. They cause the degradation of protein-containing stains on the items to be cleaned.
  • a subset of the serine proteases, subtilases has been reported by Siezen et al. (Protein Eng. 4 (1991) 719-737 and Protein Science 6 (1997) 501-523 ) based on homology analysis of more than 170 amino acid sequences of serine proteases previously referred to as subtilisin-like proteases.
  • 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. Synergies between the enzymes, in particular proteases, and other constituents of the respective detergents or cleaning agents, and preferably with regard to the cleaning performance of protease-sensitive soiling, are advantageously obtained in detergents or cleaners.
  • amino acids or polyamino acids can interact favorably with proteases and improve the cleaning performance on protease-sensitive stains.
  • the disadvantage is that the required amounts of polymer, for example over 3 wt .-%, often can not be incorporated stable in the detergents or cleaning agents. Particularly problematic are such high polymer concentrations in liquid formulations and especially serious in high-surfactant liquid formulations.
  • 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.
  • An object of the invention is therefore a protease-containing washing or cleaning agent comprising a polymer and a complexing agent according to claim 1.
  • Another object of the invention is a method for increasing the cleaning performance of a protease-containing detergent or cleaning agent according to claim 11.
  • compositions according to the invention are distinguished by advantageous stability and advantageous, in particular 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 respect to at least one protease-sensitive soiling, in particular also at low temperatures, for example between 10 ° C and 50 ° C, between 10 ° C and 40 ° C or between 20 ° C and 40 ° C.
  • cleaning performance means the ability of the washing or cleaning agent to remove an existing soiling partially or completely when the agent is used.
  • this is preferably the whitening performance on one or more stains on textiles.
  • laundry soiling are blood milk / cotton on cotton, whole egg / pigment on cotton, chocolate milk / cotton ink, peanut oil pigment / ink on polyester / cotton, grass on cotton, chocolate pudding on cotton, chocolate milk or cocoa on cotton.
  • cleaning performance describes the ability of the dishwashing detergent to remove an existing soiling from the hard surface of the dishware.
  • scrape dirt are milk, minced meat, egg yolk, oatmeal and starch.
  • both the washing or cleaning agent which comprises the protease and the polymer and the complexing agent or the wash liquor formed by this agent, and the protease itself have a respective cleaning performance.
  • the cleaning performance of the enzyme thus contributes to the cleaning performance of the agent or of the wash liquor formed by the agent.
  • the proteolytic cleaning performance refers to the cleaning performance of the agent on protease-sensitive stains, especially on blood milk / ink on cotton.
  • the cleaning performance is determined in a customary manner, preferably as indicated below.
  • 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.
  • the polymer is a homopolymer or preferably a heteropolymer (copolymer).
  • a polymer to be used according to the invention is obtainable by polymerization of 50 to 100 mole percent, preferably 80 to 100 mole percent, of a hydrophilic monomer selected from the group consisting of acrylic acid and its salts (H1), methacrylic acid and its salts (H2), maleic acid and their salts (H3), fumaric acid and its 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 (H11), 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 consist
  • Particularly preferred polymers are composed as follows: Polymers No Hydrophilic monomer (50-100 mole percent) Lipophilic monomer (0-50 mole percent) Lipophilic monomer (0-20 mole percent) 1-6 H1 L1 L2 L3 L1 L2 L3 7-12 H2 L1 L2 L3 L1 L2 L3 13-18 H3 L1 L2 L3 L1 L2 L3 19-24 H4 L1 L2 L3 L1 L2 L3 25-30 H5 L1 L2 L3 L1 L2 L3 31-36 H6 L1 L2 L3 L1 L2 L3 37-42 H7 L1 L2 L3 L1 L2 L3 43-48 H8 L1 L2 L3 L1 L2 L3 49-54 H9 L1 L2 L3 L1 L2 L3 55-60 H10 L1 L2 L3 L1 L2 L3 66-72 H11 L1 L2 L3 L1 L2 L3 73-78 H12 L1 L2 L3 L1 L2 L3 Hydrophilic monomer (
  • heteropolymers of the present invention are random copolymers in which the distribution of the two monomers in the chain is random, gradient copolymers having a variable proportion of a monomer in the course of the chain, alternating copolymers having a regular, alternating arrangement of the monomers along the chain , Block copolymers consisting of longer sequences (blocks) of each monomer or graft copolymers in which blocks of one monomer are grafted onto the backbone of another monomer.
  • the polymers and copolymers may, if they comprise acid groups, be present as an acid or as a salt or in a mixture.
  • the polymer or copolymer comprises from 80 to 100 mole percent of a hydrophilic monomer and / or from 0 to 20 mole percent of a lipophilic monomer.
  • the washing or cleaning agent is characterized in that more than 50% of the monomers of the polymer in each case comprise at least one acrylic acid, modified acrylic acid, in particular a methacrylic acid, or a carboxylate.
  • the molar mass of the polymer is preferably between 1000 g / mol and 30,000 g / mol and more preferably between 1000 g / mol and 20,000 g / mol and between 1200 and 14,000 g / mol.
  • 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 polymer is in an agent of the invention in an amount of 0.25 to 2 wt .-%, preferably from 0.5 to 1.75 wt .-%, from 0.75 to 1.5 wt .-% or of 1 to 2 wt .-%, present.
  • the complexing agent is a phosphonate. This is in an agent 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 .-%, available.
  • 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 compounds) are used.
  • Organic P-substituted phosphonates are formed, for example, by the Michaelis-Arbusov reaction. Many of these phosphonates are soluble in water.
  • the complex-forming phosphonates comprise a number of different compounds such as, for example, diethylenetriaminepenta (methylenephosphonic acid) (DTPMP). Hydroxyalkane or aminoalkane phosphonates are particularly preferred in this application. Among the hydroxyalkane phosphonates, 1-hydroxyethane-1,1-diphosphonate (HEDP) is of particular importance. It is preferably used as the sodium salt, the disodium salt neutral and the tetrasodium salt alkaline (pH 9).
  • 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 the hexasodium salt of EDTMP or as hepta- and octa-sodium salt of DTPMP used.
  • the complexing agent used here is preferably HEDP for machine dishwashing detergents and DTPMP for detergents from the class of phosphonates.
  • the aminoalkanephosphonates also have a pronounced heavy metal binding capacity. Accordingly, in particular if the agents also contain bleach, it may be preferable to use aminoalkanephosphonates, in particular DTPMP, or to use mixtures of the phosphonates mentioned.
  • HEDP 1-hydroxyethane-1,1-diphosphonic acid
  • DTPMP diethylenetriaminepenta
  • 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 2 is 1 to 1 to 3, and more preferably 2 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 very particularly preferably 1 to 1. Such proportions lead to particularly advantageous forms of synergistic interaction of polymer and 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 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. 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.
  • SEQ ID NO. Figure 1 is the sequence of the mature (mature) alkaline protease from Bacillus lentus DSM 5483, which is disclosed in the international patent application WO 92/21760 , and the disclosure of which is hereby incorporated by reference.
  • SEQ ID NO. Figure 2 is the sequence of the mature (mature) protease from Bacillus amyloliquefaciens (BPN ').
  • proteases are:
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence 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, 90, 91, 91, 92, 92, 92 93.5%, 94.0%, 94.5%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0%, 98.5%, 99.0% and 99.5% is identical, and in the count according to SEQ ID NO.
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence 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.
  • SEQ ID NO. 1 has the amino acid substitution R99D, in particular a protease according to SEQ ID NO. 1 with the amino acid substitution R99D.
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence 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, 90, 91, 91, 92, 92, 92 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.
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence 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.
  • amino acid substitution R99E in combination with the amino acid substitutions S3T and V199I has, in particular a protease according to SEQ ID NO. 1 with the amino acid substitutions S3T, R99E and V199I.
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO.
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence 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.
  • SEQ ID NO. 1 has 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.
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence 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%, 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.
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence 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.
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence 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.
  • proteases as described above, in particular those which are based on SEQ ID NO. 1, which is also located at position 211 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. At least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, of the total amino acid sequence indicated. 85, 86, 87, 88, 89, 90, 90, 91, 91, 92, 92, 92 93.5%, 94.0%, 94.5%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0%, 98.5%, 99.0% and 99.5% is identical, and in the count according to SEQ ID NO.
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. At least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, of the total amino acid sequence indicated.
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. At least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, of the total amino acid sequence indicated. 85, 86, 87, 88, 89, 90, 90, 91, 91, 92, 92, 92 93.5%, 94.0%, 94.5%, 95.0%, 95.5%, 96.0%, 96.5%, 97.0%, 97.5%, 98.0%, 98.5%, 99.0% and 99.5% is identical, and in the count according to SEQ ID NO.
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. At least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, of the total amino acid sequence indicated.
  • SEQ ID NO. 2 has the amino acid substitution Y217K, in particular a protease according to SEQ ID NO. 2 with the amino acid substitution Y217K.
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO.
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. At least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, of the total amino acid sequence indicated.
  • SEQ ID NO. 2 has the amino acid substitution Y217S, in particular a protease according to SEQ ID NO. 2 with the amino acid substitution Y217S.
  • a protease comprising an amino acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO.
  • the amino acid positions are in the context of the present invention by an alignment of the amino acid sequence of the protease to be used with the amino acid sequence of the protease according to SEQ ID NO. 1 or SEQ ID NO. 2 defined as specified. Furthermore, the count depends on the mature (mature) protein. This assignment is also to be used in particular if the amino acid sequence of the protease to be used comprises a higher number of amino acid residues than the protease according to SEQ ID NO. 1 or SEQ ID NO. 2. Starting from the positions mentioned in the respective reference sequence, the amino acid positions in a protease to be used according to the invention are those which are just assigned to these positions in an alignment.
  • nucleic acid or amino acid sequences is determined by a sequence comparison. Such a comparison is made by assigning similar sequences in the nucleotide sequences or amino acid sequences to each other. This sequence comparison is preferably carried out based on the BLAST algorithm established and commonly used in the prior art (cf., for example, US Pat Altschul, SF, Gish, W., Miller, W., Myers, EW & Lipman, DJ (1990) "Basic local alignment search tool.” J. Mol. Biol. 215: 403-410 , and Altschul, Stephan F., Thomas L. Madden, Alejandro A. Schaffer, Jinghui Zhang, Hheng Zhang, Webb Miller, and David J.
  • T-Coffee cf., for example Notredame et al. (2000): T-Coffee: A novel method for multiple sequence alignments. J. Mol. Biol. 302, 205-217 ) or programs based on these programs or algorithms.
  • sequence comparisons and alignments are preferably created using the Vector NTI® Suite 10.3 computer program (Invitrogen Corporation, 1600 Faraday Avenue, Carlsbad, California, USA) with the default default parameters specified.
  • Such a comparison allows a statement about the similarity of the compared sequences to each other. It is usually given in percent identity, that is to say the proportion of identical nucleotides or amino acid residues at the same positions or in an alignment with one another.
  • the broader concept of homology involves conserved amino acid substitutions in the consideration of amino acid sequences, that is, amino acids with similar properties, since these usually perform similar activities or functions within the protein. Therefore, the similarity of the compared sequences can also be percent Homology or percent similarity.
  • Identity and / or homology information can be made about whole polypeptides or genes or only over individual regions. Homologous or identical regions of different nucleic acid or amino acid sequences are therefore defined by matches in the sequences. They often have the same or similar functions.
  • nucleic acid or amino acid sequence can be small and comprise only a few nucleotides or amino acids. Often, such small regions exert essential functions for the overall activity of the protein. It may therefore be useful to relate sequence matches only to individual, possibly small areas. Unless stated otherwise, identity or homology information in the present application, however, refers to the total length of the respectively indicated nucleic acid or amino acid sequence.
  • An agent according to the invention increasingly contains the protease in an amount of 1 ⁇ 10 -8 -5% by weight, of 0.0001-3% by weight, of 0.0005-1% by weight, of 0.001 to 0.75% by weight .-% and more preferably from 0.005 to 0.5 wt .-%, based on active protein.
  • 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 ).
  • the determination of the active protein concentration was carried out in this regard via a titration of the active sites using a suitable irreversible inhibitor (for proteases, for example, phenylmethylsulfonyl fluoride (PMSF)) and determination of the residual activity (see. Bender, M., et al., J. Am. Chem. Soc. 88, 24 (1966), p. 5890-5913 ).
  • a suitable irreversible inhibitor for proteases, for example, phenylmethylsulfonyl fluoride (PMSF)
  • the protease may also be adsorbed to carriers and / or embedded in encapsulants to protect against premature inactivation. In the wash liquor, ie under conditions of use, the enzyme is then released and can develop its catalytic activity.
  • amylase is an enzyme as described in the introduction.
  • synonymous terms may be used, for example, 1,4-alpha-D-glucan glucanohydrolase or glycogenase.
  • Preparable amylases according to the invention are preferably .alpha.-amylases.
  • Crucial for determining whether an enzyme is an ⁇ -amylase according to the invention is its ability to hydrolyze a (1-4) -glycoside bonds in the amylose of the starch.
  • Amylases which can be synthesized according to the invention are, for example, the ⁇ -amylases from Bacillus licheniformis, from Bacillus amyloliquefaciens or from Bacillus stearothermophilus, and in particular also their further developments improved for use in detergents or cleaners.
  • the enzyme from Bacillus licheniformis is from the company Novozymes under the name Termamyl® and from the company Danisco / Genencor under the name Purastar®ST available.
  • this ⁇ -amylase is available from the company Novozymes under the trade name Duramyl® and Termamyl®ultra, from the company Danisco / Genencor under the name Purastar®OxAm and from the company Daiwa Seiko Inc., Tokyo, Japan, as Keistase®.
  • the Bacillus amyloliquefaciens ⁇ -amylase is sold by the company 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, for this purpose, the ⁇ -amylase from Bacillus sp.
  • a 7-7 (DSM 12368) and cyclodextrin glucanotransferase (CGTase) from Bacillus agaradherens (DSM 9948).
  • fusion products of all the molecules mentioned can be used.
  • the further developments of the ⁇ -amylase from Aspergillus niger and A. oryzae available under the trade name Fungamyl® from the company Novozymes are suitable.
  • Further advantageously usable commercial products are, for example, the amylase-LT® and Stainzyme® or Stainzyme ultra® or Stainzyme plus®, the latter also from the company Novozymes.
  • variants of these enzymes obtainable by point mutations can be used according to the invention.
  • Particularly preferred amylases are disclosed in International Publications WO 00/60060 .
  • WO 03/002711 WO 03/054177 and WO07 / 079938 .
  • Detergents or cleaning compositions according to the invention which contain or are used together with the described active compounds or are used in a method according to the invention may contain all customary other constituents of such agents which do not interact in an undesired manner with the active ingredients essential to the invention.
  • the agent preferably contains synthetic anionic surfactant of the sulfate and / or sulfonate type, in particular alkylbenzenesulfonate, fatty alkylsulfate, fatty alkyl ether sulfate, alkyl and / or dialkylsulfosuccinate, sulfo fatty acid esters and / or sulfo fatty acid salts, in particular in an amount in the range of 2 wt .-% to 25 wt. -%.
  • synthetic anionic surfactant of the sulfate and / or sulfonate type in particular alkylbenzenesulfonate, fatty alkylsulfate, fatty alkyl ether sulfate, alkyl and / or dialkylsulfosuccinate, sulfo fatty acid esters and / or sulfo fatty acid salts, in particular in an amount in the range of 2
  • the anionic surfactant is preferably selected from the alkylbenzenesulfonates, the alkyl or alkenyl sulfates and / or the alkyl or alkenyl ether sulfates in which the alkyl or alkenyl group has 8 to 22, in particular 12 to 18, carbon atoms. These are usually not individual substances, but cuts or mixtures.
  • Another embodiment of such agents comprises the presence of nonionic surfactant selected from fatty alkyl polyglycosides, fatty alkyl polyalkoxylates, especially ethoxylates and / or propoxylates, fatty acid polyhydroxyamides and / or ethoxylation and / or propoxylation products of fatty alkylamines, vicinal diols, fatty acid alkyl esters and / or fatty acid amides and mixtures thereof, in particular in an amount in the range of 2 wt .-% to 25 wt .-%.
  • nonionic surfactant selected from fatty alkyl polyglycosides, fatty alkyl polyalkoxylates, especially ethoxylates and / or propoxylates, fatty acid polyhydroxyamides and / or ethoxylation and / or propoxylation products of fatty alkylamines, vicinal diols, fatty acid alkyl esters and / or fatty acid
  • Suitable nonionic surfactants include the alkoxylates, in particular the ethoxylates and / or propoxylates of saturated or mono- to polyunsaturated linear or branched-chain alcohols having 10 to 22 C atoms, preferably 12 to 18 C atoms.
  • the degree of alkoxylation of the alcohols is generally between 1 and 20, preferably between 3 and 10. They can be prepared in a known manner by reacting the corresponding alcohols with the corresponding alkylene oxides.
  • Particularly suitable are the derivatives of fatty alcohols, although their branched-chain isomers, in particular so-called oxo alcohols, can be used for the preparation of usable alkoxylates.
  • alkoxylates in particular the ethoxylates, primary alcohols with linear, in particular dodecyl, tetradecyl, hexadecyl or octadecyl radicals and mixtures thereof.
  • suitable alkoxylation products of alkylamines, vicinal diols and carboxamides, which correspond to the said alcohols with respect to the alkyl part usable.
  • the ethylene oxide and / or propylene oxide insertion products of fatty acid alkyl esters and Fettklarepolyhydroxyamide into consideration.
  • alkylpolyglycosides which are suitable for incorporation in the compositions according to the invention are compounds of the general formula (G) n -OR 12 , in which R 12 is an alkyl or alkenyl radical having 8 to 22 C atoms, G is a glycose unit and n is a number between 1 and 10 mean.
  • the glycoside component (G) n are oligomers or polymers of naturally occurring aldose or ketose monomers, in particular glucose, mannose, fructose, galactose, talose, gulose, altrose, allose, idose, ribose, arabinose, Include xylose and lyxose.
  • the oligomers consisting of such glycosidically linked monomers are characterized not only by the nature of the sugars contained in them by their number, the so-called Oligomermaschinesgrad.
  • the degree of oligomerization n assumes as the value to be determined analytically generally broken numerical values; it is between 1 and 10, with the glycosides preferably used below a value of 1.5, in particular between 1.2 and 1.4.
  • Preferred monomer building block is glucose because of its good availability.
  • Nonionic surfactant is in agents which contain the active ingredients described or used together or used in a method according to the invention, preferably in amounts of 1 wt .-% to 30 wt .-%, in particular from 1 wt .-% to 25 wt .-%, wherein amounts in the upper part of this range are more likely to be found in liquid detergents and particulate detergents preferably contain rather lower amounts of up to 5 wt .-%.
  • the agents may instead or additionally surfactants, preferably synthetic anionic surfactants of the sulfate or sulfonate type, to which, for example, the already mentioned alkylbenzenesulfonates, in amounts of preferably not more than 20 wt .-%, in particular from 0.1 wt .-% to 18 wt .-%, each based on the total agent included.
  • Suitable synthetic anionic surfactants which are particularly suitable for use in such compositions are the alkyl and / or alkenyl sulfates having 8 to 22 C atoms which carry an alkali, ammonium or alkyl or hydroxyalkyl-substituted ammonium ion as counter cation.
  • alkyl and alkenyl sulfates can be prepared in a known manner by reaction of the corresponding alcohol component with a conventional sulfating reagent, in particular sulfur trioxide or chlorosulfonic acid, and subsequent neutralization with alkali metal, ammonium or alkyl or hydroxyalkyl-substituted ammonium bases.
  • Sulfur-type surfactants which can be used also include the sulfated alkoxylation products of the alcohols mentioned, known as ether sulfates.
  • Such ether sulfates preferably contain from 2 to 30, in particular from 4 to 10, ethylene glycol groups per molecule.
  • Suitable anionic surfactants of the sulfonate type include the ⁇ -sulfoesters obtainable by reaction of fatty acid esters with sulfur trioxide and subsequent neutralization, in particular those of fatty acids having 8 to 22 C atoms, preferably 12 to 18 C atoms, and linear alcohols having 1 to 6 carbon atoms, preferably 1 to 4 carbon atoms, derivative sulfonation, as well as the formal saponification resulting from these sulfo fatty acids.
  • Preferred anionic surfactants are also the salts of sulfosuccinic acid esters, which are also referred to as alkylsulfosuccinates or dialkylsulfosuccinates, and the monoesters or diesters of sulfosuccinic acid with alcohols, preferably fatty alcohols and in particular ethoxylated fatty alcohols.
  • Preferred sulfosuccinates contain C 8 to C 18 fatty alcohol residues or mixtures of these.
  • Particularly preferred sulfosuccinates contain an ethoxylated fatty alcohol radical, which in itself is a nonionic surfactant.
  • Sulfosuccinates whose fatty alcohol residues are derived from ethoxylated fatty alcohols with a narrow homolog distribution, are again particularly preferred.
  • soaps saturated fatty acid soaps, such as the salts of lauric acid, myristic acid, palmitic acid or stearic acid, and from natural fatty acid mixtures, for example coconut, palm kernel or tallow fatty acids, derived soaps are suitable.
  • those soap mixtures are preferred which are composed of 50% to 100% by weight of saturated C 12 -C 18 fatty acid soaps and up to 50% by weight of oleic acid soap.
  • soap is included in amounts of from 0.1% to 5% by weight.
  • higher amounts of soap can be contained, usually up to 20 wt .-%.
  • 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.
  • 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.
  • the compositions may contain peroxygen bleaching agents, in particular in amounts ranging from 5% to 70% by weight, and optionally bleach activators, especially in amounts ranging from 2% to 10% by weight.
  • the bleaches in question are preferably the peroxygen compounds generally used in detergents, such as percarboxylic acids, for example dodecanedioic acid or phthaloylaminoperoxicaproic acid, hydrogen peroxide, alkali metal perborate, which may be in the form of tetra- or monohydrate, percarbonate, perpyrophosphate and persilicate, which are generally used as alkali metal salts, in particular as sodium salts.
  • Such bleaching agents are in detergents containing an active ingredient according to the invention, 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 total agent, present, in particular percarbonate is used.
  • the optionally present component of the bleach activators comprises the commonly used N- or O-acyl compounds, for example polyacylated alkylenediamines, in particular tetraacetylethylenediamine, acylated glycolurils, in particular tetraacetylglycoluril, N-acylated hydantoins, hydrazides, triazoles, urazoles, diketopiperazines, sulphurylamides and cyanurates, and also carboxylic acid anhydrides , in particular phthalic anhydride, carboxylic acid esters, in particular sodium isononanoyl-phenolsulfonate, and acylated sugar derivatives, in particular pentaacetylglucose, and also cationic nitrile derivatives such as trimethylammonium acetonitrile salts.
  • N- or O-acyl compounds for example polyacylated alkylenediamines, in particular tetraacety
  • 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 ingredients 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.
  • agents which contain an active substance used according to the invention up to 1% by weight, in particular 0.01% by weight to 0.5% by weight, of optical brighteners, in particular compounds from the class of the substituted 4,4 ' -Bis (2,4,6-triamino-s-triazinyl) -stilbene-2,2'-disulfonic acids, up to 5 wt .-%, in particular 0.1 wt .-% to 2 wt .-% complexing agent for Heavy metals, in particular Aminoalkylenphosphonklaren and their salts and up to 2 wt .-%, in particular 0.1 wt .-% to 1 wt .-% foam inhibitors, wherein said weight fractions refer to the total agent.
  • optical brighteners in particular compounds from the class of the substituted 4,4 ' -Bis (2,4,6-triamino-s-triazinyl) -stilbene-2,2'-disulfonic acids, up to 5
  • Solvents which can be used in particular for liquid agents are, in addition to water, preferably those which are water-miscible. These include the lower alcohols, for example, ethanol, propanol, isopropanol, and the isomeric butanols, glycerol, lower glycols, such as ethylene and propylene glycol, and the derivable from said classes of compounds ether.
  • the active compounds used in the invention are usually dissolved or in suspended form.
  • an agent according to the invention may contain, in addition to the protease, further enzymes.
  • an agent according to the invention is characterized in that it comprises at least one further enzyme, in particular an amylase, cellulase, hemicellulase, mannanase, pectin-splitting enzyme, tannase, xylanase, xanthanase, ⁇ -glucosidase, carrageenase, perhydrolase, Oxidoreductase, oxidase or lipase, and combinations thereof.
  • Such a further enzyme is advantageously contained in the agent in each case in an amount of 1 ⁇ 10 -8 to 5 percent by weight based on active protein. More preferably, each further enzyme is in an amount of 1 x 10 -7 -3 wt%, from 0.00001 to 1 wt%, from 0.00005 to 0.5 wt%, from 0.0001 to 0.1 wt .-% and particularly preferably from 0.0001 to 0.05 wt .-% in inventive compositions, based on active protein.
  • the determination of the active protein concentration can be carried out in a customary manner, in the case of hydrolases, for example, via a titration of the active sites using a suitable irreversible inhibitor and determination of the residual activity (cf., for example Bender, M., et al., J. Am. Chem. Soc. 88, 24 (1966), p. 5890-5913 ; 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 ⁇ -amylases from Bacillus licheniformis, from Bacillus amyloliquefaciens or from Bacillus stearothermophilus, and in particular also their further developments improved for use in detergents or cleaners.
  • the enzyme from Bacillus licheniformis is available from the company Novozymes under the name Termamyl® and from the company Danisco / Genencor under the name Purastar®ST.
  • this ⁇ -amylase is available from the company Novozymes under the trade name Duramyl® and Termamyl®ultra, from the company Danisco / Genencor under the name Purastar®OxAm and from the company Daiwa Seiko Inc., Tokyo, Japan, as Keistase®.
  • the Bacillus amyloliquefaciens ⁇ -amylase is sold by the company 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, for this purpose, the ⁇ -amylase from Bacillus sp.
  • a 7-7 (DSM 12368) and cyclodextrin glucanotransferase (CGTase) from Bacillus agaradherens (DSM 9948).
  • CCTase cyclodextrin glucanotransferase
  • fusion products of all the molecules mentioned can be used.
  • the further developments of the ⁇ -amylase from Aspergillus niger and A. oryzae available under the trade name Fungamyl® from the company Novozymes are suitable.
  • Further advantageously usable commercial products are, for example, the amylase-LT® and Stainzyme® or Stainzyme ultra® or Stainzyme plus®, the latter also from the company Novozymes.
  • variants of these enzymes obtainable by point mutations can be used according to the invention.
  • amylases are disclosed in International Publications WO 00/60060 . WO 03/002711 . WO 03/054177 and WO07 / 079938 , whose disclosure is therefore expressly referred to, or whose disclosure in this regard is therefore expressly incorporated into the present patent application. Further, amylases which can be synthesized according to the invention are preferably .alpha.-amylases.
  • lipases or cutinases which can be synthesized according to the invention, which are contained in particular because of their triglyceride-splitting activities, but also in order to generate in situ peracids from suitable precursors, are the lipases which are originally obtainable from Humicola lanuginosa (Thermomyces lanuginosus) or further developed, in particular those with the amino acid exchange D96L. They are 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 have been originally isolated from Fusarium solani pisi and Humicola insolens.
  • the lipases or cutinases can be used, the initial enzymes originally from Pseudomonas mendocina and Fusarium solanii have been isolated. Further important commercial products are the preparations M1 Lipase.RTM. And Lipomax.RTM., which were originally sold by Gist-Brocades, and the enzymes marketed by Meito Sangyo KK, Japan, under the name Lipase MY-30®, Lipase OF® and Lipase PL® to mention also the product Lumafast® from the company Genencor.
  • cellulases may be present, depending on the purpose, as pure enzymes, as enzyme preparations or in the form of mixtures in which the individual components advantageously supplement each other in terms of their various performance aspects.
  • aspects of performance include, in particular, contributions to the primary washing performance, to the secondary washing performance of the composition (anti-redeposition effect or graying inhibition) and finishing (fabric effect), up to the exercise of a "stone-washed" effect.
  • Cellulases (endoglucanases, EG) which can be synthesized according to the invention comprise, for example, the fungal cellulase preparation rich in endoglucanase (EG) or its further developments, which is offered by the company Novozymes under the trade name Celluzyme®. 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®.
  • cellulases available from the company AB Enzymes, Finland, under the trade names Ecostone® and Biotouch®, which are based, at least in part, on the 20 kD-EG of melanocarpus.
  • Other cellulases from 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 is available from the company Danisco / Genencor under the trade name Puradax®.
  • Other usable commercial products of the company Danisco / Genencor are "Genencor detergent cellulase L" and IndiAge®Neutra.
  • cellulases are Thielavia terrestris cellulase variants described in International Publication WO 98/12307 Cellulases from Melanocarpus, in particular Melanocarpus albomyces, disclosed in the international publication WO 97/14804 Cellulases of the EGIII type from Trichoderma reesei disclosed in the European patent application EP 1 305 432 and variations obtainable therefrom, in particular those disclosed in the European patent applications EP 1240525 and EP 1305432 , as well as cellulases, which are disclosed in international publications WO 1992006165 .
  • WO 96/29397 and WO 02/099091 Their respective disclosure is therefore expressly referred to or the relevant disclosure content thereof is therefore expressly included in the present patent application.
  • enzymes can be used, which are summarized by the term hemicellulases, in particular for the removal of certain problem soiling.
  • mannanases include, 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, EndoPolygalacturonase, poly- ⁇ -1,4-galacturonide glycanohydrolase, endogalacturonase, endo-D-galacturonase, galacturan 1,4- ⁇ -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 the company Novozymes, under the name Rohapect UF®, Rohapect TPL®, Rohapect PTE100®, Rohapect MPE®, Rohapect MA plus HC, Rohapect DA12L®, Rohapect 10L®, Rohapect B1L® 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 H2O2 concentrations), peroxidases, such as halo, chloro, bromo, lignin, glucose or manganese peroxidases, dioxygenases or laccases, can also be used to increase the bleaching effect (Phenol oxidases, polyphenol oxidases) may be included. Suitable commercial products Denilite 1 and 2 of the company Novozymes are mentioned. As an example of advantageous systems for enzymatic perhydrolysis can be applied to the applications WO 98/45398 A1 . WO 2005/056782 A2 such as WO 2004/058961 A1 directed. A combined enzymatic bleaching system comprising an oxidase and a perhydrolase describes the application WO 2005/124012 ,
  • customary enzyme stabilizers present in particular, if appropriate, in liquid agents include amino alcohols, for example mono-, di-, triethanol- and -propanolamine and mixtures thereof, lower carboxylic acids, boric acid, alkali borates, boric acid-carboxylic acid combinations, Boric acid esters, boronic acid derivatives, calcium salts, for example, Ca-formic acid combination, magnesium salts, and / or sulfur-containing reducing agents.
  • a phenylboronic acid derivative having the structural formula in which R is hydrogen, a hydroxyl, a C1-C6 alkyl, a substituted C1-C6 alkyl, a C1-C6 alkenyl or a substituted C1-C6 alkenyl group, preferably 4-formyl-phenyl boronic acid (4-FPBA).
  • an enzyme stabilizer is or comprises a polyol, in particular glycerol, 1,2-ethylene glycol or propylene glycol, an antioxidant, glyceric acid, lactate or a lactate derivative. It may also be one or more of those enzyme-stabilizing compounds described in international patent applications WO 07/113241 A1 and WO 02/008398 A1 are disclosed.
  • 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 behenic soap, fatty acid amides, paraffins, waxes, microcrystalline waxes, organopolysiloxanes and mixtures thereof, which moreover can contain microfine, optionally silanated or otherwise hydrophobicized silica.
  • foam inhibitors are preferably bound to granular, water-soluble carrier substances.
  • polyester-active soil release polymers which can be used in addition to the active compounds 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, wherein the first monomer is a dicarboxylic acid HOOC-Ph-COOH and the second monomer is a diol HO- (CHR 11 -) a OH, also known as polymeric Diol H- (O- (CHR 11 -) a ) b OH may be present.
  • Ph is 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 11 is hydrogen, an alkyl radical having 1 to 22 C atoms and mixtures thereof
  • a is a number from 2 to 6
  • b is a number from 1 to 300.
  • both monomer diol units -O- ( CHR 11 -) a O- as well as polymer diol units - (O- (CHR 11 -) a ) b O-.
  • 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 of 4 to 200, particularly 12 to 140.
  • the molecular weight or the average molecular weight or the maximum of the molecular weight distribution of preferred soil release polyester is in the range of 250 g / mol to 100,000 g / mol, in particular from 500 g / mol to 50,000 g / mol.
  • the acid underlying the remainder Ph is preferably selected from terephthalic acid, isophthalic acid, phthalic acid, trimellitic acid, mellitic acid, the isomers of sulfophthalic acid, sulfoisophthalic acid and sulfoterephthalic acid and mixtures thereof. If their acid groups are not part of the ester bonds in the polymer, they are preferably in salt form, in particular as alkali or ammonium salt. Among these, the sodium and potassium salts are particularly preferable.
  • 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.
  • the preferred diols HO- (CHR 11 -) a OH include those in which R 11 is hydrogen and a is a number from 2 to 6, and those in which a is 2 and R 11 is hydrogen and the alkyl radicals 1 to 10, in particular 1 to 3 C-atoms is selected.
  • R 11 is hydrogen and a is a number from 2 to 6
  • R 11 is hydrogen and the alkyl radicals 1 to 10, in particular 1 to 3 C-atoms is selected.
  • those of the formula HO-CH 2 -CHR 11 -OH in which R 11 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 an average molecular weight in the range from 1000 g / mol to 6000 g / mol.
  • these 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.
  • the ester groups bound by end groups alkyl, alkenyl and Arylmonocarbonklaren with 5 to 32 carbon atoms, in particular 5 to 18 carbon atoms, based.
  • 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, benzoic acid, which may carry 1 to 5 substituents having a total of up to 25 carbon atoms, in particular 1 to 12 carbon atoms, for example tert-butylbenz
  • the end groups may also be based on hydroxymonocarboxylic acids having 5 to 22 carbon atoms, which include, for example, hydroxyvaleric acid, hydroxycaproic acid, ricinoleic acid, their hydrogenation product 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 hydroxymonocarboxylic acid units per end group is in the range from 1 to 50, in particular from 1 to 10.
  • polymers of ethylene terephthalate and polyethylene oxide terephthalate in which the polyethylene glycol units have molecular weights of 750 g / mol to 5000 g / mol and the molar ratio of ethylene terephthalate to polyethylene oxide terephthalate is 50:50 to 90:10 used in combination with an essential ingredient of the invention.
  • 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.
  • preferred polymers have a solubility of at least 1 g per liter, in particular at least 10 g per liter, under these conditions.
  • Liquid or pasty compositions according to the invention in the form of customary solvents, in particular water, containing solutions are usually prepared by simply mixing the ingredients, which can be added in bulk or as a solution in an automatic mixer.
  • 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 soiling, in particular of protease-sensitive stains, on textiles or hard surfaces, ie for the cleaning of textiles or of hard surfaces the combination of protease, polymer and complexing agent contained, are advantageously used to remove contaminants from textiles or from 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 of the facts, subjects, and embodiments described for washing or cleaning compositions of the invention are also contemplated this subject invention applicable. 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.
  • 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.
  • the method is characterized in that the protease in the wash liquor in a concentration of 1 x 10 -10 -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 are shown (all data in% by weight): A B C D e F G H C9-13-Alkylbenzenesulfonate, Na salt 9 10 12 7 5 15 15 9 C12-18 fatty alcohol with 7 EO 8th 9 12 7 5 6 11 10 C12-14 fatty alcohol sulfonate with 2EO 7 10 2 2 5 C12-18 fatty acid, Na salt 4 3 4 3 4 0 4 7 citric acid 2 3 3 2 2 2 2 3 Sodium hydroxide, 50% 3 3 2 3 3 3 3 4 boric acid 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 Enzymes (amylase, protease, cellulase) + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + + +
  • the standard soiling "blood on cotton" Product No. 111 available from the company Eidgenössische Material- und Anlagentician (EMPA) Testmaterialien AG, St. Gallen, Switzerland, served as a protease-sensitive soiling.
  • the protease used 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 dosage of the detergent was 75ml detergent per 17I water
  • the water hardness was 2.5 mmol / l Ca: Mg 3: 1
  • the washing time 60 minutes Each approach was determined 6 times.
  • Example 2 Improved stability of detergents according to the invention

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  • Enzymes And Modification Thereof (AREA)

Claims (11)

  1. Agent de lavage ou de nettoyage contenant des protéases, comprenant un polymère et un agent de chélation, caractérisé en ce que le polymère peut être obtenu par polymérisation de 50 à 100 % en mol d'un monomère hydrophile, choisi dans le groupe constitué de l'acide acrylique, l'acide méthacrylique, l'acide maléique, l'acide fumarique, l'anhydre d'acide maléique, l'acide crotonique, l'acide itaconique, l'acide diméthylacrylique, l'acide vinylacétique, l'acide glutaconique, l'acide carboxyéthylacrylique, des sels des éléments susmentionnés et de mélanges de ces derniers, et de 0 à 50 % en mol d'un monomère lipophile choisi dans le groupe constitué des esters d'acide acrylique et des esters d'acide méthacrylique de formule CH2-CR1-C(=O)-O-R2 et des alpha-oléfines de formule CH2=CR1-R2, où R1 est H ou CH3, et R2 est un radical alkyle en C1-20 linéaire ou ramifié, et en ce que le polymère est présent dans une quantité allant de 0,25 à 2 % en poids et l'agent de chélation est présent dans une quantité allant de 1 à 5 % dans l'agent, l'agent de chélation étant un phosphonate et l'agent de lavage ou de nettoyage contenant des protéases étant liquide.
  2. Agent de lavage ou de nettoyage selon la revendication 1, caractérisé en ce que l'agent de chélation est un phosphonate, lequel est présent dans une quantité allant de 1 à 3 % en poids dans l'agent.
  3. Agent de lavage ou de nettoyage selon la revendication 1 ou 2, caractérisé en ce que le polymère présente de 80 à 100 % en mol du monomère hydrophile et de 0 à 20 % en mol du monomère lipophile.
  4. Agent de lavage ou de nettoyage selon l'une des revendications 1 à 3, caractérisé en ce que le rapport entre le polymère et le phosphonate est de 2:1 à 1:3.
  5. Agent de lavage ou de nettoyage selon l'une des revendications 1 à 4, caractérisé en ce que l'agent de chélation est un phosphonate, lequel est choisi dans le groupe constitué de
    a) l'acide aminotriméthylène phosphonique (ATMP) et/ou ses sels ;
    b) l'acide éthylènediaminetétraméthylène phosphonique (EDTMP) et/ou ses sels ;
    c) l'acide diéthylènetriamine-pentaméthylène phosphonique (DTPMP) et/ou ses sels ;
    d) l'acide 1-hydroxyéthane 1,1-diphosphonique (HEDP) et/ou ses sels ;
    e) l'acide 2-phosphonobutane-1,2,4-tricarboxylique (PBTC) et/ou ses sels ;
    f) l'acide hexaméthylènediamine-tétraméthylène phosphonique (HDTMP) et/ou ses sels ;
    g) l'acide nitrilotriméthylène phosphonique (NTMP) et/ou ses sels.
  6. Agent de lavage ou de nettoyage selon l'une des revendications 1 à 5, caractérisé en ce qu'il comprend en outre un autre agent de chélation, de préférence du citrate, de préférence dans une quantité allant de 1 à 6 % en poids.
  7. Agent de lavage ou de nettoyage selon l'une des revendications 1 à 6, caractérisé en ce que la protéase comprend une séquence d'acide aminé qui est sur sa longueur totale identique au moins à 70 % à la séquence d'acide aminé indiquée dans SEQ ID NO. 1 ou qui est sur sa longueur totale identique au moins à 70 % à la séquence d'acide aminé indiquée dans SEQ ID NO. 2.
  8. Agent de lavage ou de nettoyage selon l'une des revendications 1 à 7, caractérisé en ce que la protéase est présente dans une quantité allant de 1 x 10-8 à 5 pour cent en poids, rapporté à la protéine active.
  9. Utilisation d'un agent de lavage ou de nettoyage selon l'une des revendications 1 à 8 pour l'élimination de souillures sensibles aux protéases sur les textiles ou les surfaces dures.
  10. Procédé de nettoyage de textiles ou de surfaces dures, caractérisé en ce que l'on utilise, lors d'au moins une étape de procédé, un agent de lavage ou de nettoyage selon l'une des revendications 1 à 8.
  11. Procédé d'amélioration du pouvoir nettoyant d'un agent de lavage ou de nettoyage contenant des protéases, caractérisé en ce qu'un polymère et un agent de chélation sont ajoutés à l'agent de manière à ce que le polymère est présent en une quantité allant de 0,25 à 2 % en poids et que l'agent de chélation est présent en une quantité allant de 1 à 5 % en poids dans l'agent, l'agent de chélation étant un phosphonate et le polymère pouvant être obtenu par polymérisation de 50 à 100 % en mol d'un monomère hydrophile, choisi dans le groupe constitué de l'acide acrylique, l'acide méthacrylique, l'acide maléique, l'acide fumarique, l'anhydre d'acide maléique, l'acide crotonique, l'acide itaconique, l'acide diméthylacrylique, l'acide vinylacétique, l'acide glutaconique, l'acide carboxyéthylacrylique, des sels des éléments susmentionnés et de mélanges de ces derniers, et de 0 à 50 % en mol d'un monomère lipophile, choisi dans le groupe constitué des esters d'acide acrylique et des esters d'acide méthacrylique de formule CH2-CR1-C(=O)-O-R2 et des alpha-oléfines de formule CH2=CR1-R2, où R1 est H ou CH3, et R2 est un radical alkyle en C1-20 linéaire ou ramifié.
EP13715693.1A 2012-04-20 2013-04-12 Composition détergente stable au stockage, à performance detergente accrue Active EP2838983B1 (fr)

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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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DE102014208507A1 (de) 2014-05-07 2015-11-12 Henkel Ag & Co. Kgaa Waschmittel
AU2017322243B2 (en) 2016-09-07 2020-05-21 Ecolab Usa Inc. Detergent compositions containing a stabilized enzyme by phosphonates
MX2022015214A (es) 2020-06-10 2023-01-04 Chemetall Gmbh Composiciones acuosas de decapado y su uso.
KR20230022960A (ko) 2020-06-10 2023-02-16 케메탈 게엠베하 수성 피클링 조성물 및 그의 용도

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