EP3234088A1 - Composition tensioactive liquide comprenant une combinaison de tensioactifs spécifique et une enzyme - Google Patents

Composition tensioactive liquide comprenant une combinaison de tensioactifs spécifique et une enzyme

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Publication number
EP3234088A1
EP3234088A1 EP15790151.3A EP15790151A EP3234088A1 EP 3234088 A1 EP3234088 A1 EP 3234088A1 EP 15790151 A EP15790151 A EP 15790151A EP 3234088 A1 EP3234088 A1 EP 3234088A1
Authority
EP
European Patent Office
Prior art keywords
amino acid
protease
surfactant composition
composition according
enzyme
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
EP15790151.3A
Other languages
German (de)
English (en)
Other versions
EP3234088B1 (fr
Inventor
Martina Seiler
Dieter Nickel
Sonja SAHNER
Christian RAMM
Timothy O'connell
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Henkel AG and Co KGaA
Original Assignee
Henkel AG and Co KGaA
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Filing date
Publication date
Application filed by Henkel AG and Co KGaA filed Critical Henkel AG and Co KGaA
Priority to PL15790151T priority Critical patent/PL3234088T3/pl
Publication of EP3234088A1 publication Critical patent/EP3234088A1/fr
Application granted granted Critical
Publication of EP3234088B1 publication Critical patent/EP3234088B1/fr
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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
    • C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/02—Anionic compounds
    • C11D1/12—Sulfonic acids or sulfuric acid esters; Salts thereof
    • C11D1/22—Sulfonic acids or sulfuric acid esters; Salts thereof derived from aromatic compounds
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/02—Anionic compounds
    • C11D1/37—Mixtures of compounds all of which are anionic
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/66—Non-ionic compounds
    • C11D1/83—Mixtures of non-ionic with anionic compounds
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/02—Anionic compounds
    • C11D1/12—Sulfonic acids or sulfuric acid esters; Salts thereof
    • C11D1/29—Sulfates of polyoxyalkylene ethers

Definitions

  • the present invention relates to the cleaning of textiles, as well as the provision of liquid compositions for this purpose.
  • liquid detergents are provided in a sufficient amount for several wash loads in storage containers. To carry out a washing process, the consumer removes the necessary for a wash dose of liquid detergent from this
  • the necessary dose is usually determined by measuring the liquid detergent in a measuring cup and then transferred, for example, in the dosing drawer of a washing machine, or placed together with the measuring cup directly into the washing drum of the washing machine.
  • liquid surfactant compositions suitable for the liquid detergents should be easily metered.
  • the liquid surfactant compositions should have a suitable rheology. Too thin compositions are perceived by consumers as more powerful. The reaction of this consumer perception must not lead to too viscous compositions, otherwise the residual emptying of the reservoir is insufficient.
  • the active substances contained in the liquid surfactant composition should also be incorporated in a storage-stable manner and retain the activity via storage.
  • compositions containing alkylbenzenesulfonate anionic surfactant, a specific combination of ethoxylated alkyl sulfates and nonionic surfactant, each in particular amounts and proportions provides a liquid surfactant composition having acceptable rheology and excellent activity of active ingredients incorporated therein, such as enzyme Dimensions guaranteed.
  • liquid surfactant compositions which contain 0.5 to 12% by weight of sodium carbonate, 5 to 35% by weight of a surfactant mixture, in each case based on the total weight of the surfactant mixture
  • Cio-16-alkyl-0- (CH 2 CH 2 0) 7-S03M, 15-55 wt .-% of a compound of formula Cio-16-alkyl-0- (CH2 CH20) 3 -H and
  • a first object of the invention is a liquid surfactant composition containing, based on the total weight of the composition
  • R is a Ci2-is-alkyl group
  • n is a number from 2 to 3 and M is a monovalent cation
  • R 2 is a Ci2-is-alkyl group
  • m is a number from 7 to 8 and M 'is a monovalent cation
  • Range limits are not included. Number ranges defined from one range limit to another range limit include the range limits.
  • Monovalent cations have a charge of 1.
  • composition of the invention is liquid at 25 ° C and 1013 mbar.
  • the surfactant composition according to the invention necessarily contains 2.0 to 8.5% by weight of C 9 -C 20 -alkylbenzenesulfonate, preferably cio-cis-alkylbenzenesulfonate, more preferably C 10 -C 13 -alkylbenzenesulfonate.
  • alkyl is preferably a linear or branched unsubstituted alkyl radical
  • Such highly preferred surfactants a) are selected from linear or branched alkylbenzenesulfonates of the formula a
  • liquid surfactant composition according to the invention necessarily contains a
  • R-O- (CH 2 CH 2 O) n -SO 3 M wherein R is a C 12-18 alkyl group, n is 2 or 3 and M is a monovalent cation stands. It is a Ci2-Ci8-alkyl sulfate with the monovalent counterion M and 2 or 3 moles of ethylene oxide per mole of Ci2-Ci8-alkyl group.
  • n is 2.
  • M is Na + , K + , ⁇ - ⁇ 2 ⁇ 2 ⁇ 3 + , (HO-CH 2 CH 2 ) 3NH + , most preferably Na + .
  • the liquid surfactant composition of the present invention contains a total of from 10.0 to 18.0 weight percent R-O- (CH 2 CH 2 O) 2-SO 3 Na where R is a C 12-18 alkyl group, especially dodecyl.
  • liquid surfactant composition according to the invention necessarily contains a
  • R 2 -O- (CH 2 CH 2 O) m -SO 3 M ' wherein R 2 is a C 12-18 alkyl group, m is 7 or 8 and M' is a monovalent cation is. It is a Ci2-Ci8-alkyl sulfate with the monovalent counterion M and 7 or 8 moles of ethylene oxide per mole of Ci2-Ci8-alkyl group.
  • m is 7. More preferably M 'is Na + , K + , ⁇ - ⁇ 2 ⁇ 2 ⁇ 3 + , (HO-CH 2 CH 2 ) 3NH + , most preferably Na + .
  • the liquid surfactant composition of the present invention contains a total of from 1.0 to 6.0% by weight of R 2 -O- (CH 2 CH 2 O) 7 -SO 3 Na, wherein R 2 is a C 12-18 alkyl group, especially for dodecyl stands.
  • compositions additionally contain soap (s) as anionic surfactant.
  • soap s
  • Soaps are the water-soluble sodium or potassium salts of the saturated and unsaturated fatty acids having from 10 to 20 carbon atoms, the rosin acids of rosin (yellow rosin soaps) and naphthenic acids which are used as solid or semi-solid mixtures mainly for washing and cleaning purposes.
  • Carbon atoms, in particular having 12 to 18 carbon atoms, according to the invention are preferred soaps.
  • Particularly preferred compositions are characterized
  • the surfactant composition according to the invention necessarily contains 2.0 to 10.0% by weight, preferably 2.5 to 7.5% by weight, more preferably 4.0 to 6.0% by weight, of nonionic surfactant.
  • compositions contain at least one nonionic surfactant from the group of fatty alcohol ethoxylates, since these surfactants are also at low
  • Washing temperatures provide high-performance compositions and have excellent cold stability in the case of liquid preparations.
  • compositions additionally contain at least one nonionic surfactant of the formula
  • R 2 is a linear or branched, substituted or unsubstituted alkyl
  • AO for an ethylene oxide (EO) or propylene oxide (PO) grouping
  • n stands for integers from 1 to 50.
  • R 2 is a linear or branched, substituted or unsubstituted alkyl, aryl or alkylaryl radical, preferably a linear, unsubstituted alkyl radical, particularly preferably a fatty alcohol radical.
  • Preferred radicals R 2 are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, Heptadecyl, octadecyl, nonadecyl, eicosyl and mixtures thereof, with the even number of carbon atoms being preferred.
  • radicals R 2 are derived from C 12-18 fatty alcohols, for example coconut oil fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl or stearyl alcohol or C 10 C 20 oxo alcohols.
  • AO represents an ethylene oxide (EO) or propylene oxide (PO) moiety, preferably an ethylene oxide moiety.
  • EO ethylene oxide
  • PO propylene oxide
  • m is an integer from 1 to 50, preferably from 1 to 20 and especially from 2 to 10. Most preferably, m is the numbers 2, 3, 4, 5, 6, 7 or 8.
  • compositions contain as nonionic surfactant, based on the total amount of the compositions, 2.0 to 10% by weight, preferably 2.5 to 7.5% by weight, more preferably 4.0 to 6.0% by weight.
  • Surfactant composition the weight ratio of the surfactant component a) to
  • Surfactant composition the weight ratio of the surfactant component a) to
  • Surfactant composition the weight ratio of the surfactant component a) to
  • liquid surfactant compositions contain based on the total weight of the composition a) a total amount of 2.0 to 8.5 wt .-% Cio-Ci5-alkyl benzene sulfonate (especially C10-C13 alkyl benzene sulfonate sodium), and
  • R is a Ci2-is-alkyl group and M is a monovalent cation (especially Na + ), and
  • R 2 is a Ci2-is-alkyl group and M 'is a monovalent cation (especially Na + ), and
  • At least one enzyme in particular at least one protease, again the proteases identified below being preferably suitable (vide infra), again preferably one or more of the surfactant weight ratios a) to b), a) to c) or a ) to d) respectively with respect to this embodiment.
  • composition according to the invention necessarily contains water as a solvent. It is inventively preferred, based on the weight of the composition, water in a total amount of 20 to 80 wt .-%, in particular from 30 to 70 wt .-%, most preferably from 40 to 60 wt .-%, use.
  • inventive liquid composition may be added organic solvents.
  • Organic solvents are liquid, dissolve at 20 ° C to at least 1 g in 100 g of distilled water and have at least one covalent bond between carbon and hydrogen in the molecule. It is essential according to the invention, based on the weight of
  • Composition amino-free organic solvents in a total amount of 0 to 10 wt .-%, in particular from 0 to 7.5 wt .-%, use.
  • Suitable amino-free organic solvents include mono- or polyhydric alcohols or glycol ethers, provided that they are miscible with water in the specified concentration range.
  • the amino-group-free organic solvents are preferably selected from ethanol, n-propanol, i-propanol, butanols, glycol, propanediol, butanediol, methylpropanediol, glycerol, diglycol, propyldiglycol, butyldiglycol, hexyleneglycol, ethylene glycol methyl ether, ethylene glycol ethyl ether,
  • Propylene glycol propyl ether dipropylene glycol monomethyl ether, dipropylene glycol monoethyl ether, methoxytriglycol, ethoxytriglycol, butoxytriglycol, 1-butoxyethoxy-2-propanol, 3-methyl-3-methoxybutanol, propylene glycol t-butyl ether, di-n-octyl ether and mixtures of two or more of these aforementioned solvents ,
  • the inventive Composition optionally contains an amino groups-free C2 to C4 alcohol having 1 to 3 hydroxyl groups, in particular ethanol and / or glycerol and / or 1, 2-propanediol.
  • composition of the invention necessarily contains at least one enzyme.
  • Variant is at the level of proteins the term corresponding to "mutant” at the level of the nucleic acids.
  • the precursor or parent molecules may be wild-type enzymes, that is, those obtainable from natural sources. They may also be enzymes which in themselves already represent variants, that is to say to the
  • Wildtype molecules have already been altered. These include, for example, point mutants, those with changes in the amino acid sequence, multiple positions or longer contiguous regions, or else hybrid molecules composed of complementary sections of various wild-type enzymes.
  • Amino acid substitutions are substitutions of one amino acid for another
  • position 320 substitution means that a variant has a different amino acid in the position that has the position 320 in the sequence of a reference protein. Usually, such substitutions occur at the DNA level via mutations
  • R320K means that the reference enzyme at position 320 has the amino acid arginine, while the variant under consideration has the amino acid lysine at the homologizable position.
  • 320K means that any that is, a normally given amino acid at a position corresponding to position 320 is usually replaced with a lysine which is in this molecule in the present molecule.
  • R320K, L means that the amino acid arginine is in position 320 is replaced by lysine or leucine.
  • R320X means that the amino acid arginine at position 320 is replaced with an essentially any other amino acid.
  • amino acid substitutions according to the invention designated by the present application are not limited to being the only substitutions in which the variant in question differs from the wild-type molecule. It is known in the art that the beneficial properties of single point mutations can complement each other. Thus, embodiments of the present invention include all variants which, in addition to other exchanges with the wild-type molecule, also comprise the exchanges according to the invention. Furthermore, it does not matter in principle in which order the relevant amino acid substitutions have been made, that is, whether a corresponding point mutant
  • the enzyme contains at least one protease.
  • a protease is an enzyme that cleaves peptide bonds by hydrolysis.
  • Each of the enzymes from class E.C. 3.4 falls within the scope of the invention (including each of the thirteen subclasses below).
  • the EC number corresponds to the Enzyme Nomenclature 1992 of NC-IUBMB, Academic Press, San Diego, Calif., Including supplements 1 to 5, published in Eur. J. Biochem. 1994, 223, 1-5; Eur. J. Biochem. 1995, 232, 1-6; Eur. J. Biochem. 1996, 237, 1-5; Eur. J. Biochem. 1997, 250, 1-6; and Eur. J. Biochem. 1999, 264, 610-650.
  • Subtilase names a subgroup of serine proteases.
  • the serine proteases or serine peptidases are a subset of the proteases that have serine in the active site of the enzyme that forms a covalent adduct with the substrate.
  • the subtilases and the subtilases (and the subtilases)
  • Serine proteases are characterized by having two more amino acid residues in the active site besides said serine with histidine and aspartame.
  • the subtilases can be divided into 6 subclasses, namely the subtilisin family, the thermitase family, the proteinase K family, the family of lantibiotic peptidases, the kexin family, and the pyrolysin family.
  • the proteases preferably excluded from the compositions according to the invention or preferably contained in reduced amounts are endopeptidases (EC 3.4.21).
  • proteolytic activity is present according to the invention if the enzyme has proteolytic activity (EC 3.4).
  • protease activity types are known: the three main types are:
  • the protease activity can be determined by the method described in Tenside, Vol. 7 (1970), pp. 125-132. It is accordingly stated in PE (protease units).
  • the protease activity of an enzyme can be determined according to customary standard methods, in particular using BSA as substrate (bovine albumin) and / or with the AAPF method.
  • Advantages of the use of this protease thus arise in particular with regard to the washing performance and / or the stability.
  • a surfactant composition comprising as an enzyme at least one protease comprising an amino acid sequence corresponding to that shown in SEQ ID NO. 1 amino acid sequence is identical over at least 70% of their total length and in the count according to SEQ ID NO. 1, the amino acid substitution R99E or R99D in combination with at least two others
  • protease Having amino acid substitutions selected from the group consisting of S3T, V4I and V199I.
  • Said protease is described in the document WO 2013/060621, as well as the method for the production of said protease, comprising the introduction of a
  • Amino acid substitutions selected from the group consisting of S3T, V4I and V199I, in the count according to SEQ ID NO. 1 into an initial protease corresponding to the amino acid sequence shown in SEQ ID NO. 1 indicated amino acid sequence over the total length of which is at least 70% identical.
  • a preferred protease within the meaning of the present patent application therefore comprises both the protease as such and a protease produced by a method according to the invention. All statements on the protease therefore relate both to the protease as a substance and to the corresponding processes, in particular production processes of the protease.
  • nucleic acids coding for these proteases, proteases or nucleic acids containing non-human host cells according to the invention and / or the protease production processes comprising the proteases according to the invention or the preparation process for proteases according to the invention are liquid
  • a modification according to the invention of position 99 namely an alteration R99E or R99D, in connection with a change to at least two of the positions 3, 4 and 199, namely S3T, V4I or V199I, in a protease which has an amino acid sequence as shown in SEQ ID NO. 1 amino acid sequence indicated at least 70% identical amino acid sequence, preferably causes an improved cleaning performance of this modified protease in detergents and cleaners on at least one protease-sensitive soiling.
  • Proteases according to the invention consequently enable an improved removal of at least one, preferably of several protease-sensitive stains on textiles and / or hard surfaces, for example crockery.
  • Particularly advantageous cleaning performances show preferred embodiments according to the invention
  • Preferred embodiments of said surfactant compositions with said preferred soil-specific protease achieve the advantageous cleaning performances at low temperatures between 10 ° C and 60 ° C, between 15 ° C and 50 ° C and between 20 ° C and 40 ° C. Consequently, particularly preferred embodiments of said
  • compositions provided with said preferred soil-specific protease whose cleaning performance targeted with regard to a soiling or more
  • Stains of similar type, in particular at temperatures of at most 25 ° C, particularly preferably at temperatures of at most 20 ° C is advantageous.
  • the spot focus of preferred embodiments of proteases of the invention is blood-borne
  • Surfactant composition preferably used proteases on a particular stability in detergents or cleaners, for example to surfactants and / or bleaches and / or to temperature influences, in particular to high temperatures, for example between 50 and 65 ° C, especially 60 ° C, and / or acidic or alkaline conditions and / or to pH changes and / or to denaturing or oxidizing agents and / or to proteolytic degradation and / or to a change in the redox ratios.
  • Such advantageous embodiments of proteases according to the invention consequently enable improved wash results on protease-sensitive soiling in a wide temperature range.
  • cleaning performance is understood to mean the whitening performance of one or more stains, in particular laundry or dishes.
  • both the washing or cleaning agent which comprises the protease or the washing or cleaning liquor formed by this agent, and the protease itself have a respective cleaning performance.
  • the cleaning performance of the enzyme thus contributes to the cleaning performance of the agent or the washing or cleaning liquor formed by the agent.
  • the cleaning performance is preferably determined as indicated below.
  • the said protease which can preferably be used according to the invention also has a proteolytic activity, that is to say it is capable of hydrolysing peptide bonds of a polypeptide or protein, in particular in a washing or cleaning agent.
  • a preferred protease according to the invention is therefore an enzyme which catalyzes the hydrolysis of peptide bonds and thereby is able to cleave peptides or proteins.
  • the protease preferred according to the invention is preferably a mature protease, ie the catalytically active molecule without signal and / or propeptide (s). Unless otherwise stated, the sequences given refer to each mature enzyme.
  • the protease comprises 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%, 90.5%, 91%, 91, 5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5% and 98.8%, and in the count according to SEQ ID NO.
  • Figure 1 has the amino acid substitution R99E in combination with at least two other amino acid substitutions selected from the group consisting of S3T, V4I and V199I.
  • the protease comprises 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%, 90.5%, 91%, 91, 5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5% and 98.8%, and in the count according to SEQ ID NO.
  • Figure 1 has the amino acid substitution R99D in combination with at least two other amino acid substitutions selected from the group consisting of S3T, V4I and V199I.
  • proteases according to the invention 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%, 90.5%, 91%, 91, 5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5% and 98.8%, and in the count according to SEQ ID NO. 1 the
  • Amino acid substitution R99E 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 R99E.
  • 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%, 90.5%, 91%, 91, 5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97, 5%, 98%, 98.5% and 98.8%, and in the count according to SEQ ID NO. 1 the
  • Amino acid substitution R99E 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, R99E and V199I.
  • 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%, 90.5%, 91%, 91, 5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5% and 98.8%, 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 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%, 90.5%, 91%, 91, 5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5% and 98.8%, 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.
  • 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%, 90.5%, 91%, 91, 5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5% and 98.8%, 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.
  • 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%, 90.5%, 91%, 91, 5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5% and 98.8%, and in the count according to SEQ ID NO. 1 the
  • proteases according to the invention are characterized in that they have the amino acid substitution R99E or R99D in combination with the three further amino acid substitutions S3T, V4I and V199I.
  • the following proteases are very particularly preferred in this regard:
  • 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%, 90.5%, 91%, 91, 5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98% and 98.5%, and in the count according to SEQ ID NO.
  • the protease of SEQ ID NO. 2 is a protease which can be used very particularly preferably in the surfactant composition according to the invention.
  • 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%, 90.5%, 91%, 91, 5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98% and 98.5%, and in the count according to SEQ ID NO.
  • proteases as described above which are furthermore located at position 21 1 in the count according to SEQ ID NO. 1 have the amino acid leucine (L).
  • sequence comparison is based on the BLAST algorithm established and commonly used in the prior art (see, for example, Altschul, SF, Gish, W., Miller, W., Myers, EW & Lipman, DJ. (1990) "Basic local alignment search Biol. 215: 403-410; and Altschul, Stephan F., Thomas L. Madden, Alejandro A. Schaffer, Jinghui Zhang, Hheng Zhang, Webb Miller, and David J.
  • Lipman (1997): "Gapped BLAST and PSI-BLAST: a new generation of protein database search programs"; Nucleic Acids Res., 25, pp.3389-3402) and is in principle accomplished by similar sequences of nucleotides or amino acids in the nucleic acid or amino acid sequences of each other be assigned. A tabular assignment of the respective positions is referred to as alignment.
  • Another algorithm available in the prior art is the FASTA algorithm. Sequence comparisons (alignments), in particular multiple sequence comparisons, are created with computer programs.
  • 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. Such areas often have identical functions. They 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 otherwise indicated, identity or homology information in the present application, however, refers to the total length of the particular nucleic acid or amino acid sequence indicated.
  • the protease is characterized in that its purification performance corresponds at least to that of a protease which comprises an amino acid sequence which corresponds to the amino acid sequence shown in SEQ ID NO. 2 corresponds to the amino acid sequence indicated, and / or at least corresponds to that of a protease, the one
  • Amino acid sequence comprising the in SEQ ID NO. 3 corresponds to the amino acid sequence, wherein the cleaning performance is determined in a washing system, the
  • Blood on cotton Product No. 1 1 1 available from the company Eidgenössische Material- und Anlagentician (EMPA) Test materials AG, St. Gallen, Switzerland, determined by measuring the Whiteness of the washed textiles, the washing process for 70 minutes at a temperature of 40 ° C and the water has a water hardness between 15.5 and 16.5 ° (German hardness).
  • the concentration of the protease in the detergent intended for this washing system is from 0.001-0, 1 wt .-%, preferably from 0.01 to 0.06 wt .-%, based on active protein.
  • liquid surfactant compositions according to the invention contain as enzyme at least one enzyme selected from ⁇ -amylase, cellulase, mannanase, lipase, pectate lyase.
  • the enzymes contained in a composition according to the invention can be adsorbed to carriers and / or embedded in encapsulating substances in order to protect them against premature inactivation.
  • compositions according to the invention may be added to the resulting enzymes in any form known in the art. These include in particular by
  • the enzymes can also be encapsulated, for example by
  • a, preferably natural polymer or in the form of capsules for example those in which the enzymes are entrapped as in a solidified gel, or in those of the core-shell type, in which an enzyme-containing core with a Water, air and / or chemical impermeable protective layer is coated.
  • further active ingredients for example stabilizers, emulsifiers, pigments, bleaches or dyes, may additionally be applied.
  • Such capsules are prepared by methods known per se, for example by shaking or
  • Roll granulation or applied in fluid-bed processes are advantageously, such granules, for example by applying polymeric film-forming agent, low in dust and storage stable due to the coating.
  • the liquid surfactant compositions preferably additionally contain at least one cellulase.
  • a cellulase is an enzyme.
  • synonymous terms may be used, especially endoglucanase, endo-1,4-beta-glucanase, carboxymethylcellulase, endo-1,4-beta-D-glucanase, beta-1,4-glucanase, beta-1,4-endoglucan hydrolase , Celludextrinase or Avicelase.
  • Crucial for determining whether an enzyme is a cellulase according to the invention is its ability to hydrolyze 1, 4-.beta.-D-glucosidic bonds in cellulose.
  • Cellulases (endoglucanases, EG) which can be synthesized according to the invention comprise, for example, the fungal cellulase preparation rich in endoglucanase (EG) or its derivatives Further developments by the company Novozymes under the trade name
  • 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
  • Ecostone® and Biotouch® which are based at least in part on the 20 kD EG from 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 lndiAge®Neutra.
  • variants of these enzymes obtainable by point mutations can be used according to the invention.
  • Particularly preferred cellulases are Thielavia terrestris cellulase variants disclosed in International Publication WO 98/12307, cellulases from Melanocarpus, in particular Melanocarpus albomyces disclosed in International Publication WO 97/14804, EGIII-type cellulases from Trichoderma reesei in European Patent Application EP 1 305 432 or variants obtainable therefrom, in particular those disclosed in European Patent Applications EP 1240525 and EP 1305432, as well as cellulases disclosed in International Publication Nos. WO 1992006165, WO 96/29397 and WO 02/099091.
  • the respective disclosure is therefore expressly referred to, or the disclosure content of which in this respect is therefore expressly included in the present patent application.
  • compositions according to the invention are characterized in that as additional cellulase at least one cellulase from Melanocarpus sp. or Myriococcum sp. 20K cellulase or those having homology in excess of 80% (more preferably greater than 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90%) , 5%, 91%, 91, 5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5 %, 97%, 97.5%, 98%, 98.5%, 99.0%, 99.1%, 99.2%, 99.3%, 99.4%, 99.5%, 99, 6%, 99.7%, 99.8%, 99.9%).
  • K20 cellulase is preferably used in amounts such that a composition of the present invention has a cellulolytic activity of from 1 NCU / g to 500 NCU / g (determinable by the hydrolysis of 1 wt% carboxymethylcellulose at 50 ° C and neutral pH and determination of the reducing Sugar by dinitrosalicylic acid as described by MJ Bailey, et al., Enzyme Microb., Technol., 3: 153 (1981); 1 NCU defines the amount of enzyme which produces reducing sugars in an amount corresponding to 1 nmol of glucose per second), in particular 2 NCU / g to 400 NCU / g and more preferably from 6 NCU / g to 200 NCU / g.
  • the composition according to the invention may optionally contain further cellulases.
  • a composition according to the invention preferably contains from 0.001 mg to 0.5 mg, in particular from 0.02 mg to 0.3 mg, of cellulolytic protein per gram of the total
  • the protein concentration can be determined by known methods, for example the bicinchonic acid method (BCA method, Pierce Chemical Co., Rockford, IL) or the biuret method (Gornall AG, CS Bardawill and MM David, J. Biol. Chem. 177, 751-766, 1948).
  • BCA method Pierce Chemical Co., Rockford, IL
  • biuret method Garnall AG, CS Bardawill and MM David, J. Biol. Chem. 177, 751-766, 1948.
  • first cellulase from Melanocarpus sp. or Myriococcum sp. 20K cellulase or those having homology in excess of 80% (more preferably greater than 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90%) , 5%, 91%, 91, 5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5 %, 97%, 97.5%, 98%, 98.5%, 99.0%, 99, 1%, 99.2%, 99.3%, 99.4%, 99.5%, 99, 6%, 99.7%, 99.8%, 99.9%) have at least one more of the first cellulase
  • Surfactant compositions additionally contain at least one lipase.
  • Lipase enzymes preferred according to the invention are selected from at least one enzyme of the group which is formed from triacylglycerol lipase (E.C 3.1 .1.3) and lipoprotein lipase (E.C 3.1.1.34) and monoglyceride lipase (E.C. 3.1.1.23).
  • compositions according to the invention are used in particular for this purpose.
  • lipases which are active in the alkaline medium are used in particular for this purpose.
  • the lipase preferably contained in a composition according to the invention is naturally present in a microorganism of the species Thermomyces lanuginosus or Rhizopus oryzae or Mucor javanicus or derived from the aforementioned naturally occurring lipases by mutagenesis.
  • the compositions according to the invention comprise at least one lipase naturally present in a microorganism of the species Thermomyces lanuginosus or naturally occurring in the above-mentioned
  • Thermomyces lanuginosus lipases derived by mutagenesis Thermomyces lanuginosus lipases derived by mutagenesis.
  • the lipase is a separate enzyme of the microorganism.
  • the lipase can thus be expressed in the microorganism from a nucleic acid sequence which is part of the chromosomal DNA of the microorganism in its wild-type form. It or the coding for them nucleic acid sequence is therefore present in the wild-type form of the microorganism and / or may be from the wild-type form of the
  • Microorganism can be isolated from this. In contrast, one would not be
  • Nucleic acid sequence was introduced by genetic engineering methods into the microorganism targeted, so that the microorganism would have been enriched to the lipase or the coding for them nucleic acid sequence.
  • a lipase naturally present in a microorganism of the species Thermomyces lanuginosus or Rhizopus oryzae or Mucor javanicus may well have been produced recombinantly from another organism.
  • the fungus Thermomyces lanuginosus (also known as Humicola lanuginosa) belongs to the class of Eurotiomycetes (subclass Eurotiomycetidae), herein to the order of the Eurotiales and herein to the family Trichocomaceae and the genus Thermomyces.
  • the fungus Rhizopus oryzae belongs to the class of Zygomycetes (subclass Incertae sedis), herein to the order Mucorales and here again to the family Mucoraceae and the genus Rhizopus.
  • the fungus Mucor javanicus also belongs to the class of Zygomycetes (subclass Incertae sedis), herein to the order Mucorales and here again to the family Mucoraceae, then herein to the genus Mucor.
  • the names Thermomyces lanuginosus, Rhizopus oryzae and Mucor javanicus are biological
  • Preferred lipases according to the invention are the lipase enzymes obtainable from the company Amano Pharmaceuticals under the names Lipase M-AP10®, Lipase LE® and Lipase F® (also Lipase JV®).
  • the Lipase F® is naturally present in Rhizopus oryzae.
  • the lipase M-AP10® is naturally present in Mucor javanicus.
  • compositions of a most preferred embodiment of the invention contain at least one lipase selected from at least one or more polypeptides having an amino acid sequence that is at least 90% (and more preferably at least 81%, 82%, 83%, 84%, 85%) %, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91, 5%, 92%, 92.5%, 93%, 93.5%, 94%, 94 , 5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99.0%, 99.1%, 99.2% , 99.3%, 99.4%, 99.5%, 99.6%, 99.7%, 99.8%, 99.9%) is identical to the wild type lipase from strain DSM 4109 Thermomyces lanuginosus. It is again preferred if, starting from said wild-type lipase from strain DSM 4109, at least the amino acid change N233R is present.
  • lipases derived from the wild-type lipase from the strain DSM 4109 are preferably usable according to the invention, which are selected from at least one lipase enzyme according to at least one of
  • compositions of the invention at least one lipase derived from the wild-type lipase of strain DSM 4109 in which at least one substitution of an electrically neutral or negatively charged amino acid by a positively charged amino acid has taken place from said wild-type lipase.
  • the charge is determined in water at pH 10.
  • Negative amino acids in the sense of the invention are E, D, Y and C.
  • Positively charged amino acids in the sense of the invention are R, K and H, in particular R and K.
  • Neutral amino acid in the sense of the invention are G, A, V, L, I. , P, F, W, S, T, M, N, Q and C when C forms a disulfide bond.
  • a most preferred lipase is commercially available under the trade name Lipex® from the company Novozymes (Denmark) and can advantageously be used in the cleaning compositions according to the invention.
  • Particularly preferred here is the lipase Lipex® 100 L (ex Novozymes A / S, Denmark).
  • Preferred compositions are characterized in that, based on the total weight of the composition, said Lipase enzyme from Lipex® 100 L in a total amount of 0.01 to 1.0% by weight, in particular 0.02 to 0.1% by weight. %, is included.
  • compositions of the invention may additionally contain at least one mannanase as enzyme.
  • mannanase as enzyme.
  • One in the composition of the invention (especially in a Mannanase contained within the scope of its mannanase activity catalyses the hydrolysis of 1, 4-beta-D-mannosidic bonds in mannans, galactomannans, glucomannans and galactoglucomannans according to the present invention as preferred washing and cleaning agents for textiles).
  • Said mannanase enzymes according to the invention are named according to enzyme nomenclature as E.C. Classified 3.2.1.78.
  • the mannanase activity of a polypeptide or enzyme can according to literature
  • Test methods are determined.
  • a test solution is placed in 4 mm diameter holes of an agar plate containing 0.2% by weight of AZGL galactomannan (carob), i.
  • compositions according to the invention include, for example, the mannanase, which is marketed under the name Mannaway® by the company Novozymes.
  • WO 99/64619 discloses examples of high total surfactant liquid protease-containing detergent compositions of at least 20% by weight which additionally comprise mannanase enzyme.
  • compositions according to the invention contain, based on the total weight of the composition, mannanase in a total amount of from 0.01 to 1.0% by weight, in particular from 0.02 to 0.1% by weight.
  • Mannanase polypeptides from strains of the Thermoanaerobacter group, such as Caldicellulosiruptor are preferably suitable according to the invention. Also useful in the invention are mannanase polypeptides of the fungi Humicola or Scytalidium, in particular the species Humicola insolens or Scytalidium thermophilum.
  • the mannanase enzyme compositions according to the invention comprise at least one mannanase polypeptide from Gram-positive alkalophilic strains of Bacillus, in particular selected from at least one member of the group from Bacillus subtilis, Bacillus lentus, Bacillus clausii, Bacillus agaradhaerens, Bacillus brevis, Bacillus stearothermophilus, Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus coagulans, Bacillus circulans, Bacillus lautus, Bacillus thuringiensis, Bacillus cheniformis, and Bacillus sp., more preferably selected from at least one member of the group from Bacillus sp.
  • a preferred mannanase of the invention is selected from at least one member of the group that is formed
  • polypeptides comprising an amino acid sequence which is at least 90% (more preferably at least 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94%) , 5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 99.0%, 99, 1%, 99.2% , 99.3%, 99.4%, 99.5%, 99.6%, 99.7% or 99.8%) Sequence identity to the polypeptide according to SEQ ID No.1 (cf.
  • polypeptides which are a fragment of (i).
  • said preferred mannanase in a total amount of 0.01 to 1, 0 wt .-%, in particular from 0.02 to 0, 1 wt .-%, each based on the total weight of the composition in the The composition of the invention is included.
  • the liquid surfactant composition of the invention contains, in addition to the preferred protease of the alkaline protease type from Bacillus lentus DSM 5483 or, in addition to the sufficiently similar protease (in terms of sequence identity), which has several of these changes in combination, additionally at least one ⁇ -amylase , ⁇ -Amylases (E.C. 3.2.1 .1) hydrolyze internal ⁇ -1, 4-glycosidic bonds of starch and starch-like polymers as an enzyme.
  • This ⁇ -amylase activity is measured, for example, according to the applications WO 97/03160 A1 and GB 1296839 in KNU (Kilo Novo Units). This is 1 KNU for the amount of enzyme, the 5.25 g of starch (available from Merck, Darmstadt, Germany) per hour at 37 ° C, pH 5.6 and in the presence of 0.0043 M
  • An alternative activity determination method is the so-called DNS method, which is described, for example, in the application WO 02/10356 A2. Thereafter, the oligosaccharides, disaccharides and glucose units released by the enzyme in the hydrolysis of starch are accompanied by oxidation of the reducing ends
  • Dinitrosalic acid detected.
  • the activity is obtained in ⁇ reducing sugars (based on maltose) per min and ml; This results in activity values in TAU.
  • the same enzyme can be determined by various methods, with the respective
  • Conversion factors may vary depending on the enzyme and thus must be determined by a standard. As an approximation one can calculate that 1 KNU corresponds to approx. 50 TAU. Another activity determination method is measurement using the Quick-Start ® test kit from Abbott, Abott Park, Illinois, USA.
  • Surfactant compositions is the cleaning of textiles. Because washing and cleaning agents for textiles predominantly have alkaline pH values, in particular a-amylases which are active in the alkaline medium are used for this purpose. Such are from microorganisms, that is Fungi or bacteria, especially those of the genera Aspergillus and Bacillus produced and secreted. Based on these natural enzymes, there is still a near-term
  • Examples of these are the ⁇ -amylases from Bacillus licheniformis, from B. amyloliquefaciens and from B. stearothermophilus, as well as their further developments improved for use in detergents or cleaners.
  • the enzyme from B. licheniformis is available from Novozymes under the name Termamyl ® and from Genencor under the name Purastar® ® ST.
  • ⁇ -amylases from other organisms are further developments available under the trade names Fungamyl.RTM ® by Novozymes of ⁇ -amylase from Aspergillus niger and A. oryzae.
  • Fungamyl.RTM ® Novozymes of ⁇ -amylase from Aspergillus niger and A. oryzae.
  • Another commercial product is, for example, the amylase LT®.
  • WO 96/23873 A1 describes in part several different point mutations in a total of more than 30 different positions in four different wild-type amylases and claims those for all amylases with at least 80% identity to one of these four; they are said to have altered enzymatic properties in terms of thermal stability, oxidation stability and calcium dependence.
  • the application WO 00/60060 A2 also names a plurality of possible amino acid substitutions in 10 different positions on the ⁇ -amylases from two different microorganisms and claims such for all amylases with a homology of at least 96% identity to them.
  • WO 01/66712 A2 finally, refers to 31 different, in part with the aforementioned identical amino acid positions that have been mutated in one of the two mentioned in the application WO 00/60060 A2 ⁇ -amylases.
  • WO 96/23873 A1 concretely suggests the possibility of substituting an M in position 9 according to the count of AA560 for an L in the abovementioned ⁇ -amylases, in position 202 M for L and in positions 182 and 183 ( or 183 and 184) to delete lying amino acids.
  • WO 00/60060 A2 discloses, inter alia, specifically the
  • Amino acid variation N 195X (that is, in principle against any other amino acid).
  • WO 01/66712 A2 discloses, inter alia, the amino acid variants R1 18K, G186X (including in particular the not relevant here G186R exchange), N299X (including in particular the not relevant here replacement N299A), R320K, E345R and R458K.
  • the liquid surfactant composition of the invention additionally contains at least one ⁇ -amylase , which has a higher activity at temperatures between 10 and 20 ° C, as the amylase with the trade name "Stainzyme 12 L" from Novozymes.
  • compositions preferred according to the invention comprise ⁇ -amylase in a total amount of 0.01 to 1.0% by weight, in particular 0.02 to 0.1% by weight.
  • liquid surfactant composition additionally contains at least one polyalkoxylated polyamine.
  • the polyalkoxylated polyamine in the context of the present invention and its individual aspects is a polymer having an N-atom-containing backbone which carries polyalkoxy groups on the N atoms.
  • the polyamine has at the ends (terminus and / or side chains) primary amino functions and internally preferably both secondary and tertiary amino functions; if appropriate, it may also have only secondary amino functions on the inside, so that the result is not a branched-chain but a linear polyamine.
  • the ratio of primary to secondary amino groups in the polyamine is preferably in the range from 1: 0.5 to 1: 1.5, in particular in the range from 1: 0.7 to 1: 1.
  • the ratio of primary to tertiary amino groups in the polyamine is preferably in the range from 1: 0.2 to 1: 1, in particular in the range from 1: 0.5 to 1: 0.8.
  • the polyamine has an average molecular weight in the range of 500 g / mol to 50,000 g / mol, in particular from 550 g / mol to 5000 g / mol.
  • the N atoms in the polyamine are separated from one another by alkylene groups, preferably by alkylene groups having 2 to 12 C atoms, in particular 2 to 6 C atoms, wherein not all alkylene groups must have the same C atom number. Particularly preferred are ethylene groups, 1, 2-propylene groups, 1, 3-propylene groups, and their
  • PEI polyethyleneimine
  • the primary amino functions in the polyamine can carry 1 or 2 polyalkoxy groups and the secondary amino functions 1 polyalkoxy group, although not every amino function must be alkoxy group-substituted.
  • the average number of alkoxy groups per The primary and secondary amino function in the polyalkoxylated polyamine is preferably 1 to 100, in particular 5 to 50.
  • the alkoxy groups in the polyalkoxylated polyamine are preferably polypropoxy groups which are bonded directly to N atoms, and / or polyethoxy groups which are attached to existing propoxy and bound to N atoms, which do not carry propoxy groups.
  • Polyethoxylated polyamines are obtained by reacting polyamines with ethylene oxide (EO for short).
  • EO ethylene oxide
  • the polyalkoxylated polyamines containing ethoxy and propoxy groups are preferably accessible by reaction of polyamines with propylene oxide (abbreviated to PO) and subsequent reaction with ethylene oxide.
  • PO propylene oxide
  • the average number of propoxy groups per primary and secondary amino function in the polyalkoxylated polyamine is preferably 1 to 40, in particular 5 to 20,
  • the average number of ethoxy groups per primary and secondary amino function in the polyalkoxylated polyamine is preferably 10 to 60, especially 15 to 30.
  • the terminal OH function polyalkoxy substituents in the polyalkoxylated polyamine may be partially or completely etherified with a C 1 -C 10, in particular C 1 -C 3, alkyl group.
  • Polyalkoxylated polyamines which are particularly preferred according to the invention can be selected from polyamine reacted with 45EO per primary and secondary amino function, PEI's reacted with 43EO per primary and secondary amino function, PEI's reacted with 15EO + 5PO per primary and secondary amino function, PEI's reacted with 15PO + 30EO per primary and secondary amino function secondary amino function, PEI's reacted with 5PO + 39.5EO per primary and secondary amino function, PEI's reacted with 5PO + 15EO per primary and secondary amino function, PEI's reacted with 10PO + 35EO per primary and secondary amino function, PEI's reacted with 15PO + 30EO per primary and secondary amino function secondary amino function and PEI's reacted with 15PO + 5EO per primary and secondary amino function.
  • a most preferred alkoxylated polyamine is PEI containing 10 to 20 nitrogen atoms reacted with 20 units of EO per primary or secondary amino function of the polyamine.
  • a further preferred subject of the invention is the use of polyalkoxylated
  • Polyamines obtainable by reaction of polyamines with ethylene oxide and
  • propylene oxide Be with ethylene oxide and propylene oxide
  • the proportion of propylene oxide in the total amount of the alkylene oxide is preferably 2 mol% to 18 mol%, especially 8 mol% to 15 mol%.
  • the liquid composition based on the total weight thereof, preferably contains polyalkoxylated polyamines in a total amount of from 0.1 to 10% by weight, in particular from 0.5 to 5.0% by weight.
  • the liquid surfactant compositions according to the invention may contain further ingredients which further improve the performance and / or aesthetic properties of the detergent.
  • the composition according to the invention preferably additionally contains one or more substances from the group of bleaches, complexing agents, builders, electrolytes, pH regulators, perfumes, perfume carriers, fluorescers, dyes, hydrotropes, foam inhibitors, silicone oils, polymeric thickeners, antiredeposition agents,
  • Anti-shrinkage agents include color transfer inhibitors, antimicrobial agents, germicides, fungicides, antioxidants, preservatives, corrosion inhibitors, antistatic agents, bittering agents, ironing aids, repellents and impregnating agents, swelling and anti-slip agents, plasticizing components and UV absorbers.
  • a polymeric thickener is understood according to the invention to mean a polymeric compound which has an average molar mass (weight average M w ) of more than 1500 g / mol and which, in an amount of 0.1 wt
  • composition increased.
  • a polymeric thickener apply according to the invention
  • polyacrylates include polyacrylate or polymethacrylate thickeners, such as, for example, the high molecular weight homopolymers of acrylic acid crosslinked with a polyalkenyl polyether, in particular an allyl ether of sucrose, pentaerythritol or propylene (INCI name according to the International Dictionary of Cosmetic Ingredients, The Cosmetic, Vol. Toiletry and Fragrance Association (CTFA): Carbomer), also known as
  • Carboxyvinyl polymers Such polyacrylic acids are i.a. from the company 3V Sigma under the trade name Polygel®, e.g. Polygel DA, and from the company Noveon under the trade name Polygel®, e.g. Polygel DA, and from the company Noveon under the trade name Polygel®, e.g. Polygel DA, and from the company Noveon under the trade name Polygel®, e.g. Polygel DA, and from the company Noveon under the
  • Carbopol® available, eg Carbopol 940 (molecular weight about 4,000,000), Carbopol 941 (molecular weight about 1 250,000) or Carbopol 934 (molecular weight about 3,000,000).
  • acrylic acid copolymers are included: (i) Copolymers of two or more monomers from the group of acrylic acid, methacrylic acid and their simple ester, preferably formed with C 1-4 -alkanols (INCI acrylates copolymer), for example the copolymers of Methacrylic acid, butyl acrylate and methyl methacrylate (CAS designation according to Chemical Abstracts Service: 25035-69-2) or of butyl acrylate and methyl methacrylate (CAS 25852-37-3) belong and, for example, the company Rohm & Haas under the trade names Aculyn® and Acusol® as well as from the company Degussa (Goldschmidt) under the trade name Tego® polymer, eg the ani
  • the liquid composition based on the total weight of the composition, comprises polymeric thickeners in a total amount of from 0 to 0.1% by weight, in particular from 0 to 0.05% by weight, more preferably from 0 to 0.01 Wt .-% contains. Most preferably, the composition is free of polymeric
  • a bleaching agent can serve all substances that destroy or absorb dyes by oxidation, reduction or adsorption and thereby discolor materials. These include, among others, hypohalite-containing bleach, hydrogen peroxide, perborate, percarbonate,
  • Peroxoacetic acid diperoxoazelaic acid, diperoxododecanedioic acid and oxidative enzyme systems.
  • Suitable builders which may be present in the composition according to the invention are in particular silicates, aluminum silicates (in particular zeolites), carbonates, salts of organic di- and polycarboxylic acids and mixtures of these substances.
  • Organic builders which may be present in the composition according to the invention are, for example, the polycarboxylic acids which can be used in the form of their sodium salts, polycarboxylic acids meaning those carboxylic acids which carry more than one acid function.
  • polycarboxylic acids meaning those carboxylic acids which carry more than one acid function.
  • these are citric acid, adipic acid, succinic acid, glutaric acid, malic acid, tartaric acid, maleic acid, fumaric acid, sugar acids, aminocarboxylic acids, and mixtures of these.
  • Preferred salts are the salts of polycarboxylic acids such as
  • Citric acid Citric acid, adipic acid, succinic acid, glutaric acid, tartaric acid, sugar acids and
  • polymeric polycarboxylates are suitable. These are, for example, the alkali metal salts of polyacrylic acid or polymethacrylic acid, for example, those having a molecular weight of 600 to 750,000 g / mol.
  • Suitable polymers are, in particular, polyacrylates, which preferably have a molecular weight of from 1, 000 to 15, 000 g / mol. Because of their superior solubility, the short-chain polyacrylates, which have molecular weights of from 1,000 to 10,000 g / mol, and particularly preferably from 1,000 to 5,000 g / mol, may again be preferred from this group. Also suitable are copolymeric polycarboxylates, in particular those of acrylic acid with methacrylic acid and of acrylic acid or methacrylic acid with maleic acid. To improve the water solubility, the polymers may also contain allylsulfonic acids, such as allyloxybenzenesulfonic acid and methallylsulfonic acid, as a monomer.
  • Soluble builders such as, for example, citric acid, or acrylic polymers having a molar mass of from 1,000 to 5,000 g / mol are preferably used in the liquid compositions according to the invention.
  • a second subject of the invention is the use of a liquid surfactant composition of the first subject of the invention in a process for textile laundering.
  • a third object of the invention is a process for textile washing, comprising the
  • a wash liquor is at least the total amount of the components used under (i) and (iii).
  • Processes for textile cleaning are generally distinguished by the fact that various cleaning-active substances are applied to the items to be cleaned and washed off after the contact time, or that the items to be cleaned are treated in any other way with a composition of the first subject of the invention or a solution of this composition. It is preferred according to the invention if, as part of a pretreatment of textiles, first at selected parts of the textile at least part of said liquid composition is applied directly and then after a contact time (preferably 30 to 300 seconds) the at least one solvent from step (ii ), the rest of the textiles from step (iii) and optionally the remainder of said liquid composition to provide the wash liquor.
  • a contact time preferably 30 to 300 seconds
  • washing liquor is supplied with the at least one solvent of the process according to the invention, then it is preferred according to the invention to combine one part by volume of the said liquid composition with 5 to 3000 parts by volume of the at least one solvent.
  • liquid detergent composition was prepared by mixing:
  • the detergents had acceptable rheology, were storage stable (no phase separation or turbidity), and the protease had high activity even after storage.

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  • Enzymes And Modification Thereof (AREA)

Abstract

L'invention concerne des compositions tensioactives liquides, comprenant, par rapport au poids total de la composition, a) une quantité totale de 2,0 à 8,5 % en poids de (alkyle en C9-C20)benzènesulfonate, et b) une quantité totale de 10,0 à 18,0 % en poids de R1-O-(CH2CH2O)n-SO3M, dans lequel R1 représente un groupe alkyle en C12-18, n représente un nombre de 2 à 3 et M représente un cation monovalent, et c) une quantité totale de 1,0 à 6,0 % en poids de R2-O-(CH2CH2O)m-SO3M', dans lequel R2 représente un groupe alkyle en C12-18 et M' représente un cation monovalent, et d) une quantité totale de 2,0 à 10,0 % en poids d'un tensioactif non ionique, et e) de l'eau, et f) au moins une enzyme, lesdites compositions tensioactives liquides possédant une rhéologie acceptable pour le consommateur, étant stables au stockage et appropriées idéalement à la stabilisation des enzymes, comme en particulier des protéases.
EP15790151.3A 2014-12-19 2015-11-05 Composition tensioactiveavec une combinaison tensioactive particulière et d'enzyme Active EP3234088B1 (fr)

Priority Applications (1)

Application Number Priority Date Filing Date Title
PL15790151T PL3234088T3 (pl) 2014-12-19 2015-11-05 Ciekła kompozycja środków powierzchniowo czynnych ze szczególną kombinacją środka powierzchniowo czynnego i enzymu

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
DE102014226681.5A DE102014226681A1 (de) 2014-12-19 2014-12-19 Flüssige Tensidzusammensetzung mit spezieller Tensidkombination und Enzym
PCT/EP2015/075794 WO2016096238A1 (fr) 2014-12-19 2015-11-05 Composition tensioactive liquide comprenant une combinaison de tensioactifs spécifique et une enzyme

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EP3234088A1 true EP3234088A1 (fr) 2017-10-25
EP3234088B1 EP3234088B1 (fr) 2021-07-14

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US (1) US20170292086A1 (fr)
EP (1) EP3234088B1 (fr)
CA (1) CA2970850C (fr)
DE (1) DE102014226681A1 (fr)
PL (1) PL3234088T3 (fr)
WO (1) WO2016096238A1 (fr)

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US11512264B2 (en) 2020-07-08 2022-11-29 The Procter & Gamble Company Liquid detergent composition

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Also Published As

Publication number Publication date
CA2970850C (fr) 2020-12-15
WO2016096238A1 (fr) 2016-06-23
DE102014226681A8 (de) 2016-08-04
CA2970850A1 (fr) 2016-06-23
US20170292086A1 (en) 2017-10-12
EP3234088B1 (fr) 2021-07-14
PL3234088T3 (pl) 2021-11-08
DE102014226681A1 (de) 2016-06-23

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