EP3083923A1 - Wasch- oder reinigungsmittel mit reduziertem tensidgehalt - Google Patents
Wasch- oder reinigungsmittel mit reduziertem tensidgehaltInfo
- Publication number
- EP3083923A1 EP3083923A1 EP14809627.4A EP14809627A EP3083923A1 EP 3083923 A1 EP3083923 A1 EP 3083923A1 EP 14809627 A EP14809627 A EP 14809627A EP 3083923 A1 EP3083923 A1 EP 3083923A1
- Authority
- EP
- European Patent Office
- Prior art keywords
- composition according
- liquid composition
- surfactant
- lipase
- total amount
- 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
Links
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- 230000001810 trypsinlike Effects 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 239000013598 vector Substances 0.000 description 1
- 239000010457 zeolite Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38618—Protease or amylase in liquid compositions only
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
Definitions
- the present invention relates to the cleaning and care of surfaces, in particular of textiles, and the provision of liquid compositions for this purpose.
- SRP Soil Release Polymers
- DTI Dye Transfer Inhibitor
- Applicant's object is to provide liquid compositions (in particular laundry or cleaning compositions for textiles) which have a reduced content of surfactant and nevertheless have excellent detergency.
- the graying of textiles is also to be prevented or almost completely contained.
- White laundry should also without the addition of a conventional optical brightener perceptibly strengthened and obtained over the surface to be cleaned seemingly homogeneous white.
- a first object of the invention is a liquid composition, in particular for the washing or cleaning of textiles containing
- composition of the invention is liquid at 20 ° C.
- the composition according to the invention contains water.
- compositions preferred according to the invention comprise water in an amount of from 2 to 90% by weight, in particular from 5 to 80% by weight, in each case based on the total weight of the composition.
- the detergent more than 5 wt .-%, preferably more than 15 wt .-% and particularly preferably more than 25 wt .-%, each based on the total amount of detergent, water.
- the detergents may be low-water detergents, the water content in a preferred embodiment being less than 10% by weight and more preferably less than 8% by weight, based in each case on the total liquid detergent. Low-water liquid compositions are
- nonaqueous solvents may be added to the detergent.
- Suitable non-aqueous solvents include mono- or polyhydric alcohols, alkanolamines or glycol ethers, provided that they are miscible with water in the specified concentration range.
- the 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, Ethylene glycol propyl ether, ethylene glycol mono-n-butyl ether, diethylene glycol methyl 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 thereof
- the inventive composition contains an alcohol, in particular ethanol and / or glycerol, in amounts of 0.5 and 5 wt .-%, based on the total composition.
- compositions at least one surfactant, more preferably a mixture of several surfactants from different classes.
- the total amount of surfactant between 0 and 16 wt .-%, in particular between 0, 1 and 13 wt .-%, preferably from 2.5 to 13 wt .-%, particularly preferably from 6 , 0 to 1 1, 0 wt .-% and most preferably from 3.0 to
- the surfactant used according to the invention is preferably at least one anionic surfactant.
- Suitable anionic surfactants in the compositions are all anionic
- surfactants are characterized by a water solubilizing, anionic group such as e.g. a carboxylate, sulfate, sulfonate or phosphate group and a lipophilic alkyl group of about 8 to 30 carbon atoms.
- anionic group such as e.g. a carboxylate, sulfate, sulfonate or phosphate group and a lipophilic alkyl group of about 8 to 30 carbon atoms.
- glycol or polyglycol ether groups, ester, ether and amide groups and hydroxyl groups may be present in the molecule.
- Suitable anionic surfactants are preferably present in the form of the sodium, potassium and ammonium as well as the mono-, di- and trialkanolammonium salts having 2 to 4 C atoms in the alkanol group.
- compositions contain, based on the total weight of the composition, anionic surfactant in a total amount of from 0.1 to 10.0% by weight, preferably from 2.0 to 9.0% by weight, particularly preferably from 4.0 to 7, 0% by weight. Should additional surfactants be included in addition, the amount of other surfactants and the amount of anionic surfactants should be chosen so that the previously defined total amount of surfactant is maintained and optionally preferably the total amount of anionic surfactants within one of the previously defined as preferred ranges.
- Preferred anionic surfactants in the compositions are alkyl sulfates,
- Alkylpolyglykolethersulfate and ether carboxylic acids each having 10 to 18 carbon atoms in the
- Alkyl group and up to 12 glycol ether groups in the molecule Alkyl group and up to 12 glycol ether groups in the molecule.
- compositions used according to the invention comprise at least one surfactant of the formula
- R is a linear or branched, substituted or unsubstituted alkyl, aryl or alkylaryl radical, preferably a linear, unsubstituted alkyl radical, more preferably a fatty alcohol radical.
- Preferred radicals R are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, eicosyl radicals and mixtures thereof, the representatives having an even number of carbon atoms are preferred.
- radicals R are derived from C 12 -C 18 -fatty alcohols, for example coconut 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.
- the index n stands for an integer from 1 to 50, preferably from 1 to 20 and especially from 2 to 10. Most preferably, n stands for the numbers 2, 3, 4, 5, 6, 7 or 8.
- X stands for a monovalent cation or the nth part of an n-valent cation, the alkali metal ions are preferred, and Na + or K + including Na, with Na + being extremely preferred. Additional cations X + can be selected from NH 4 + , Mg 2+ , Y 2 Ca 2+ 2 Mn 2+ , and mixtures thereof.
- compositions contain at least one anionic surfactant selected from fatty alcohol ether sulfates of formula A-1
- compositions contain based on the total amount of
- Composition 0.1 to 10 wt .-%, preferably 1, 0 to 7.5 wt .-%, more preferably 2.0 to 4.0 wt .-% fatty alcohol ether sulfate (s) (in each case in particular of the formula A1). If additional surfactants are additionally present, the amount of fatty alcohol ether sulfate (e) used should be selected within the preferred range (vide supra) in such a way that
- the previously defined total amount of surfactant is complied with and - Optionally preferred as the preferred defined total amount of anionic surfactants is maintained.
- compositions additionally or alternatively (in particular additionally) contain at least one surfactant of the formula (A-2)
- R 3 is a linear or branched, substituted or unsubstituted alkyl, aryl or alkylaryl radical and the grouping -A- for -O- or a chemical bond.
- certain radicals R 3 are preferred.
- R 3 is preferably a linear, unsubstituted alkyl radical, more preferably a fatty alcohol radical.
- Preferred radicals R are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, eicosyl radicals and mixtures thereof, where the representatives with even number of carbon atoms are preferred.
- Particularly preferred radicals R are derived from C 12 -C 18 -fatty alcohols, for example coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl or stearyl alcohol or C 10 -C 20 oxo alcohols.
- Y stands for a monovalent cation or the n-th part of an n-valent cation, the alkali metal ions being preferred, and Na + or K + being preferred, Na + being extremely preferred.
- Further cations Y + can be selected from NH 4 + , Mg 2+ , Y 2 Ca 2+ 2 Mn 2+ , and mixtures thereof.
- Such particularly preferred surfactants are selected from fatty alcohol sulfates of the formula A-2a
- compositions contain based on the total amount of
- Compositions 0, 1 to 10 wt .-%, preferably 0.5 to 7.5 wt .-%, more preferably 1, 0 to 3.0 wt .-% surfactant from the group comprising C9-i3-alkylbenzenesulfonates, olefinsulfonates, C12-18-alkanesulfonates ester sulfonates, alk (en) ylsulfate, and mixtures thereof (in particular the group of C9-i3-alkylbenzenesulfonates, preferably the group of formula (A2)).
- the amount of surfactants used is selected from the group consisting of C 9-13 -alkylbenzenesulfonates, olefin sulfonates, C 12 -11-alkanesulfonates, ester sulfonates, alk (en) ylsulfates, and mixtures thereof (in particular the group of C 9 -13).
- alkylbenzenesulfonates preferably the group according to formula (A2) to be selected within the preferred range of quantities (vide supra) such that
- R 3 is preferably a linear or branched unsubstituted alkylaryl radical.
- X is a monovalent cation or the nth part of an n-valent cation, the alkali metal ions being preferred, and Na + or K + being preferred, Na + being extremely preferred.
- Other cations X + can be selected from NhV,
- Such highly preferred surfactants are selected from linear or branched
- R ' and R " together contain from 9 to 19, preferably from 1 to 15, and in particular from 1 to 13, carbon atoms
- a particularly preferred representative can be described by the formula A-3a:
- 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
- soap (s) included characterized in that they - based on their weight - 0.1 to 1, 5 wt .-%, particularly preferably 0.2 to 1, 0 wt .-%, most preferably 0.3 to 0.8 wt .-% soap (s) included. If additional surfactants are additionally present, the amount of soap (s) used should be selected within the preferred range (vide supra) in such a way that
- compositions of this embodiment are optionally preferably characterized in that it contains one or more soaps (preferably - based on their weight - 0.1 to 1, 5 wt .-%, particularly preferably 0.2 to 1, 0 wt. %, most preferably from 0.3 to 0.8% by weight of soap (s)).
- soaps preferably - based on their weight - 0.1 to 1, 5 wt .-%, particularly preferably 0.2 to 1, 0 wt. %, most preferably from 0.3 to 0.8% by weight of soap (s)).
- Nonionic surfactant (s) used according to the invention compositions.
- 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,
- radicals R 2 are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, eicosyl radicals and mixtures thereof, where the representatives with even number of carbon atoms Atoms are 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 nonionic surfactants in certain amounts.
- Extremely preferred compositions according to the invention are characterized
- the total amount of nonionic surfactants based on the weight of the compositions, is 0, 1 to 10% by weight, preferably 0.5 to 7.5% by weight, more preferably 2.0 to 4.0% by weight. is.
- the amount of further surfactants and the amount of nonionic surfactants should be selected such that the previously defined total amount of surfactant is maintained and, optionally, preferably the total amount of nonionic surfactants is within one of the previously defined preferred ranges.
- compositions contain based on the total amount of
- compositions 0, 1 to 10 wt .-%, preferably 1, 0 to 7.5 wt .-%, more preferably 2.0 to 4.0% by weight of fatty alcohol ethoxylate (s) (especially of formula (C-1)). Should additional surfactants be included in addition, the total amount of used inventive
- compositions are based on the total weight of the composition
- anionic surfactant in a total amount of 0, 1 to 10.0 wt .-%, preferably from 2.0 to 9.0 wt .-%, particularly preferably from 4.0 to 7.0 wt .-%, and
- nonionic surfactant in a total amount of 0, 1 to 10 wt .-%, preferably 0.5 to 7.5 wt .-%, more preferably 2.0 to 4.0 wt .-%,
- the total amount of surfactant is between 0 and 16 wt .-%, in particular from 2.5 to 13 wt .-%, most preferably from 6.0 to 1 1, 0 wt .-%, is.
- R is a linear or branched, substituted or unsubstituted alkyl
- R 'and R together contain 9 to 19, preferably 1 to 15 and in particular 1 1 to 13 C atoms,
- AO independently of one another for an ethylene oxide (EO) or propylene oxide (PO)
- n, m independently of one another for integers from 1 to 50,
- X represents a monovalent cation or the nth part of an n-valent cation.
- surfactants i) and ii) have been described above as preferred surfactants a) of the formulas (A-1) and (A-3a), the surfactant iii) as the preferred surfactant having the formula (C-1).
- preferred Compositions of this embodiment are again characterized in that they additionally contain at least one soap.
- those compositions are preferred based on the weight of the composition
- R is a linear or branched, substituted or unsubstituted alkyl
- R 'and R together contain 9 to 19, preferably 1 to 15 and in particular 1 1 to 13 C atoms,
- AO independently of one another for an ethylene oxide (EO) or propylene oxide (PO)
- n, m independently of one another for integers from 1 to 50,
- X is a monovalent cation or the nth part of an n-valent cation, with the proviso that the total amount of surfactant is between 0 and 16% by weight, especially between 0, 1 and 13% by weight, most especially preferably from 3.0 to 10.0 wt .-%, is.
- surfactants i) and ii) have been described above as preferred surfactants a) of the formulas (A-1) and (A-3a), the surfactant iii) as the preferred surfactant having the formula (C-1). preferred
- compositions of this embodiment are again characterized in that they contain, based on their weight, from 0.1 to 1.5% by weight, particularly preferably from 0.2 to 1.0% by weight, very particularly preferably from 0.3 to 0.8 wt .-% soap (s) included.
- composition according to the invention furthermore necessarily contains a special combination of the three enzymes lipase, amylase and mannanase.
- lipase amylase
- mannanase a special combination of the three enzymes lipase, amylase and mannanase.
- Enzymes are 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 considered 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.
- sequence comparison is made by assigning similar sequences in the nucleotide sequences or amino acid sequences to each other.
- This sequence comparison is preferably 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 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).
- amino acids in the nucleic acid or amino acid sequences are assigned to each other.
- 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 usually with
- sequence comparisons and alignments are preferably created with the computer program Vector NTI® Suite 10.3 (Invitrogen Corporation, 1600 Faraday Avenue, Carlsbad, California, USA) with the default parameters specified.
- Amino acid sequences include conserved amino acid substitutions, ie, amino acids with similar chemical activity, as they usually perform similar chemical activities within the protein. Therefore, the similarity of the compared sequences may also be given in percent homology or percent similarity. Identity and / or Homology information can be found on whole polypeptides or genes or only on 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 only a few
- Nucleotides or amino acids include. Often, such small areas practice for the
- Fragments are understood as meaning all polypeptides, proteins or peptides which are smaller than corresponding comparison proteins or those which correspond to completely translated genes and, for example, can also be obtained synthetically. Because of your
- Amino acid sequences can be assigned to the relevant complete comparison proteins. For example, they may adopt the same spatial structures or perform proteolytic or partial activities, such as the complexation of a substrate. Fragments and deletion variants of starting proteins are in principle similar; while fragments are rather small fragments, the deletion mutants tend to lack only short regions (possibly only one or more amino acids). Thus, for example, it is possible to delete further single amino acids at the termini or in the loops of the enzyme, without thereby losing or reducing the enzymatic activity.
- enzymes refer to active protein.
- the protein concentration can be determined by known methods, for example the BCA method or the biuret method.
- compositions of the invention necessarily contain at least one lipase.
- a lipase present in the composition according to the invention (in particular in a textile washing and cleaning agent preferred according to the invention) has a lipolytic activity, that is, it is capable of hydrolysis (lipolysis) of lipids such as glycerides or cholesterol esters.
- This lipase activity is determined in the usual manner, preferably as described in Bruno Stellmach, "Determination Methods Enzymes for Pharmacy,
- lipase-containing samples are added to an olive oil emulsion in emulsifier-containing water and incubated at 30 ° C and pH 9.0 These are titrated continuously with 0.01 N sodium hydroxide solution over a period of 20 minutes using an autotitrator, so that the pH value remains constant (“pH-stat titration") the determination of lipase activity
- the method for measuring the lipase activity is the release of a dye from a suitable pNP-labeled substrate.
- Total weight of the composition Lipase in a total amount of 0.01 to 1, 0 wt .-%, in particular from 0.02 to 0.1 wt .-%, is included.
- 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 the cleaning of textiles. Because washing and cleaning agents for textiles predominantly have alkaline pH values, 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. More preferably, 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 Eurotiales and herein 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 Mucorjavanicus 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 was carried out 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.
- the very particularly preferred lipase in the compositions according to the invention comprises at least one lipase which, starting from said wild-type lipase from the strain DSM 4109 Thermomyces lanuginosus, has one of the following
- 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 necessarily contain at least one mannanase.
- Mannanase present in the composition according to the invention catalyzes, as part of its mannanase activity, the hydrolysis of 1,4-D-mannosidic bonds in mannans, galactomannans, glucomannans and galactoglucomannans.
- 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.
- 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. 1633, Bacillus sp. AAI12, Bacillus clausii, Bacillus agaradhaerens and Bacillus licheniformis.
- Bacillus subtilis Bacillus subtilis
- 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 (see Sequence Listing), and
- 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 fragment defined above under (ii) is understood as meaning all polypeptides, proteins or peptides which are smaller than the polypeptides covered under (i) or those which are completely translated correspond, and for example can be obtained synthetically. Due to their amino acid sequences, they can be assigned to the relevant complete proteins. For example, they may adopt the same structures or perform proteolytic or partial activities, such as the complexation of a substrate. Fragments and deletion variants of starting proteins are in principle similar; while fragments are rather small fragments, the deletion mutants tend to lack only short regions (possibly only one or more amino acids).
- the enzymatic activity of the mannanase is preferably not reduced or only to a small extent, in particular only up to a reduction of 15% of the activity of the parent enzyme (particularly preferred for mannanase according to SeqlD No. 1).
- the mannanase is selected from at least one member of the group formed from polypeptides comprising an amino acid sequence that 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 of positions 31 to 490 according to SEQ ID No.1 (see Sequence Listing).
- the polypeptides have 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 of positions 31 to 490 according to SEQ ID No.1 (cf. sequence Listing).
- polypeptides whose amino acid sequence is more than 99.0% identical to the sequence according to SEQ ID No.1.
- a preferred mannanase enzyme is disclosed according to claim 1 of WO 99/64619, further described in the specification of this WO-document and is thus selected from at least one mannanase enzyme selected from at least one member of the group that is formed out
- polypeptides which can be encoded by the mannanase enzyme-encoding portion of the DNA sequence cloned into the plasmid present in Escherichia coli DSM 12197,
- polypeptides comprising an amino acid sequence as shown at positions 33-340 of SEQ ID NO: 1 in WO 99/64619,
- polypeptides comprising an amino acid sequence as shown at positions 31-990 or positions 91-1470, each of SEQ ID NO: 1 in WO 99/64619, or iv) analogs of those in (i) or (ii) at least 90% (and 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%, 99.8%, 99.9%) have sequence identity to the polypeptide, or a fragment of (i), (ii) or (iii) are.
- sequence described in the context of the present invention under SEQ ID No.1 corresponds to the sequence disclosed in WO 99/64619 under SEQ ID No.2.
- mannanase enzymes mentioned as being preferred in WO 99/64619 are preferred in the sense of the composition according to the invention.
- compositions according to the invention necessarily contain 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).
- 1 KNU stands for the amount of enzyme which contains 5.25 g of starch (available from Merck,
- 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.
- compositions according to the invention are the cleaning of textiles. Because detergents and cleaners for textiles predominantly have alkaline pH values, in particular ⁇ -amylases which are active in the alkaline medium are used for this purpose. Such are produced and secreted by microorganisms, ie fungi or bacteria, especially those of the genera Aspergillus and Bacillus. Based on these natural enzymes, there remains an almost unmanageable wealth of variants that have been derived by mutagenesis and have specific advantages depending on the field of application.
- 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 these.
- 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 variations R1 18K, G186X (including in particular the not relevant here G 186R exchange), N299X (including in particular the not relevant here replacement N299A), R320K, E345R and R458K.
- 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.
- the agent according to the invention as ⁇ -amylase at least one polypeptide having an identity of at least 92% (and increasingly preferably at least 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%) of the sequence having the SEQ ID NO. 2 (see Sequence Listing).
- SEQ ID NO. 2 is identical to SEQ ID NO. WO 2005/108537 disclosed.
- the preferred ⁇ -amylase having the sequence of SEQ ID NO. 2 is a variant of the ⁇ -amylase AA349, which can be derived from this enzyme via the point or deletion mutations R1 18K, G 182, D 183, N 195F, R320K and R458K.
- the ⁇ -amylase AA349 as sequence under SEQ ID NO. 3 of the aforementioned application WO 2005/108537. It is identical at the amino acid level with the ⁇ -amylase AA560 as mentioned in the same application. According to this application, both wild-type enzymes are naturally produced by Bacillus spec / es strains, which are available under the numbers DSM 12648 and DSM 12649 from the German Collection of Microorganisms and Cell Cultures GmbH, Mascheroder Weg 1 b, 38124 Braunschweig (http: //www.dsmz .de) from the company
- compositions according to the invention comprise as ⁇ -amylase at least one polypeptide having an identity of at least 92%, (in particular at least 93%, preferably at least 95%, particularly preferably at least 96%, very particularly preferably at least 98%) to the sequence of SEQ ID NO. 2 in a total amount of 0.01 to 1, 0 wt .-%, in particular from 0.02 to 0, 1 wt .-%.
- the agents according to the invention contain as amylase enzyme at least one ⁇ -amylase enzyme which can be obtained from a starting ⁇ -amylase which can be homologated with the ⁇ -amylase AA560 via amino acid changes in the following positions: 9, 149, 182, 186, 202, 257, 295, 299, 323, 339, 345 and optionally further (in the count according to the ⁇ -amylase AA560). It is preferred if, starting from a starting ⁇ -amylase which can be homologated with the ⁇ -amylase AA560, at least the amino acid change M202L is present. According to the invention, the ⁇ -amylase AA560 from the microorganism deposited under DSM 12649 as reference enzyme with regard to the numbering of the positions is according to the invention
- any ⁇ -amylase AA560 (AA560) which can be homologized with the ⁇ -amylase AA560 (AA560) is any amylolytic enzyme which corresponds to the ⁇ -amylase AA560 (AA560), that is to say the amino acid sequence shown in SEQ ID NO. 4 ⁇ -amylase shown by WO 00/60060 A2
- Minimum homology value of 20% Ident2011 has, as can be determined for example according to the method given by D. J. Lipman and W. R. Pearson in Science 227 (1985), pp 1435-1441. More preferably, the molecule has an identity of 30, 40, 50, 60, 70, 80 or 90% to one of these two ⁇ -amylases.
- compositions preferred according to the invention contain said ⁇ -amylase in a total amount of from 0.01 to 1.0% by weight, in particular from 0.02 to 0.1% by weight.
- amylase enzyme is selected from at least one ⁇ -amylase which can be obtained from the ⁇ -amylase AA560 via the following amino acid changes:
- M202L is preferably selected among the amylases having the amino acid change.
- the ⁇ -amylases used in the compositions according to the invention can be produced by biotechnological methods known per se by suitable microorganisms, for example by filamentous fungi as transgenic expression hosts or preferably those of the genera Bacillus, because the parent enzymes AA349 and AA560 themselves are Bacillus enzymes .
- suitable microorganisms for example by filamentous fungi as transgenic expression hosts or preferably those of the genera Bacillus, because the parent enzymes AA349 and AA560 themselves are Bacillus enzymes .
- suitable microorganisms for example by filamentous fungi as transgenic expression hosts or preferably those of the genera Bacillus, because the parent enzymes AA349 and AA560 themselves are Bacillus enzymes .
- suitable microorganisms for example by filamentous fungi as transgenic expression hosts or preferably those of the genera Bacillus, because the parent enzymes AA349 and AA560 themselves are Bacillus enzymes .
- Single-stranded oligonucleotides are synthesized and hybridized with the single-stranded gene; subsequent DNA polymerization then yields corresponding point mutants. These genes are integrated into vectors by known methods and used to produce the desired expression hosts.
- the purification is conveniently carried out by established methods, for example by precipitation, sedimentation, concentration, filtration of the liquid phases, microfiltration, ultrafiltration, exposure to chemicals, such as precipitation, chromatographic steps, deodorization or suitable combinations of these steps.
- compositions according to the invention which contain at most very small amounts or no protease at all.
- protease in a total amount of 0 to 0.001 wt .-%, particularly preferably from 0 to 0.0005 wt .-%, most preferably from 0 to 0, 0001 wt .-%, most preferably from 0 to 0.00005 wt .-%.
- the compositions of the invention are free of protease.
- a protease is an enzyme that cleaves peptide bonds by hydrolysis.
- Each of the enzymes from class EC 3.4 is included according to the invention (comprising 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 characterized in that they contain, in addition to said serine, histidine and
- 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:
- protease activity can be described by the method described in Tenside, Volume 7 (1970), pp. 125-132
- 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.
- the liquid compositions additionally contain at least one cellulase.
- a cellulase is an enzyme.
- synonymous terms may be used, especially endoglucanase, endo-1, 4-beta-glucanase,
- 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
- 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.
- cellulases are Thielavia terrestris cellulase variants disclosed in International Publication WO 98/12307, cellulases from Melanocarpus, especially Melanocarpus albomyces, disclosed in International Publication WO 97/14804, EGIII-type cellulases from Trichoderma reesei, U.S. Patent Nos. 4,199,431; 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 means of 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.
- 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 as in a solidified gel, or in those of the core-shell type, in which an enzyme-containing core is coated with a water, air and / or chemical impermeable protective layer.
- 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.
- compositions according to the invention may contain further ingredients which further improve the performance and / or aesthetic properties of the detergent.
- inventive compositions according to the invention may contain further ingredients which further improve the performance and / or aesthetic properties of the detergent.
- Composition preferably additionally one or more substances from the group of bleaches, complexing agents, builders, electrolytes, pH adjusters, perfumes, perfume carriers, fluorescers, dyes, hydrotropes, foam inhibitors, silicone oils, antiredeposition agents, anti-shrinkage agents, anti-crease agents, color transfer inhibitors, antimicrobial agents, germicides, Fungicides, antioxidants, preservatives, corrosion inhibitors, antistatic agents, bittering agents, ironing auxiliaries, repellents and impregnating agents, swelling and anti-slip agents, softening components and UV absorbers.
- 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 Alka Ii 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.
- copolymeric polycarboxylates in particular those of acrylic acid with methacrylic acid and of acrylic acid or methacrylic acid with maleic acid.
- the polymers may also contain allylsulfonic acids, such as allyloxybenzenesulfonic acid and methallylsulfonic acid, as a monomer.
- liquid compositions according to the invention are preferably soluble builders, such as citric acid, or acrylic polymers having a molecular weight of 1,000 to
- liquid composition in particular for the cleaning of textiles containing
- (b1) at least one anionic surfactant of the formula R -O- (AO) n -SO 3 " X + , and
- R is a linear or branched, substituted or unsubstituted alkyl
- R 'and R together contain 9 to 19, preferably 1 to 15 and in particular 1 1 to 13 C atoms,
- AO independently of one another for an ethylene oxide (EO) or propylene oxide (PO)
- n, m independently of one another for integers from 1 to 50,
- X is a monovalent cation or the nth part of an n-valent cation
- enzyme having protease activity in a total amount of 0 to 0.005 wt.%, preferably of 0 to 0.001 wt.%, particularly preferably of 0 to 0.0005 wt.
- Total amount of surfactant between 0 and 16 wt .-%, in particular between 0, 1 and 13 wt .-%, most preferably from 3.0 to 10.0 wt .-%, is.
- the representatives (vide supra) of the above features (a) to (g), which were previously identified as preferred, are mutatis mutandis again, in particular the preferred amounts of the ingredients.
- a second subject of the invention is the use of a liquid composition of the first subject of the invention against the graying of textiles.
- a third subject of the invention is the use of a liquid composition according to any one of claims 1 to 17 for the cleaning of textiles.
- a fourth object of the invention is a process for textile cleaning, comprising
- a wash liquor is at least the total amount of the components listed 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.
- wash liquor is additionally fed component (ii) of the process according to the invention
- temperatures of 60 ° C or less, 40 ° C or less, 30 ° C or less or 20 ° C or less are employed. These temperature data refer to the temperatures used in the washing steps.
- compositions were prepared:
- compositions E1 according to the invention were prepared as further comparison compositions without the addition of lipase, without the addition of mannanase and without the addition of lipase and without mannanase, and the enzyme content was replaced by water.
- composition E1 according to the invention has the best anti-skid performance.
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- Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Wood Science & Technology (AREA)
- Organic Chemistry (AREA)
- Detergent Compositions (AREA)
Abstract
Description
Claims
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PL14809627T PL3083923T3 (pl) | 2013-12-20 | 2014-12-08 | Środek piorący lub czyszczący ze zredukowaną zawartością środka powierzchniowo czynnego |
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Application Number | Priority Date | Filing Date | Title |
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DE102013226835.1A DE102013226835A1 (de) | 2013-12-20 | 2013-12-20 | Wasch- oder Reinigungsmittel mit reduziertem Tensidgehalt |
PCT/EP2014/076874 WO2015091053A1 (de) | 2013-12-20 | 2014-12-08 | Wasch- oder reinigungsmittel mit reduziertem tensidgehalt |
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EP3083923A1 true EP3083923A1 (de) | 2016-10-26 |
EP3083923B1 EP3083923B1 (de) | 2019-02-06 |
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DE (1) | DE102013226835A1 (de) |
ES (1) | ES2718320T3 (de) |
PL (1) | PL3083923T3 (de) |
WO (1) | WO2015091053A1 (de) |
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CN113906124A (zh) * | 2019-06-28 | 2022-01-07 | 联合利华知识产权控股有限公司 | 洗涤剂组合物 |
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DE102014218064A1 (de) | 2014-09-10 | 2016-03-10 | Henkel Ag & Co. Kgaa | Vorrichtung zur Behandlung von Flecken sowie Verfahren zur Behandlung von Flecken unter Verwendung einer solchen Vorrichtung |
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GB1296839A (de) | 1969-05-29 | 1972-11-22 | ||
EP0877077B1 (de) | 1991-06-11 | 2010-05-26 | Genencor International, Inc. | Cellulasezusammensetzungen mit einem Defizit an Komponenten des Typs-CBH I enthaltende Reinigungsmittelzusammensetzungen |
AR000862A1 (es) | 1995-02-03 | 1997-08-06 | Novozymes As | Variantes de una ó-amilasa madre, un metodo para producir la misma, una estructura de adn y un vector de expresion, una celula transformada por dichaestructura de adn y vector, un aditivo para detergente, composicion detergente, una composicion para lavado de ropa y una composicion para la eliminacion del |
NZ303162A (en) | 1995-03-17 | 2000-01-28 | Novo Nordisk As | Enzyme preparations comprising an enzyme exhibiting endoglucanase activity appropriate for laundry compositions for textiles |
GB2303145A (en) | 1995-07-08 | 1997-02-12 | Procter & Gamble | Detergent compositions |
DK0857216T3 (en) | 1995-10-17 | 2014-12-15 | Ab Enzymes Oy | Cellulases, GENES ENCODING THEM AND USES THEREOF |
CN100362100C (zh) | 1996-09-17 | 2008-01-16 | 诺沃奇梅兹有限公司 | 纤维素酶变体 |
ATE528394T1 (de) | 1998-06-10 | 2011-10-15 | Novozymes As | Neuartige mannasen |
CN1234854C (zh) | 1999-03-31 | 2006-01-04 | 诺维信公司 | 具有碱性α-淀粉酶活性的多肽以及编码该多肽的核酸 |
JP4523178B2 (ja) | 1999-03-31 | 2010-08-11 | ノボザイムス アクティーゼルスカブ | リパーゼ変異体 |
WO2001046700A2 (en) | 1999-12-23 | 2001-06-28 | Pharmacia & Upjohn Company | Sodium channels as targets for amyloid beta |
CN101532000A (zh) | 2000-03-08 | 2009-09-16 | 诺维信公司 | 具有改变的特性的变体 |
SK912003A3 (en) | 2000-07-28 | 2003-07-01 | Henkel Kgaa | Novel amylolytic enzyme extracted from bacillus sp. A 7-7 (DSM 12368) and washing and cleaning agents containing this novel amylolytic enzyme |
AU2001280920A1 (en) | 2000-08-04 | 2002-02-18 | Genencor International, Inc. | Mutant trichoderma reesei egiii cellulases, dna encoding such egiii compositions and methods for obtaining same |
MXPA03011194A (es) | 2001-06-06 | 2004-02-26 | Novozymes As | Endo-beta-1,4-glucanasa. |
DE102004048591A1 (de) | 2004-04-27 | 2005-11-24 | Henkel Kgaa | Reinigungsmittel mit Klarspültensid und einer speziellen α-Amylase |
MX2013002248A (es) * | 2010-08-30 | 2013-05-09 | Novozymes As | Lavado con remojado concentrado. |
US20130284637A1 (en) * | 2012-04-30 | 2013-10-31 | Danisco Us Inc. | Unit-dose format perhydrolase systems |
-
2013
- 2013-12-20 DE DE102013226835.1A patent/DE102013226835A1/de not_active Withdrawn
-
2014
- 2014-12-08 WO PCT/EP2014/076874 patent/WO2015091053A1/de active Application Filing
- 2014-12-08 ES ES14809627T patent/ES2718320T3/es active Active
- 2014-12-08 PL PL14809627T patent/PL3083923T3/pl unknown
- 2014-12-08 EP EP14809627.4A patent/EP3083923B1/de active Active
Cited By (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN113906124A (zh) * | 2019-06-28 | 2022-01-07 | 联合利华知识产权控股有限公司 | 洗涤剂组合物 |
CN113906124B (zh) * | 2019-06-28 | 2024-08-02 | 联合利华知识产权控股有限公司 | 洗涤剂组合物 |
Also Published As
Publication number | Publication date |
---|---|
WO2015091053A1 (de) | 2015-06-25 |
EP3083923B1 (de) | 2019-02-06 |
ES2718320T3 (es) | 2019-07-01 |
DE102013226835A1 (de) | 2015-06-25 |
PL3083923T3 (pl) | 2019-09-30 |
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