DE102014225475A1 - Washing or cleaning agent with special a-amylase and defined viscosity - Google Patents

Abstract

Liquid compositions, in particular for the purification of textiles, comprising (a) at least one surfactant, (b) at least one α-amylase which is at least 89% and more preferably at least 89% of the sequence given in SEQ ID NO 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%, 99.5% and up to 100% is identical and in the count according to SEQ ID NO. 1 at one or more of positions 180, 181, 182, 183 and 184, with the proviso that the composition has a viscosity of less than 2000 mPas, in particular in the range of 100 to 700 mPas (Brookfield LVDV, 20 ° C, Spindle 2 or 3, 20 rpm).

Description

The present invention relates to the cleaning of surfaces, in particular textiles, and the provision of liquid compositions for this purpose.

Mostly one and the same washing and cleaning agent is used for the removal of a variety of stains on substrates. To meet the requirements of the greatest possible stain removal, detergents and cleaners include various active ingredients. The person skilled in the art knows, for example, stains which can be removed better by the use of enzymes, the so-called enzyme-sensitive soiling. For the removal of enzyme-sensitive soiling, washing or cleaning agents are therefore added in addition to the surfactants commonly used for soil removal, for example, the enzymes protease, lipase, amylase, mannanase.

Detergents or detergents often contain the enzyme α-amylase to remove starch-based stains. The activity of the amylase during the washing or cleaning process depends on various factors. In addition to the temperature and the pH of the washing or cleaning medium, the storage stability of the enzyme in the washing or cleaning agent is a decisive factor. The activity of the enzyme should always be guaranteed to a high degree for the period from the production of the washing or cleaning agent to the last use by the consumer.

The Applicant has therefore taken on the task to provide liquid compositions (especially laundry or cleaning compositions for textiles), which have excellent detergency with regard to the removal of starch-based stains. These effects should be achieved at the lowest possible application temperatures, in particular between 10 ° C and 40 ° C. Furthermore, the washing power caused by the enzyme should be retained as completely as possible over the storage period of the washing or cleaning agent.

• (a) mindestens ein Tensid,
• (b) mindestens eine α-Amylase, die zu der in SEQ ID NO.1 angegeben Sequenz über deren Gesamtlänge zu mindestens 89% und zunehmend bevorzugt zu mindestens 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%, 99,5% und bis zu 100% identisch ist und in der Zählung gemäß SEQ ID NO. 1 an einer oder mehreren der Positionen 180, 181, 182, 183 und 184 Deletionen aufweist,

mit der Maßgabe, dass die Zusammensetzung eine Viskosität von weniger als 2000 mPas (Brookfield LVDV, 20°C, Spindel 2 oder 3, 20 rpm) aufweist. A first object of the invention is a liquid composition, in particular for the washing or cleaning of textiles containing

• (a) at least one surfactant,
• (b) at least one α-amylase corresponding to the sequence given in SEQ ID NO.1 over its total length of at least 89% and increasingly preferably at least 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%, 99.5% and up to 100% identical and in the count according to SEQ ID NO. 1 has deletions at one or more of the positions 180, 181, 182, 183 and 184,

with the proviso that the composition has a viscosity of less than 2000 mPas (Brookfield LVDV, 20 ° C, spindle 2 or 3, 20 rpm).

The liquid compositions of the invention have excellent enzyme stability and detergency at temperatures of 10 to 40 ° C. Furthermore, the liquid compositions according to the invention are optimally suitable as pretreatment agents for direct application to the soiled areas of the substrate, in particular of the soiled textile, before the beginning of the washing process.

For the purposes of the invention, for the definition of a number range, which should be "between" two range limits, following the general usage, the range limits are not included. Number ranges defined from one range limit to another range limit include the range limits.

The composition of the invention is liquid at 25 ° C and 1013 mbar.

The composition of the invention necessarily has a viscosity of less than 2000 mPas, in particular in the range of 100 to 700 mPas (Brookfield LVDV, 20 ° C, spindle 2 or 3, 20 rpm). To determine the viscosity, first a viscosity measurement is carried out with spindle no. If the measurement result is more than 1200 mPas, another measurement with spindle 3 is performed and this measurement result with spindle 3 is used as the viscosity value.

To develop a cleaning or washing performance, the compositions of the invention contain at least one surfactant, more preferably a mixture of several surfactants from different classes.

It is preferred for the invention if the total amount of surfactant 2.0 to 70 wt .-%, preferably 5.0 to 60.0 wt .-%, more preferably from 10.0 to 40.0 wt .-% , particularly preferably from 15.0 to 36.0 wt .-%, each based on the total weight of the composition.

The surfactant used according to the invention is preferably at least one anionic surfactant.

Suitable anionic surfactants in the compositions are all anionic surfactants. These are characterized by a water-solubilizing, anionic group such as. As a carboxylate, sulfate, sulfonate or phosphate group and a lipophilic alkyl group having about 8 to 30 carbon atoms. In addition, 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.

Preferred compositions contain, based on the total weight of the composition, anionic surfactant in a total amount of from 1.0 to 35.0% by weight, preferably from 5.0 to 30.0% by weight, particularly preferably from 10.0 to 25, 0% by weight.

Preferred anionic surfactants in the compositions are alkyl sulfates, alkyl polyglycol ether sulfates 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.

Preferred compositions used according to the invention comprise at least one surfactant of the formula R ^{1 is} -O- (AO) _n -SO ₃ ^- X ⁺ .

In this formula, R ^{1 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 ¹ are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, eicosyl radicals and mixtures thereof, where the representatives with an even number of carbon atoms Atoms are preferred. Particularly preferred radicals R ¹ 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. Other cations X + may be selected from NH4 ^+, 1 / 2Zn ^2+, 1 / 2Mg ^2+, 1 / 2Ca ^2+, 1 / 2Mn ^2+, and mixtures thereof.

mit k = 11 bis 19, n = 2, 3, 4, 5, 6, 7 oder 8. Ganz besonders bevorzugte Vertreter sind Na-C_12-14 Fettalkoholethersulfate mit 2 EO (k = 11–13, n = 2 in Formel A-1). In summary, particularly preferred compositions contain at least one anionic surfactant selected from fatty alcohol ether sulfates of formula A-1

with k = 11 to 19, n = 2, 3, 4, 5, 6, 7 or 8. Very particularly preferred representatives are Na-C _12-14 fatty alcohol _ether sulfates with 2 EO (k = 11-13, n = 2 in formula A-1).

Preferred compositions contain, based on the total amount of the composition, from 1.0 to 15% by weight, preferably from 2.5 to 12.5% by weight, more preferably from 5.0 to 10.0% by weight, of fatty alcohol ether sulfate (e) ( in particular of the formula A1).

Further preferred compositions additionally or alternatively (in particular additionally) contain at least one surfactant of the formula (A-2) R ³ -A-SO ₃ ^- Y ⁺ (A-2).

In this formula, 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. In other words, sulfate (A = O) or sulfonate (A = chemical bond) surfactants can be described by the above formula. Depending on the choice of the group A, certain radicals R ^{3 are} preferred. In the sulfate surfactants (A = O), R ^{3 is} preferably a linear, unsubstituted alkyl radical, more preferably a fatty alcohol radical. Preferred radicals R ¹ are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, eicosyl radicals and mixtures thereof, where the representatives with an even number of carbon atoms Atoms are preferred. Particularly preferred radicals R ¹ 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. Other cations may be selected from Y + NH4 ^+, 1 / 2Zn ^2+, 1 / 2Mg ^2+, 1 / 2Ca ^2+, 1 / 2Mn ^2+, and mixtures thereof.

mit k = 11 bis 19. Ganz besonders bevorzugte Vertreter sind Na-C_12-14 Fettalkoholsulfate (k = 11–13 in Formel A-2a). Such particularly preferred surfactants are selected from fatty alcohol sulfates of the formula A-2a

with k = 11 to 19. Very particularly preferred representatives are Na-C _12-14 fatty alcohol sulfates (k = 11-13 in formula A-2a).

Further preferred compositions contain from 1.0 to 25.0% by weight, preferably 2.5 to 20.5% by weight, more preferably 5.0 to 20.0% by weight of surfactant, based on the total amount of the compositions group C ₉ comprising - ₁₃ alkyl benzene sulfonates, olefin sulfonates, C _12-18 -alkanesulphonates ester, alk (en) yl sulfates, and mixtures thereof (in particular the group of C _9-13 alkylbenzene sulfonates, preferably the group of formula (A2)) ,

In the case of the sulfonate surfactants (A = chemical bond), which are preferred over the sulfate surfactants of the above formula, R ^{3 is} preferably a linear or branched unsubstituted alkylaryl radical. Here, too, 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 + may be selected from NH4 ^+, 1 / 2Zn ^2+, 1 / 2Mg ^2+, 1 / 2Ca ^2+, 1 / 2Mn ^2+, and mixtures thereof.

in der R´ und R´´ zusammen 9 bis 19, vorzugsweise 11 bis 15 und insbesondere 11 bis 13 C-Atome enthalten. Ein ganz besonders bevorzugter Vertreter lässt sich durch die Formel A-3a beschreiben:

Such highly preferred surfactants are selected from linear or branched alkylbenzenesulfonates of the formula A-3

in which R 'and R "together contain 9 to 19, preferably 11 to 15 and in particular 11 to 13 carbon atoms. A particularly preferred representative can be described by the formula A-3a:

It has proved to be advantageous for the cold washing performance if the compositions additionally contain soap (s) as anionic surfactant. Soaps are the water-soluble sodium or potassium salts of the saturated and unsaturated fatty acids having 10 to 20 carbon atoms, the rosin acids of the rosin (yellow resin soaps) and the naphthenic acids, which are used as solid or semi-solid mixtures in the main Washing and cleaning purposes can be used. Sodium or potassium salts of the saturated and unsaturated fatty acids having 10 to 20 carbon atoms, in particular having 12 to 18 carbon atoms, are preferred soaps according to the invention. Particularly preferred compositions are characterized in that they contain, based on their weight, from 0.1 to 6% by weight, particularly preferably from 0.2 to 4.5% by weight, very particularly preferably from 0.3 to 4.1 Wt .-% soap (s) included.

• – mindestens einem Fettalkoholethersulfat der Formel A-1
  
  mit k = 11 bis 19, n = 2, 3, 4, 5, 6, 7 oder 8 (besonders bevorzugte Vertreter sind Na-C_12-14 Fettalkoholethersulfate mit 2 EO (k = 11–13, n = 2 in Formel A-1), und
• – mindestens einem linearen oder verzweigten Alkylbenzolsulfonaten der Formel A-3
  
  in der R´ und R´´ zusammen 9 bis 19, vorzugsweise 11 bis 15 und insbesondere 11 bis 13 C-Atome enthalten (insbesondere der obigen Formel (A-3a)),

in den erfindungsgemäßen Zusammensetzungen zu verwenden. Bevorzugte Zusammensetzungen dieser Ausführungsform sind dabei optional bevorzugt dadurch gekennzeichnet, dass sie eine oder mehrere Seifen enthält (bevorzugt – bezogen auf ihr Gewicht – 0,1 bis 6 Gew.-%, besonders bevorzugt 0,2 bis 4,5 Gew.-%, ganz besonders bevorzugt 0,3 bis 4,1 Gew.-% Seife(n)). To improve the solution of the technical problem, it is very particularly preferred according to the invention, a combination of

• At least one fatty alcohol ether sulfate of the formula A-1
  
  with k = 11 to 19, n = 2, 3, 4, 5, 6, 7 or 8 (particularly preferred representatives are Na-C _12-14 fatty alcohol _ether sulfates with 2 EO (k = 11-13, n = 2 in formula A) -1), and
• - At least one linear or branched alkylbenzenesulfonates of the formula A-3
  
  in which R 'and R "together contain 9 to 19, preferably 11 to 15 and in particular 11 to 13 C atoms (in particular of the above formula (A-3a)),

to use in the compositions of the invention. Preferred compositions of this embodiment are optionally preferably characterized in that it contains one or more soaps (preferably - based on their weight - 0.1 to 6 wt .-%, particularly preferably 0.2 to 4.5 wt .-%, most preferably 0.3 to 4.1% by weight soap (s)).

In addition to or in place of the anionic surfactant (s), the compositions used in the invention may contain nonionic surfactant (s).

With particular preference, the compositions contain at least one nonionic surfactant from the group of fatty alcohol ethoxylates, since these surfactants give high-performance compositions even at low washing temperatures and have excellent low-temperature stability in the case of liquid preparations.

Accordingly, preferred compositions additionally contain at least one nonionic surfactant of the formula R ^{2 is} -O- (AO) _m -H, in the
R ^{2 is} a linear or branched, substituted or unsubstituted alkyl, aryl or alkylaryl radical,
AO for an ethylene oxide (EO) or propylene oxide (PO) grouping,
m stands for integers from 1 to 50.

In the abovementioned formula, 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 radicals and mixtures thereof, where the representatives with even number of carbon atoms Atoms are preferred. Particularly preferred radicals R ² 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 subscript 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.

mit k = 11 bis 19, m = 2, 3, 4, 5, 6, 7 oder 8. Ganz besonders bevorzugte Vertreter sind C_12-18 Fettalkohole mit 7 EO (k = 11–17, m = 7 in Formel C-1). In summary, particularly preferred surfactants are selected from fatty alcohol ethoxylates of the formula C-1

with k = 11 to 19, m = 2, 3, 4, 5, 6, 7 or 8. Very particularly preferred representatives are C _12-18 fatty alcohols with 7 EO (k = 11-17, m = 7 in formula C- 1).

Particularly preferred compositions contain nonionic surfactants in certain amounts. Extremely preferred compositions according to the invention are characterized in that the total amount of nonionic surfactants, based on the weight of the compositions, is 1.0 to 25% by weight, preferably 2.5 to 20.0% by weight, more preferably 5.0 to 18 , 0 wt .-% is.

Further preferred compositions contain, based on the total amount of the compositions, 1.0 to 25% by weight, preferably 2.5 to 20.0% by weight, more preferably 5.0 to 18.0% by weight of fatty alcohol ethoxylate (s) (in particular of the formula (C-1)).

• – anionisches Tensid in einer Gesamtmenge von 1,0 bis 35,0 Gew.-%, bevorzugt von 5,0 bis 30,0 Gew.-%, besonders bevorzugt von 10,0 bis 25,0 Gew.-%, und
• – nichtionisches Tensid in einer Gesamtmenge von 1,0 bis 25 Gew.-%, vorzugsweise 2,5 bis 20,0 Gew.-%, weiter bevorzugt 5,0 bis 18,0 Gew.-%.

Preferred compositions are based on the total weight of the composition

• Anionic surfactant in a total amount of 1.0 to 35.0 wt .-%, preferably from 5.0 to 30.0 wt .-%, particularly preferably from 10.0 to 25.0 wt .-%, and
• - Nonionic surfactant in a total amount of 1.0 to 25 wt .-%, preferably 2.5 to 20.0 wt .-%, more preferably 5.0 to 18.0 wt .-%.

In this case, it is again preferred to use the preferred surfactants (most preferably in the amounts characterized as preferred). The amount of the specific anionic and nonionic surfactants in this case should be chosen so that the previously defined total amount of anionic surfactant and the previously defined total amount of nonionic surfactant is maintained.

• i) mindestens ein anionisches Tensid der Formel R¹-O-(AO)_n-SO₃ ^– X⁺, und
• ii) mindestens ein anionisches Tensid der Formel A-3
  
  und
• iii) mindestens ein nichtionisches Tensid der Formel R²-O-(AO)_m-H, enthalten, in denen R¹ für einen linearen oder verzweigten, substituierten oder unsubstituierten Alkyl-, Aryl- oder Alkylarylrest, R’ und R’’ zusammen 9 bis 19, vorzugsweise 11 bis 15 und insbesondere 11 bis 13 C-Atome enthalten, AO unabhängig voneinander für eine Ethylenoxid-(EO) oder Propylenoxid-(PO)Gruppierung, n, m unabhängig voneinander für ganze Zahlen von 1 bis 50, X für ein einwertiges Kation oder den n-ten Teil eines n-wertigen Kations stehen.

Die Tenside i) und ii) wurden weiter oben als bevorzugte Tenside a) mit den Formeln (A-1) und (A-3a) beschrieben, das Tensid iii) als bevorzugtes Tensid mit der Formel (C-1). Bevorzugte Zusammensetzungen dieser Ausführungsform sind dabei wiederum dadurch gekennzeichnet, dass sie zusätzlich mindesten eine Seife enthalten. According to a particularly preferred embodiment, those compositions are preferred which

• i) at least one anionic surfactant of the formula R ¹ -O- (AO) _n -SO ₃ ^- X ⁺ , and
• ii) at least one anionic surfactant of formula A-3
  
  and
• iii) at least one nonionic surfactant of the formula R ² -O- (AO) _m -H, in which R ^{1 is} a linear or branched, substituted or unsubstituted alkyl, aryl or alkylaryl radical, R 'and R "together Contain from 9 to 19, preferably 11 to 15 and in particular 11 to 13 C atoms, AO independently of one another for an ethylene oxide (EO) or propylene oxide (PO) grouping, n, m independently of one another for integers from 1 to 50, X represent a monovalent cation or the nth part of an n-valent cation.

The 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.

• i) in einer Gesamtmenge von 1,0 bis 15 Gew.-%, vorzugsweise 2,5 bis 12,5 Gew.-%, weiter bevorzugt 5,0 bis 10,0 Gew.-% mindestens ein anionisches Tensid der Formel R¹-O-(AO)_n-SO₃ ^– X⁺, und
• ii) in einer Gesamtmenge von 1,0 bis 25 Gew.-%, vorzugsweise 2,5 bis 20,5 Gew.-%, weiter bevorzugt 5,0 bis 20,0 Gew.-% mindestens ein anionisches Tensid der Formel A-3
  
  und
• iii) in einer Gesamtmenge von 1,0 bis 25 Gew.-%, vorzugsweise 2,5 bis 20,0 Gew.-%, weiter bevorzugt 5,0 bis 18,0 Gew.-% mindestens ein nichtionisches Tensid der Formel R²-O-(AO)_m-H, enthalten, in denen R¹ für einen linearen oder verzweigten, substituierten oder unsubstituierten Alkyl-, Aryl- oder Alkylarylrest, R’ und R’’ zusammen 9 bis 19, vorzugsweise 11 bis 15 und insbesondere 11 bis 13 C-Atome enthalten, AO unabhängig voneinander für eine Ethylenoxid-(EO) oder Propylenoxid-(PO)Gruppierung, n, m unabhängig voneinander für ganze Zahlen von 1 bis 50, X für ein einwertiges Kation oder den n-ten Teil eines n-wertigen Kations stehen,

Bevorzugte Zusammensetzungen dieser Ausführungsform sind dabei wiederum dadurch gekennzeichnet, dass sie – bezogen auf ihr Gewicht – 0,1 bis 6 Gew.-%, besonders bevorzugt 0,2 bis 4,5 Gew.-%, ganz besonders bevorzugt 0,3 bis 4,1 Gew.-% Seife(n) enthalten. In a most preferred embodiment, those compositions are preferred based on the weight of the composition

• i) in a total amount of 1.0 to 15 wt .-%, preferably 2.5 to 12.5 wt .-%, more preferably 5.0 to 10.0 wt .-% of at least one anionic surfactant of formula R ¹ -O- (AO) _n -SO ₃ ^- X ⁺ , and
• ii) in a total amount of 1.0 to 25% by weight, preferably 2.5 to 20.5% by weight, more preferably 5.0 to 20.0% by weight of at least one anionic surfactant of the formula A- 3
  
  and
• iii) in a total amount of 1.0 to 25 wt .-%, preferably 2.5 to 20.0 wt .-%, more preferably 5.0 to 18.0 wt .-% of at least one nonionic surfactant of formula R ² -O- (AO) _m -H, in which R ^{1 is} a linear or branched, substituted or unsubstituted alkyl, aryl or alkylaryl radical, R 'and R "together are 9 to 19, preferably 11 to 15 and in particular Contain 11 to 13 C atoms, AO independently of one another for an ethylene oxide (EO) or propylene oxide (PO) grouping, n, m independently of one another for integers from 1 to 50, X for a monovalent cation or the nth part of an N-valent cation,

Preferred compositions of this embodiment are again characterized in that they contain, based on their weight, from 0.1 to 6% by weight, particularly preferably from 0.2 to 4.5% by weight, very particularly preferably from 0.3 to 4 , 1 wt .-% soap (s) included.

The composition according to the invention may contain water as solvent. Compositions which are preferred according to the invention comprise water in an amount of from 0 to 55% by weight, in particular from 2 to 50% by weight, based in each case on the total weight of the composition. It is preferred that the detergent more than 5 wt .-%, preferably more than 15 wt .-% and particularly preferably more than 25 wt .-%, most preferably more than 40 wt .-%, each based on the Total amount of detergent, containing water. In this case, it is again particularly preferred if the detergent contains less than 55% by weight, preferably less than 50% by weight and especially preferably less than 45% by weight, in each case based on the total amount of detergent, of water.

Alternatively and particularly preferably, the detergents are water-poor detergents, the water content in a preferred embodiment being less than 35% by weight, more preferably less than 30% by weight, particularly preferably less than 10% by weight. , very particularly preferably less than 8 wt .-%, each based on the total liquid detergent is.

In addition to the components which are present according to the invention, non-aqueous solvents may be added to the liquid composition according to the invention. 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. Preferably, the solvents are selected from ethanol, n-propanol, i-propanol, butanols, glycol, propanediol, butanediol, methylpropanediol, glycerol, diglycol, propyldiglycol, butyldiglycol, hexylene glycol, ethylene glycol methyl ether, ethylene glycol ethyl ether, ethylene glycol propyl ether, ethylene glycol mono-n-butyl ether, diethylene glycol methyl ether, Diethylene glycol ethyl ether, propylene glycol methyl ether, propylene 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 thereof Solvent. However, it is preferred that the inventive composition contains an alcohol, in particular ethanol and / or glycerol and / or 1,2-propanediol, in amounts of 0.5 and 5 wt .-%, based on the total composition.

The liquid composition according to the invention furthermore necessarily contains a special α-amylase as enzyme. The following terms and definitions also apply in the context of the present application with regard to the definition of enzymes.

"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 have already been changed with respect to the wild-type molecules. 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.

In principle, the 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 starting 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 parent molecule, also comprise the exchanges according to the invention.

Furthermore, in principle, it does not matter in which order the relevant amino acid substitutions have been made, that is to say whether a corresponding point mutant is further developed according to the invention or if, for example, a variant according to the invention is produced from an initial molecule, which is further developed according to other teachings found in the prior art , It is also possible to carry out several exchanges simultaneously in a mutagenesis approach, for example according to the invention and others together.

The determination of the identity of nucleic acid or amino acid sequences is carried out according to the invention by a sequence comparison. Such a comparison is made by assigning similar sequences in the nucleotide sequences or amino acid sequences to each other. This sequence comparison is preferably carried out based on the BLAST algorithm established and commonly used in the prior art (cf., for example, US Pat Altschul, SF, Gish, W., Miller, W., Myers, EW & Lipman, DJ (1990) "Basic local alignment search tool." J. Mol. Biol. 215: 403-410 , and Altschul, Stephan F., Thomas L. Madden, Alejandro A. Schaffer, Jinghui Zhang, Hheng Zhang, Webb Miller, and David J. Lipman (1997): "Gapped BLAST and PSI-BLAST: a new generation of protein database search programs " ; Nucleic Acids Res., 25, pp. 3389-3402 ) and in principle takes place in that similar sequences of nucleotides or amino acids in the nucleic acid or amino acid sequences are assigned to one another. 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 created using computer programs. Frequently used, for example, the Clustal series (see, for example Chenna et al. (2003): Multiple sequence alignment with the Clustal series of programs. Nucleic Acid Research 31, 3497-3500 ), T-Coffee (cf., for example Notredame et al. (2000): T-Coffee: A novel method for multiple sequence alignments. J. Mol. Biol. 302, 205-217 ) or programs based on these programs or algorithms. For example, Clustal (cf. for example, Chenna et al. (2003): Multiple sequence alignment with the Clustal series of programs. Nucleic Acid Research 31, 3497-3500 ) or T-Coffee (cf., for example Notredame et al. (2000): T-Coffee: A novel method for multiple sequence alignments. J. Mol. Biol. 302, 205-217 ) as well as BLAST or FASTA for the database search, or programs based on these programs or algorithms. In the present invention, sequence comparisons and alignments (1600 Faraday Avenue, Carlsbad, California, United States Invitrogen Corporation) are preferred to the computer program Vector NTI ^® Suite 10.3 created with the preset default parameters.

Such a comparison allows a statement about the similarity of the compared sequences to each other. It is usually given in percent identity, that is, the proportion of identical nucleotides or amino acid residues at the same or in an alignment corresponding positions. The broader concept of homology involves conserved amino acid substitutions in the consideration of amino acid sequences, that is, amino acids with similar chemical activity, as these 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 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 stated otherwise, identity or homology information in the present application, however, refers to the total length of the respectively indicated nucleic acid or amino acid sequence.

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. Due to their amino acid sequences, they can be assigned to the respective complete comparison proteins. For example, they can assume 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.

All amounts of enzymes refer to active protein. The protein concentration can be determined by known methods, for example the BCA method or the biuret method. The determination of the active protein concentration can in this regard via a titration of the active sites using a suitable irreversible inhibitor (for proteases, for example, phenylmethylsulfonyl fluoride (PMSF)) and determination of the residual activity (see. Bender, M., et al., J. Am. Chem. Soc. 88, 24 (1966), p. 5890-5913 ) respectively.

In addition to the amino acid changes described above, enzymes according to the invention may have further amino acid changes, in particular amino acid substitutions, insertions or deletions. Such enzymes are, for example, by targeted genetic modification, i. by mutagenesis, further developed and optimized for specific applications or specific properties (for example, in terms of catalytic activity, stability, etc.). Furthermore, nucleic acids of the invention can be introduced into recombination approaches and thus used to generate completely novel enzymes or other polypeptides.

The goal is to introduce into the known molecules targeted mutations such as substitutions, insertions or deletions, for example, to improve the cleaning performance of enzymes of the invention. For this purpose, in particular the surface charges and / or the isoelectric point of the molecules and thereby their interactions with the substrate can be changed. Thus, for example, the net charge of the enzymes can be changed in order to influence the substrate binding, in particular for use in detergents and cleaners. Alternatively or additionally, one or more corresponding mutations can increase the stability of the amylase and thereby improve its purification performance. Advantageous properties of individual mutations, e.g. individual substitutions can complement each other. An amylase which has already been optimized with regard to certain properties, for example with respect to its stability towards surfactants and / or bleaches and / or other components, can therefore be further developed within the scope of the invention.

For the description of substitutions that concern exactly one amino acid position (amino acid substitutions), the following convention is used: first, the naturally occurring amino acid is designated in the form of the international one-letter code, followed by the associated sequence position and finally the inserted amino acid. Several exchanges within the same polypeptide chain are separated by slashes. For insertions, additional amino acids are named after the sequence position. For deletions, the missing amino acid is replaced by a symbol, such as a star or a dash. For example, A95G describes the substitution of alanine at position 95 by glycine, A95AG the insertion of glycine after the amino acid alanine at position 95 and A95 * the deletion of alanine at position 95. This nomenclature is known to those skilled in the art of enzyme technology.

The liquid composition according to the invention necessarily contains at least one α-amylase corresponding to the sequence given in SEQ ID NO.1 over at least 89% of its total length and increasingly preferably at least 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%, 99.5% and up to 100% identical and in the count according to SEQ ID NO. 1 at one or more of positions 180, 181, 182, 183 and 184 has deletions.

Amino acid positions which are given in the context of the present invention with the formulation "counting according to SEQ ID NO. 1" are as follows: The further amino acid positions are determined by an alignment of the amino acid sequence of an amylase according to the invention with the amino acid sequence as shown in SEQ ID NO. 1 is defined. Furthermore, the assignment of the positions depends on the mature (mature) protein. This assignment is also to be used in particular if the amino acid sequence of a protein according to the invention comprises a higher number of amino acid residues than the amylase in SEQ ID NO. 1. Starting from the mentioned positions in the amino acid sequence, the change positions in an amylase according to the invention are those which are just assigned to these positions in an alignment.

Particularly preferred is a deletion of two positions selected from 180 + 181, 181 + 182, 182 + 183 and 183 + 184, most preferably deletions at positions 183 + 184 in the count according to SEQ ID NO. 1, more preferably the deletions H183 * + G184 *.

Preferably, the α-amylase of the liquid composition according to the invention in the count according to SEQ ID NO. 1 further includes an amino acid substitution at one or more of 405, 421, 422, and 428. Most preferably, the substitutions are I405L; A421H, A422P and A428T.

In a particularly preferred embodiment, the α-amylase of the liquid composition according to the invention in the count according to SEQ ID NO. 1 the deletions H183 * + G184 * and additionally the substitutions I405L, A421H, A422P and A428T.

A further subject of the present invention is therefore a washing and cleaning agent containing a combination of an α-amylase and a protease, wherein the α-amylase is characterized in that it can be obtained from an amylase according to the invention as starting molecule by single or multiple conservative amino acid substitution is. The term "conservative amino acid substitution" means the replacement of one amino acid residue with another amino acid residue, which substitution does not result in a change in polarity or charge at the position of the exchanged amino acid, e.g. Example, the replacement of a nonpolar amino acid residue against another nonpolar amino acid residue. Conservative Aminosäure¬ substitutions in the context of the invention include, for example: G = A = S, I = V = L = M, D = E, N = Q, K = R, Y = F, S = T, G = A = I. = V = L = M = Y = F = W = P = S = T.

• (a) (i) aus einer α-Amylase als Ausgangsmolekül durch Fragmentierung, Deletions-, Insertions- oder Substitutionsmutagenese erhältlich ist, und (ii) besagtes Ausgangsmolekül zu der in SEQ ID NO.1 angegebenen Sequenz über deren Gesamtlänge zu mindestens 89% und zunehmend bevorzugt zu mindestens 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%, 99,5% und bis zu 100% identisch ist und in der Zählung gemäß SEQ ID NO. 1 an einer oder mehreren der Positionen 180, 181, 182, 183 und 184 Deletionen aufweist, und
• (b) eine Aminosäuresequenz umfasst, die über eine Länge von mindestens 50, 60, 70, 80, 90, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240, 250, 260, 270, 280, 290, 300, 310, 320, 330, 340, 350, 360, 370, 380, 390, 400, 410, 420, 430, 440, 450, 460, 470, 475, 480, 482, 484 oder 485 zusammenhängenden Aminosäuren mit dem Ausgangsmolekül übereinstimmt.

A further embodiment of the present invention is therefore a said liquid composition, in particular for washing or cleaning textiles, comprising at least one α-amylase, wherein the α-amylase is characterized in that it

• (a) (i) is obtainable from an α-amylase as the starting molecule by fragmentation, deletion, insertion or substitution mutagenesis, and (ii) said starting molecule to the sequence given in SEQ ID NO.1 at least 89% over its entire length more preferably at least 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%, 99.5% and up to 100% is identical and in the count according to SEQ ID NO. 1 at one or more of positions 180, 181, 182, 183 and 184 has deletions, and
• (b) an amino acid sequence having a length of at least 50, 60, 70, 80, 90, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230 , 240, 250, 260, 270, 280, 290, 300, 310, 320, 330, 340, 350, 360, 370, 380, 390, 400, 410, 420, 430, 440, 450, 460, 470, 475 , 480, 482, 484 or 485 contiguous amino acids matches the parent molecule.

For example, it is possible to delete individual amino acids at the termini or in the loops of the enzyme (starting molecule) without the proteolytic activity thereby being lost or reduced. Furthermore, such fragmentation, deletion, insertion or substitution mutagenesis can also reduce, for example, the allergenicity of the enzymes concerned and thus improve their overall applicability. Advantageously, the enzymes retain their proteolytic activity even after mutagenesis, i. their proteolytic activity is at least equal to that of the parent enzyme. Substitutions can also show beneficial effects. Both single and multiple contiguous amino acids can be substituted for other amino acids.

An amylase according to the invention may additionally be stabilized, in particular by one or more mutations, for example substitutions, or by coupling to a polymer. For an increase in the stability during storage and / or during use, for example in the washing process, causes the enzymatic activity lasts longer and thus the cleaning performance is improved. In principle, all stabilization options described in the prior art and / or appropriate considerations come into consideration. Preference is given to those stabilizations which are achieved by mutations of the enzyme itself, since such stabilizations do not require any further working steps following the recovery of the enzyme. Sequences suitable for this purpose are known from the prior art.

• – Veränderung der Bindung von Metallionen, insbesondere der Calcium-Bindungsstellen, beispielsweise durch Austauschen von einer oder mehreren der an der Calcium-Bindung beteiligten Aminosäure(n) gegen eine oder mehrere negativ geladene Aminosäuren und/oder durch Einführen von Sequenzveränderungen in mindestens einer der Folgen der beiden Aminosäuren Arginin/Glycin;
• – Schutz gegen den Einfluss von denaturierenden Agentien wie Tensiden durch Mutationen, die eine Veränderung der Aminosäuresequenz auf oder an der Oberfläche des Proteins bewirken;
• – Austausch von Aminosäuren, die nahe dem N-Terminus liegen, gegen solche, die vermutlich über nicht-kovalente Wechselwirkungen mit dem Rest des Moleküls in Kontakt treten und somit einen Beitrag zur Aufrechterhaltung der globulären Struktur leisten.

Other ways of stabilization z. B .:

• Changing the binding of metal ions, in particular the calcium binding sites, for example by exchanging one or more of the amino acid (s) involved in the calcium binding for one or more negatively charged amino acids and / or introducing sequence changes in at least one of the sequences the two amino acids arginine / glycine;
• Protection against the influence of denaturing agents, such as surfactants, on mutations causing an alteration of the amino acid sequence on or at the surface of the protein;
• Replacement of amino acids located near the N-terminus against those likely to contact non-covalent interactions with the rest of the molecule, thus contributing to the maintenance of the globular structure.

Preferred embodiments are those in which the enzyme is stabilized in several ways, as several stabilizing mutations act additive or synergistic.

A further embodiment of the invention is a said liquid composition, in particular for washing or cleaning textiles, comprising at least one α-amylase as described above, which is characterized in that it has at least one chemical modification. An amylase with such a change is called a derivative, i. the amylase is derivatized.

For the purposes of the present application, derivatives are understood as meaning those proteins whose pure amino acid chain has been chemically modified. Such derivatizations can be done, for example, in vivo by the host cell expressing the protein. In this regard, couplings of low molecular weight compounds such as lipids or oligosaccharides are particularly noteworthy. However, derivatizations can also be carried out in vitro, for example by the chemical transformation of a side chain of an amino acid or by covalent binding of another compound to the protein. For example, the coupling of amines to carboxyl groups of an enzyme to alter the isoelectric point is possible. Such another compound may also be another protein that is bound to a protein of the invention via bifunctional chemical compounds, for example. Similarly, derivatization is to be understood as meaning the covalent binding to a macromolecular carrier, or else a noncovalent inclusion in suitable macromolecular cage structures. Derivatizations may, for example, affect the substrate specificity or binding strength to the substrate or cause a temporary blockage of the enzymatic activity when the coupled substance is an inhibitor. This can be useful, for example, for the period of storage. Such modifications may further affect stability or enzymatic activity. They can also serve to reduce the allergenicity and / or immunogenicity of the protein and thus, for example, increase its skin compatibility. For example, couplings with macromolecular compounds, for example, polyethylene glycol, can improve the protein in terms of stability and / or skin tolerance.

Derivatives of a protein according to the invention can also be understood in the broadest sense to mean preparations of these proteins. Depending on the extraction, processing or preparation, a protein may be associated with various other substances, for example from the culture of the producing microorganisms. A protein may also have been deliberately added to other substances, for example to increase its storage stability. Therefore, all preparations of a protein according to the invention are also according to the invention. This is also independent of whether or not it actually exhibits this enzymatic activity in a particular preparation. Because it may be desired that it has no or only low activity during storage, and unfolds its enzymatic function only at the time of use. This can be controlled, for example, via appropriate accompanying substances.

The compositions according to the invention preferably additionally 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 way, preferably as described in US Pat Bruno Stellmach, "Methods of Determination Enzymes for Pharmacy, Food Chemistry, Technology, Biochemistry, Biology, Medicine" (Steinkopff Verlag Darmstadt, 1988, p. 172 ff) , In this case, lipase-containing samples are added to an olive oil emulsion in emulsifier-containing water and incubated at 30 ° C and pH 9.0. This fatty acids are released. These are done with an autotitrator over 20 min. titrated continuously with 0.01 N sodium hydroxide solution so that the pH remains constant ("pH-stat titration"). Based on the sodium hydroxide consumption, the determination of the lipase activity takes place by reference to a reference lipase sample. Another suitable method for measuring lipase activity is the release of a dye from a suitable pNP-labeled substrate.

Preferred compositions are characterized in that based on the 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 (EC 3.1.1.3) and lipoprotein lipase (EC 3.1.1.34) and monoglyceride lipase (EC 3.1.1.23).

The preferred field of use of the compositions according to the invention is 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.

Furthermore, 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 derived from the aforementioned naturally occurring lipases in Thermomyces lanuginosus by mutagenesis. Naturally present in this context means that 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 can be isolated from the wild-type form of the microorganism from this. In contrast to this, a lipase not present in the microorganism or the nucleic acid sequence coding for it would have been deliberately introduced into the microorganism with the aid of genetic engineering, so that the microorganism would have been enriched by the lipase or the nucleic acid sequence coding for it. However, 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 the biological species names within the respective genus.

According to preferred lipases are those of the company Amano Pharmaceuticals under the names Lipase M-AP10 ^®, Lipase LE ^® and Lipase F ^® lipase enzymes (including lipase JV ^®) available. For example, the ^{Lipase F®} is naturally present in Rhizopus oryzae. The lipase M-AP10 ^®, for example, naturally present in Mucor javanicus available

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.

In the context of a further embodiment, in particular those lipases derived from the wild-type lipase from 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 claims 1 to 13 of the document WO 00/60063 A1 , On the revelation pamphlet WO 00/60063 A1 is expressly referred to in its entirety.

It is particularly preferred to employ in the 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 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, if C forms a disulfide bridge. In the context of this embodiment of the invention, it is again preferred if, starting from the wild-type lipase from strain DSM 4109, at least one of the following amino acid substitutions is present in positions D96L, T213R and / or N233R, particularly preferably T213R and N233R.

It has been found that 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 strain DSM 4109 Thermomyces lanuginosus, has one of the following amino acid changes of numbers (L1) to (L41) as a single change (changes in brackets optional): (L1) T231R + N233R (L2) N94K + D96L + T231R + N233R + Q249R + 270P + 271G + 272L (L3) D96L + T231R + N233R (L4) G91A + E99K + T231R + N233R + Q249R (L5) (N33Q) + D96L + T231R + N233R + Q249R + 270 PGL (L6) R209P + T231R + N233R (L7) (N33Q) + E99N + N101S + T231R + N233R + Q249R + 270 PGL (L8) K24C + (N33Q) + D96S + T231R + N233R + Q249R + 270 PCL (L9) (N33Q) + G91A + E99K + T231R + N233R + Q249R + 270 PGL (L10) E1A + (N33Q) + G91A + E99K + T231R + N233R + Q249R + 270 PGL (L11) (N33Q) + G91A + E99K + G255R + T231R + N233R + Q249R + 270 PGL (L12) (N33Q) + G91A + E99K + T231R + N233R + T244R + Q249R + 270 PGL (L13) G91A + E99K + T231R + N233R + Q249R (L14) E87K + G91D + D96L + G225P + T231R + N233R + Q249R + N251D (L15) G91A + E99K + T231R + N233R + Q249R + 270AGVF (L16) G91A + E99K + T189G + T231R + N233R + Q249R (L17) D102G + T231R + N233R + Q249R (L18) T231R + N233R + Q249R + 270AGVF (L19) R209P + T231R + N233R (L20) N33Q + N94K + D96L + T231R + N233R + Q249R + 270PGLPFKRV (L21) N33Q + N94K + D96L + T231R + N233R + Q249R (L22) N33Q + D96S + T231R + N233R + Q249R (L23) N33Q + D96S + V228I + T231R + N233R + Q249R (L24) E1A + N33Q + G91A + E99K + T231R + N233R + Q249R + 270PGLPFKRV (L25) N33Q + S83T + E87K + G91A + E99K + T231R + N233R + Q249R + 270PGLPFKRV (L26) N33Q + G91A + E99K + T231R + N233R + Q249R + 270PGLPFKRV (L27) T231R + N233R + 270CP (L28) T231R + N233R + 270RE (L29) N33Q + E99N + N101S + T231R + N233R + Q249R + 270PGLPFKRV (L30) D62A + S83T + G91A + E99K + T231R + N233R + Q249R (L31) E99N + N101S + T231R + N233R + Q249R (L32) R84W + G91A + E99K + T231R + N233R + Q249R (L33) G91A + E99K + T231R + N233R + Q249R + 270SPG (L34) G91A + E99K + T231R + N233R + Q249R + 270VVVP (L35) G91A + E99K + T231R + N233R + Q249R + 270LLA88GRGGHR (L36) G91 A + E99K + T231R + N233R + Q249R + 270VTT (L37) G91A + E99K + T231R + N233R + Q249R + 270VLQ (L38) G91A + E99K + T231R + N233R + Q249R + 270T8T (L39) G91A + E99K + T231R + N233R + Q249R + 270LRI (L40) V60G + D62E + G91A + E99K + T231R + N233R + Q249R (L41) G91A + D96W + E99K + T231R + N233R + G263Q + L264A + 1265T + G2668 + T267A + L269N + 270AGGF8

Preferred compositions of this embodiment are characterized in that, based on the total weight of the composition, said polypeptide is present in a total amount of from 0.01 to 1.0% by weight, in particular from 0.02 to 0.1% by weight.

A highly preferred lipase is commercially available under the tradename Lipex ^® from the company Novozymes (Denmark) to relate and advantageously used in the inventive cleaning compositions. Particularly preferred here are the lipase Lipex ^® 100 L (ex Novozymes A / S, Denmark) is. Preferred compositions are characterized in that, based on the total weight of the composition of said lipase enzyme from Lipex ^® 100 L in a total amount of 0.01 to 1.0 wt .-%, in particular from 0.02 to 0.1 by weight %, is included.

The compositions according to the invention preferably additionally contain at least one mannanase. Mannanase present in the composition according to the invention (in particular in a textile washing and cleaning agent preferred according to the invention) catalyzes, as part of its mannanase activity, the hydrolysis of 1,4-β-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 be determined according to test methods known from the literature. Here, for example, a test solution in 4 mm diameter holes of an agar plate containing 0.2% by weight AZGL galactomannan (carob), ie substrate for the endo-1,4-beta-D-mannanase essay, available under catalog number I-AZGMA of Company Megazyme ( http://www.megazyme.com ), brought in.

Suitable compositions of the invention contain, for example, mannanase, which is marketed under the name Mannaway ^® from Novozymes.

Mannanase enzymes have been identified in numerous Bacillus organisms:
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.

Preferably, the 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.

It is particularly preferred according to the invention when 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. I633, Bacillus sp. AAI12, Bacillus clausii, Bacillus agaradhaerens and Bacillus licheniformis.

• i) Polypeptiden, die eine Aminosäuresequenz umfassen, die mindestens 90% (zunehmend bevorzugt mindestens 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% oder 99,8%) Sequenzidentität zu dem Polypeptid gemäß SEQ ID No.1 (vgl. Sequenzprotokoll), und
• ii) Polypeptiden, die ein Fragment von (i) sind.

Dabei ist es wiederum bevorzugt, wenn besagte bevorzugte Mannanase in einer Gesamtmenge von 0,01 bis 1,0 Gew.-%, insbesondere von 0,02 bis 0,1 Gew.-%, jeweils bezogen auf das Gesamtgewicht der Zusammensetzung, in der erfindungsgemäßen Zusammensetzung enthalten ist. A preferred mannanase of the invention is selected from at least one member of the group that is formed

• i) 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
• ii) polypeptides which are a fragment of (i).

It is again preferred if 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.

• i) Polypeptiden, die durch den für das Mannanaseenzym kodierenden Teil der DNA-Sequenz kodiert werden können, die in das in Escherichia coli DSM 12197 vorliegende Plasmid kloniert ist,
• ii) Polypeptiden, die eine Aminosäuresequenz umfassen, wie an den Positionen 33–340 von SEQ ID NO: 1 in WO 99/64619 gezeigt,
• iii) Polypeptiden, die eine Aminosäuresequenz umfassen, wie an den Positionen 31–990 oder den Positionen 91–1470, jeweils von SEQ ID NO: 1 in WO 99/64619 gezeigt, oder
• iv) Analoga der in (i) oder (ii) definierten Polypeptide, die mindestens 90% (und zunehmend bevorzugt zu mindestens 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%) Sequenzidentität zu dem Polypeptid haben, oder ein Fragment von (i), (ii) oder (iii) sind.

A preferred mannanase enzyme according to claim 1 of WO 99/64619 is described in more detail in the specification of this WO publication and is therefore selected from at least one mannanase enzyme selected from at least one member of the group that is formed

• i) 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,
• ii) polypeptides comprising an amino acid sequence as shown at positions 33-340 of SEQ ID NO: 1 in FIG WO 99/64619 shown,
• iii) polypeptides comprising an amino acid sequence, as at positions 31-990 or positions 91-1470, each of SEQ ID NO: 1 in FIG WO 99/64619 shown, or
• iv) Analogs of the polypeptides defined in (i) or (ii) containing 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).

For the interpretation of the features of the previously defined, according to the invention preferred mannanase enzymes (vide supra) is expressly the overall disclosure of WO 99/64619 to use fully. Likewise apply in the WO 99/64619 Preferred mannanase enzymes in the sense of the composition according to the invention are preferred.

Compositions which are preferred according to the invention additionally contain at least one 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. Furthermore, the subtilases (and 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).

"Protease activity" is present according to the invention if the enzyme has proteolytic activity (EC 3.4). Various types of protease activity are known: the three main types are: trypsin-like, with cleavage of the amide substrate following the amino acids Arg or Lys at P1; Chymotrypsin-like, with cleavage after one of the hydrophobic amino acids at P1; and elastase-like, wherein cleavage of the amide substrate after Ala occurs at P1.

The protease activity can after the in Surfactants, Vol. 7 (1970), pp. 125-132 method described. 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.

It is preferred according to the invention if the liquid compositions additionally contain at least one cellulase. A cellulase is an enzyme. For cellulases, 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-β-D-glucosidic bonds in cellulose.

According to the invention attachable cellulases (endoglucanases, EC) include, for example, fungal endoglucanase (EG) -rich cellulase preparation and developments thereof, which is offered by the company Novozymes under the trade name Celluzyme ^®. The products Endolase ^® and Carezyme ^® , also available from Novozymes, are based on the 50 kD EG or the 43 kD EG from Humicola insolens DSM 1800. Further commercial products of this company are Cellusoft ^® , Renozyme ^® and Celluclean ^® . Also usable are, for example cellulases, which are available from the company AB Enzymes, Finland, under the trade names Ecostone ^® and Biotouch ^®, and the at least partly based on the 20 kD EG Melanocarpus. Other cellulases from the company 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 by the company Danisco / Genencor under the trade name Puradax® ^® available. Further usable commercial products of the company Danisco / Genencor are "Genencor detergent cellulase L" and IndiAge ^® Neutra. Also variants of these enzymes obtainable by point mutations can be used according to the invention. Particularly preferred cellulases are Thielavia terrestris cellulase variants described in International Publication WO 98/12307 Cellulases from Melanocarpus, in particular Melanocarpus albomyces, disclosed in the international publication WO 97/14804 Cellulases of the EGIII type from Trichoderma reesei disclosed in the European patent application EP 1 305 432 and variations obtainable therefrom, in particular those disclosed in the European patent applications EP 1240525 and EP 1305432 , as well as cellulases, which are disclosed in international publications WO 1992006165 . WO 96/29397 and WO 02/099091 , 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.

Particularly preferred 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%).

The from Melanocarpus sp. or Myriococcum sp. 20K cellulase available is from the international patent application WO 97/14804 known. It has as described there a molecular weight of about 20 kDa and has at 50 ° C in the pH range of 4 to 9 at least 80% of their maximum activity, while still maintaining almost 50% of the maximum activity at pH 10. It can, as also described there, be isolated from Melanocarpus albomyces and produced in genetically engineered Trichoderma reseei transformants. Also useful in the present invention are cellulases having a homology of greater than 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%) to 20K cellulase.

K20 cellulase is preferably used in amounts such that a composition of the 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. In addition, 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 composition. 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 ).

It is again particularly preferred according to the invention, in addition to at least one 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%) to employ at least one other second cellulase different from the first cellulase.

In general, 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 the solid preparations obtained by granulation, extrusion or lyophilization, advantageously as concentrated as possible, low in water and / or added with stabilizers. In an alternative dosage form, the enzymes may also be encapsulated, for example by spray drying or extrusion of the enzyme solution together with 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 such Core-shell type in which an enzyme-containing core is coated with a water, air and / or chemical impermeable protective layer. In deposited layers, further active ingredients, for example stabilizers, emulsifiers, pigments, bleaches or dyes, may additionally be applied. Such capsules are applied by methods known per se, for example by shaking or rolling granulation or in fluid-bed processes. Advantageously, such granules, for example by applying polymeric film-forming agent, low in dust and storage stable due to the coating.

In addition, the compositions according to the invention may contain further ingredients which further improve the performance and / or aesthetic properties of the detergent. In the context of the present invention, the composition according to the invention preferably additionally contains one or more substances from the group of bleaching agents, complexing agents, builders, electrolytes, pH adjusters, perfumes, perfume carriers, fluorescers, dyes, hydrotropes, foam inhibitors, silicone oils, anti redeposition agents, anti-shrinkage agents, anti-crease agents , 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.

As 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. For example, 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, adipic acid, succinic acid, glutaric acid, tartaric acid, sugar acids and mixtures thereof.

As builders further 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 composition of the first subject of the invention for the stabilization of α-amylase, which leads to the sequence given in SEQ ID NO.1 over its total length to at least 89% and increasingly preferably to at least 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%, 99.5% and up to 100% is identical and in the count according to SEQ ID NO. 1 at one or more of positions 180, 181, 182, 183 and 184 has deletions.

A third subject of the invention is the use of a liquid composition of the first subject of the invention for the cleaning of textiles.

• (i) mindestens einer flüssigen Zusammensetzung des ersten Erfindungsgegenstandes,
• (ii) mindestens einem Lösemittel, insbesondere Wasser, und
• (iii) mindestens einem Textil.

A fourth object of the invention is a process for textile cleaning, comprising providing a wash liquor using at least the following components

• (i) at least one liquid composition of the first subject of the invention,
• (ii) at least one solvent, especially water, and
• (iii) at least one textile.

According to the invention, a wash liquor is at least the total amount of the components listed under (i) to (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, at least some of the liquid composition of the first subject of component (i) is applied directly to selected spots of the textile and then after a contact time (preferably from 30 to 300 seconds) at least one solvent of component (ii), the remainder of the textiles (iii) and optionally the remainder of the liquid composition of the first subject of the invention (i) are combined to provide the wash liquor.

If the wash liquor is additionally fed component (ii) of the process according to the invention, it is preferred according to the invention to combine one part by volume of component (i) with 5 to 3000 parts by volume of component (ii).

In the described methods, in various embodiments of 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.

Examples

The following compositions were prepared: 1. Liquid detergent: ingredient E1 amount in% by weight boric acid 1.0 Citric acid monohydrate 3.2 Fatty alcohol ether sulfate with 2 moles of EO 9.0 Fatty alcohol ether with 7 EO 9.0 alkyl benzene sulfonic acid 7.0 NaOH 3.1 Diethylenetriaminepenta (methylenephosphonic acid), heptasodium salt 0.7 fatty acid soap 4.0 ethanol 2.0 1,2-propanediol 5.7 Amylase (according to the invention) 0.44 mannanase 0.22 lipase 0.20 cellulase 0.15 protease 0.65 Perfume 1.3 water Ad 100 viscosity 150 mPas

The detergent exhibited excellent stability of the amylase.

This is followed by a sequence protocol according to WIPO St. 25. This can be downloaded from the official publication platform of the DPMA.

QUOTES INCLUDE IN THE DESCRIPTION

This list of the documents listed by the applicant has been generated automatically and is included solely for the better information of the reader. The list is not part of the German patent or utility model application. The DPMA assumes no liability for any errors or omissions.

Cited patent literature

• WO 00/60063 A1 [0077, 0077]
• WO 99/64619 [0085, 0090, 0090, 0090, 0091, 0091]
• WO 98/12307 A [0097]
• WO 97/14804 A [0097]
• EP 1305432 [0097, 0097]
• EP 1240525 [0097]
• WO 1992006165 A [0097]
• WO 96/29397 [0097]
• WO 02/099091 A [0097]
• WO 9714804 [0099]

Cited non-patent literature

• Altschul, SF, Gish, W., Miller, W., Myers, EW & Lipman, DJ (1990) "Basic local alignment search tool." Biol. 215: 403-410 [0048]
• 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 [0048]
• Nucleic Acids Res., 25, pp. 3389-3402 [0048]
• Chenna et al. (2003): Multiple sequence alignment with the Clustal series of programs. Nucleic Acid Research 31, 3497-3500 [0048]
• Notredame et al. (2000): T-Coffee: A novel method for multiple sequence alignments. Biol. 302, 205-217 [0048]
• for example, Chenna et al. (2003): Multiple sequence alignment with the Clustal series of programs. Nucleic Acid Research 31, 3497-3500 [0048]
• Notredame et al. (2000): T-Coffee: A novel method for multiple sequence alignments. Biol. 302, 205-217 [0048]
• Bender, M., et al., J. Am. Chem. Soc. 88, 24 (1966), pp. 5890-5913 [0051]
• Bruno Stellmach, "Methods of Determination Enzymes for Pharmacy, Food Chemistry, Technology, Biochemistry, Biology, Medicine" (Steinkopff Verlag Darmstadt, 1988, p. 172 ff) [0069]
• http://www.megazyme.com [0083]
• 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 [0092]
• Eur. J. Biochem. 1995, 232, 1-6; Eur. J. Biochem. 1996, 237, 1-5 [0092]
• Eur. J. Biochem. 1997, 250, 1-6 [0092]
• and Eur. J. Biochem. 1999, 264, 610-650 [0092]
• Surfactants, Vol. 7 (1970), pp. 125-132 [0095]
• Gornall AG, CS Bardawill and MM David, J. Biol. Chem. 177, 751-766, 1948 [0101]

Claims (14)

 Liquid composition, in particular for the cleaning of textiles, containing (a) at least one surfactant, (b) at least one α-amylase corresponding to the sequence given in SEQ ID NO.1 over its total length of at least 89% and increasingly preferably at least 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%, 99.5% and up to 100% identical and in the count according to SEQ ID NO. 1 has deletions at one or more of the positions 180, 181, 182, 183 and 184, with the proviso that the composition has a viscosity of less than 2000 mPas, in particular in the range of 100 to 700 mPas, (Brookfield LVDV, 20 ° C, spindle 2 or 3, 20 rpm). Liquid composition according to claim 1, characterized in that based on the total weight of the composition, surfactant in a total amount of 2.0 to 70.0 wt .-%, preferably from 5.0 to 55.0 wt .-%, particularly preferably of 5.0 to 30.0 wt .-%, is included. Liquid composition according to one of Claims 1 or 2, characterized in that the anionic surfactant comprises at least one surfactant of the formula (A-3),

in which R 'and R "together contain 9 to 19, preferably 11 to 15 and in particular 11 to 13 C atoms, Liquid composition according to one of claims 1 to 3, characterized in that as anionic surfactant at least one fatty alcohol ether sulfate of formula A-1

with k = 11 to 19, n = 2, 3, 4, 5, 6, 7 or 8 is included. Liquid composition according to one of claims 1 to 4, characterized in that the surfactant is at least one nonionic surfactant. Liquid composition according to one of Claims 1 to 5, characterized in that the amylase deletions are selected from at least two positions selected from the positions 180 + 181, 181 + 182, 182 + 183 and 183 + 184 in the counting according to SEQ ID NO. 1, and most preferably at positions 183 + 184 in the count according to SEQ ID NO. 1 has. A liquid composition according to any one of claims 1 to 6, characterized in that the amylase deletions H183 * + G184 * according to the numbering according to SEQ ID NO. 1 has. Liquid composition according to one of claims 1 to 7, characterized in that the amylase in the count according to SEQ ID NO. 1 further comprises amino acid substitutions at one or more of positions 405, 421, 422 and 428. Liquid composition according to one of claims 1 to 8, characterized in that the amylase in the count according to SEQ ID NO. 1 the substitutions I405L; A421H, A422P and A428T. Liquid composition according to one of claims 1 to 9, characterized in that in addition at least one protease is contained. A liquid composition according to any one of claims 1 to 10, characterized in that additionally at least one lipase is selected, selected from one or more polypeptides with a Amino acid sequence which is at least 90% identical to the wild-type lipase from strain DSM 4109 Thermomyces lanuginosus. Liquid composition according to claim 11, characterized in that it contains at least one lipase selected from one or more polypeptides having an amino acid sequence derived from the wild-type lipase of strain DSM 4109, in which at least one of the following amino acid substitutions in positions D96L and / or T213R and / or N233R, preferably at least T213R and N233R, is present.  A process for textile cleaning, comprising providing a wash liquor using at least the following components (i) at least one liquid composition according to any one of claims 2 to 12, (ii) at least one solvent, especially water, and (iii) at least one textile. A method according to claim 13, characterized in that as part of a pretreatment of textiles first at selected spots of at least one textile at least a portion of the liquid composition (i) is applied directly and then after a contact time, the at least one solvent of component (ii), the rest of the textiles (iii) and optionally the remainder of the liquid composition (i) are combined to provide the wash liquor.