The present invention relates to the cleaning of surfaces, particularly of textiles, as well as to the provision of liquid compositions for this purpose.

Usually, one and the same detergent composition is used to remove a wide variety of contaminants on substrates. In order to meet demands for the greatest possible effective removal of stains, detergents compositions contain a wide variety of active ingredients. A person skilled in the art is familiar with contaminants, for example, that can be better removed through the use of enzymes - so-called enzyme- sensitive contaminants. Therefore, in addition to the surfactants that are commonly used for soil removal of enzyme-sensitive contaminants, enzymes, for example selected from protease, lipase, amylase, and/or mannanase, are additionally added to detergents compositions.

The activity of the enzymes during the washing or cleaning process depends on various factors. Besides the temperature and the pH value of the detergent or cleaning agent, the storage stability of the enzyme in the detergent composition is a crucial factor. A high degree of enzyme activity should also be ensured for the entire period of time from the production of the detergent composition through the last use by the consumer.

It was therefore the applicant's objective to provide liquid detergent compositions (liquid laundry detergent compositions) that have outstanding washing performance. These effects are to be achieved at application temperatures that are as low as possible, particularly between 10 °C and 40 °C. Furthermore, the washing performance provided by the enzyme should be sustained to the greatest possible extent over the storage period of the detergent or cleaning agent.

The foam level of a liquid detergent formulation during the use in an automatic washing machine is typically controlled by the addition of soap. High soap levels of 3 wt.% or more are frequently used to reduce the foaming power of the wash liquor. On the other side a high soap level is detrimental to a good formula stability. Higher soap levels lead to formula instabilities upon storage especially at lower temperatures (e.g. 0°C). Alternatively, a reduction of the foam level by reducing the overall surfactant level of the formula leads to a general reduction of the stain removal performance, which is not desired. It was therefore another objective of the invention to combine an outstanding washing performance with a low foam level of the wash liquor and a good stability of the overall liquid detergent composition upon storage at low temperatures.

A first object of the invention is a liquid detergent composition, particularly for cleaning textiles, containing based on the total weight of the composition

(a) a total amount of 5.5 to 6.5 wt.% of at least one anionic surfactant of the alkyl polyglycol ether sulfate-type of the formula (A)

R -0-(AO)n-S0 ₃ - X ⁺ (A)

wherein

R is selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, and eicosyl residues,

AO stands for an ethylene oxide (EO) or propylene oxide (PO) group, preferably for an ethylene oxide group (EO),

the index n stands for an integer from 1 to 10 (most preferably n stands for the numbers 1 , 2,

3),

X ⁺ stands for a monovalent cation or the n ^th part of an n-valent cation, and

(b) a total amount of 3.0 to 5.0 wt.% of at least one anionic surfactant of the linear C9-C2o-alkyl benzene sulfonate-type, preferably of the linear C9-Ci3-alkyl benzene sulfonate-type, and

(c) a total amount of 0.8 to 2.5 wt.-% of at least one fatty acid soap, and

(d) a total amount of 4.7 to 5.7 wt.% of at least one nonionic surfactant of the alkylalcohol alkoxylate-type of the formula in which

R ² stands for a linear or branched, substituted or unsubstituted alkyl, aryl, or alkylaryl residue, having 12 to 18 carbon atoms repectively,

AO stands for an ethylene oxide (EO) or propylene oxide (PO) group, preferably an ethylene oxide group (EO),

m stands for integers from 1 to 9, and

(e) at least two enzymes.

In terms of the invention, and in keeping with general linguistic use, when a numerical range is defined as lying "between" two range limits, the range limits are not included. Numerical ranges that are defined by a range limit up to another range limit include the range limits.

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

All amounts of ingredients of said composition are given in wt.-% based on the total weight of the composition, if not otherwise noted.

All amounts of weight (e.g. wt.-%) of anionic surfactant and of fatty acid soap are normalized and are given in wt.-% of their neutralized form with sodium as counterion.

Anionic surfactants are characterized by a water-solubilizing, anionic group such as a carboxylate, sulfate, sulfonate or phosphate group and a lipophilic alkyl group with about 8 to 30 C atoms. In addition, glycol or polyglycol ether groups, ester, ether and amide groups as well as hydroxyl groups can be contained 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 trialkanol ammonium salts with 2 to 4 C atoms in the alkanol group.

Compositions according to the invention comprise based on the total weight of the composition a total mount of 5.5 to 6.5 wt.% of at least one anionic surfactant of the alkyl polyglycol ether sulfates-type of the formula (An)

R ^! -CKAOJirSO. ^" X ^* . (An)

In this formula, R stands for a Ci2-Cis-alkyl group derived from C12-C18 fatty alcohols, for example from coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl, or stearyl alcohol, or from C10-C20 oxo alcohols;

AO stands for an ethylene oxide (EO) or propylene oxide (PO) group, preferably for an ethylene oxide group; the index n stands for an integer from 1 to 10 (most preferably n stands for the numbers 1 , 2, 3);

X stands for a monovalent cation or the n ^th part of an n-valent cation (with the alkali metal ions and, among those, Na ⁺ or K ⁺ , being preferred, and with Na ⁺ being most preferred). Other cations X ⁺ can be selected from among NHV, ½ Zn2 ⁺ ,½ Mg2 ⁺ , ½ Ca2 ⁺ , ½ Mn2 ⁺ , and mixtures thereof.

Preferred compositions contain 5.8 to 6.2 wt% alkyl polyglycol ether sulfate-type of the formula (A) with respect to the total quantity of the composition.

In summary, especially preferred compositions contain at least one anionic surfactant selected from among fatty alcohol ether sulfates of formula An-1 Na

(An-1 )

where k = 11 to 19, n = 2, 3, 4, 5, 6, 7, or 8. Very especially preferred representatives are Na-Ci2 -14 fatty alcohol ether sulfates with 2 EO (k = 11 -13, n = 2 in formula An-1 ). Preferred compositions contain 5.8 to 6.2 wt% fatty alcohol ether sulfate(s) with respect to the total quantity of the composition (each particularly of formula An-1 ).

Other compositions may additionally contain at least one surfactant of the formula (An-2) different from surfactants of formula (A) and of anionic surfactants of the linear C9-C2o-alkyl benzene sulfonate-type

R ³ -A-SOa Y ^" (An-2)

In this formula, R ³ stands for a linear or branched, substituted or unsubstituted alkyl, aryl, or alkylaryl residue, and the group -A- stands for -O- or a chemical bond. In other words, sulfate surfactants (A = O) or sulfonate surfactants (A = chemical bond) can be described by the above formula. Certain residues R ³ are preferred depending on the choice of group A. In the sulfate surfactants (A = O), R ³ preferably stands for a linear, unsubstituted alkyl residue, especially preferably for a fatty alcohol residue. Preferred residues R ³ are selected from among decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, and eicosyl residues and mixtures thereof, with the representatives with an even number of C atoms being preferred. Especially preferred residues R are derived from C12-C18 fatty alcohols, for example from coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl, or stearyl alcohol, or from C10-C20 oxo alcohols. Y stands for a monovalent cation or the nth part of an n-valent cation, with the alkali metal ions and, among those, Na+ or K+, being preferred, and with Na+ being most preferred. Other cations Y ⁺ can be selected from among NHV, ½ Zn2 ⁺ ,½ Mg2 ⁺ , ½ Ca2 ⁺ , ½ Mn2 ⁺ , and mixtures thereof.

Such surfactants of formula (An-2) are preferably selected from among fatty alcohol sulfates of formula An-2a

(An-2a)

where k = 11 to 19. Very especially preferred representatives are Na-Ci2 -14 fatty alcohol sulfates (k =11 - 13 in formula A-2a).

Compositions of the present invention comprise a total amount of 3.0 to 5.0 wt.% of at least one anionic surfactant of the linear C9-C2o-alkyl benzene sulfonate-type, preferably of the linear C9-Ci3-alkyl benzene sulfonate-type.

Preferred compositions comprise a total amount of 3.2 to 3.6 wt.-% of of at least one anionic surfactant of the linear C9-C2o-alkyl benzene sulfonate-type, preferably of the linear C9-Ci3-alkyl benzene sulfonate- type.

In a particular embodiment of the invention at least one anionic surfactanst of the linear Cg-C2o-alkyl benzene sulfonate-type are most preferably selected from among linear or branched alkylbenzene sulfonates of formula An-3

in which R' and R" together contain 8 to 19, preferably 8 to 15, and particularly 8 to 12 C atoms. One very especially preferred representative can be described by formula An-3a:

(An-3a)

The compositions of the present invention comprise based on the weight of the composition, a total amount of 0.8 to 2.5 wt.-% of at least one fatty acid soap. Preferred compositions comprise based on the weight of the composition, a total amount of 0.8 to below 1 .6 wt.-% of at least one fatty acid soap.

Fatty acid soaps are preferably selected from the water-soluble sodium, potassium or alkanolammonium salts of the saturated and unsaturated fatty acids with 10 to 20 carbon atoms. Sodium or potassium salts of the saturated and unsaturated fatty acids with 10 to 20 carbon atoms, particularly with 12 to 18 carbon atoms, are most preferred soaps according to the invention.

Preferred fatty acid soaps are prepared from fatty acids selected from coconut fatty acid , tallow fatty acid , capric acid , lauric acid , myristic acid , stearic acid , palmitic acid, oleic acid , linoleic acid , elaidic acid linoelaidic acid , olinolenic acid , or mixtures thereof.

More Preferred compositions comprise at least one fatty acid soap are selected from soaps of formula (An-4) wherein R ⁵ preferably stands for a linear or branched, saturated or unsaturated hydrocarbon residue with 9 to 19 carbon atoms (preferably with 11 to 17 carbonatoms). Preferred residues R ⁵ are selected from among nonyl, decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, and mixtures thereof, with the representatives of residues R ⁵ with an odd number of C atoms being particularly preferred. Especially preferred residues R ⁵ are from C11-C17 alkyl groups. Y of formula (An-4) stands for a monovalent cation or the n ^th part of an n-valent cation, with monovalent cations (especially the alkali metal ions and, among those, Na+ or K+) being preferred, and with Na+ being most preferred.

The compositions contains a total amount of 4.7 to 5.7 wt.% of at least one nonionic surfactant of the alkylalcohol alkoxylate-type of the formula the Alkylalcohol alkoxylate-type according to formula (C)

R^AOWH,

(C)

in which

R ² stands for a linear or branched, substituted or unsubstituted alkyl, aryl, or alkylaryl residue, having 12 to 18 carbon atoms repectively

AO stands for an ethylene oxide (EO) or propylene oxide (PO) group,

m stands for integers from 1 to 9.

In the abovementioned formula, R ² stands for a linear or branched, substituted or unsubstituted alkyl, aryl, or alkylaryl residue, preferably for a linear, unsubstituted alkyl residue, especially preferably for a fatty alcohol residue. Preferred residues R ² are selected from among decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, and eicosyl residues and mixtures thereof, with the representatives with an even number of C atoms being preferred. Especially preferred residues R ² are derived from C12-C18 fatty alcohols, for example from coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl, or stearyl alcohol, or from C10-C20 oxo alcohols.

AO stands for an ethylene oxide (EO) or propylene oxide (PO) group, preferably for an ethylene oxide group. The index m stands for an integer from 1 to 50, preferably from 1 to 20, and particularly from 2 to 10. Very especially preferably, m stands for the numbers 2, 3, 4, 5, 6, 7, or 8. In summary, especially preferred surfactants are selected from among fatty alcohol ethoxylates of formula C-1

where k = 11 to 17, m = 2, 3, 4, 5, 6, 7, or 8. Very especially preferred representatives are C12-14 fatty alcohols with 7 EO (k = 1 1-13, m = 7 in formula C-1 ).

Particularly preferred compositions contain said nonionic surfactants of the alkylalcohol alkoxylate-type in a total amount of 5.0 to 5.4 wt.%.

The liquid composition according to the invention must necessarily contain at least two enzymes. Preferably those two enzymes are selected from Enzymes with different E.C.-number. The enzyme E.C.- Nomenclature is based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided (see for example Enzyme E.C. nomenclature databases: ExPASy-database (https://enzyme.expasy.org) or ExploreEnz-Database (www.enzyme-database.org)).

Preferred liquid compositions of the invention are characterized in that they comprise at least one protease enzyme and at least one additional enzyme, selected from amylase, lipase, cellulase, mannanase, pectinase or mixtures thereof.

Particularly preferred liquid compositions of the invention are characterized in that they comprise at least four enzymes. It is most preferred, that the liquid composition according to the invention are characterized in that they comprise at least one protease enzyme and at least one amylase enzyme and at least one lipase enzyme and at least one additional enzyme, selected from cellulase, mannanase, pectinase or mixtures thereof.

As used herein, a "variant" is at the level of proteins of the term corresponding with "mutant" at the nucleic acid level. The predecessor or starting molecules can be wild-type enzymes, i.e. those that can be obtained from natural sources. They can also be enzymes that represent variants that have already been modified, i.e. with respect to the wild-type molecules. These can include, for example, point mutants, those with changes in the amino acid sequence over multiple positions or longer contiguous areas, or even hybrid molecules that are composed from complementary sections of various wild-type enzymes. Addition of a suitable enzyme can improve the overall cleaning performance of the liquid detergent composition. Cleaning performance is understood to mean the capacity to brighten one or more stains, particularly on laundry or dishes. The cleaning performance of an enzyme thus contributes to the overall cleaning performance of the liquid detergent composition or the wash or cleaning bath formed by the liquid detergent composition.

In general, an enzyme can be added to the liquid detergent compositions in any form that yields a desirable product, process, performance, characteristic, or result. For example, an enzyme included in the liquid detergent composition can be absorbed onto support substances and/or embedded in shell substances to protect them against premature inactivation. Non-limiting examples can include solid preparations obtained through granulation, extrusion, or lyophilization, advantageously as concentrated as possible, with small amounts of water and/or offset with stabilizers. In an alternative form of administration, the enzymes can also be encapsulated. This can be accomplished, for example, through spray-drying or extrusion of an enzyme solution together with natural polymer or in the form of a capsule. For example, the enzyme can be enclosed as if in a solid gel or those of the core-shell type, in which an enzyme-containing core is coated with a protective layer that is impermeable to water, air, and/or chemicals. Additional ingredients can be applied, for example stabilizers, emulsifiers, pigments, bleaching agents, or dyes, optionally in layers. These types of capsules can be created according to known methods, for example through agitating or rolled granulation or in fluid-bed processes. Advantageously, these types of granular masses can be low-dust grains due to the application of polymeric film formers and can have a long shelf life due to the coating.

With this in mind, in some specific examples, the liquid detergent composition can include a protease enzyme. A protease is an enzyme that cleaves off peptide bonds by means of hydrolysis, or an enzyme that has protease activity. "Protease activity" is considered to be present when the enzyme has proteolytic activity. In one aspect, protease activity can be determined according to the method described in Surfactants, Volume 7 (1970), pgs. 125-132. Accordingly protease activity is stated in PE (protease units). The protease activity of an enzyme can be determined according to common standard methods such as, in particular, using BSA as a substrate (bovine albumin) and/or using the AAPF method. For example, each of the enzymes from class E.C. 3.4 can be considered a protease enzyme (including each of the 13 sub-classes). The EC number corresponds to the 1992 Enzyme

Nomenclature of the NC-IUBMB, Academic Press, San Diego, California, 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. In some examples, the liquid detergent composition can include from about 0.1 wt% to about 5 wt%, or from about 0.5 wt% to about 3 wt% of protease enzyme. In some additional examples, the liquid detergent composition can include a cullulase. Synonymous terms can be used for cellulases, particularly endoglucanase, endo-1 ,4-beta-glucanase,

carboxymethylcellulase, endo-1 ,4-beta-D-glucanase, beta-1 ,4-glucanase, beta-1 ,4- endoglucanhydrolase, celludextrinase, or avicelase. A cellulose enzyme can be determined by its ability to hydrolyze 1 ,4-B-D-glucosidic bonds in cellulose. Commercially available examples can include the fungal, endoglucanase(EG)-rich cellulase preparation or the further developments thereof sold by Novozymes under the trade name Celluzyme®. Additionally, products called Endolase® and Carezyme®, which are also sold by Novozymes, are based on 50kD-EG or 43kD-EG from Humicola insolens DSM 1800. Other usable commercial products from this company are Cellusoft®,

Renozyme®, and Celluclean®. Also usable are cellulases, for example, sold by AB Enzymes, in Finland, under the trade names Ecostone® and Biotouch®, and which are at least partially based on the 20 kD-EG from Melanocarpus. Other cellulases from AB Enzymes are Econase® and Ecopulp®. Additional suitable cellulases are from Bacillus sp. CBS 670.93 and CBS 669.93, wherein the one from Bacillus sp. CBS 670.93 sold by Danisco/Genencor is available under the trade name Puradax®. Additional usable commercial products from Danisco/Genencor include "Genencor detergent cellulase L" and lndiAge®Neutra. However, any suitable cellulase enzyme can be used. In some examples, the cellulase can be present in the liquid detergent composition in an amount from about 0.01 wt% to 1 wt%, or from 0.05 wt% to 0.5 wt%.

In some additional examples, the liquid detergent composition can also include a lipase enzyme. Non- limiting examples of lipase enzymes can include an enzyme of the group that is formed from triacylglycerol lipase (E.C. 3.1.1 .3), lipoprotein lipase (E.C. 3.1 .1 .34), monoglyceride lipase (E.C. 3.1 .1 .23), and combinations thereof. In some examples, the lipase can be active in an alkaline medium. Furthermore, in some examples, the lipase can be naturally available from a microorganism such as Thermomyces lanuginosus or Rhizopus oryzae or Mucor javanicus species, or can be derived from the aforementioned naturally available lipases via mutagenesis. In one specific example, the lipase can be naturally available from a microorganism of the Thermomyces lanuginosus species or derived from the aforementioned lipases naturally available from Thermomyces lanuginosus via mutagenesis.

In this context, naturally available means that the lipase is an inherent enzyme of the microorganism. The lipase can consequently be expressed by a nucleic acid sequence, which is part of the chromosomal DNA of the microorganism in its wild-type form. It or the nucleic acid sequence coding for it is consequently available in the wild-type form of the microorganism and/or can be isolated from the wild-type form of the microorganism. Contrary to this, a lipase that is not naturally available in the microorganism and/or the nucleic acid sequence coding for it can be incorporated into the microorganism in a targeted manner with the assistance of genetic processes, such that the microorganism can be enriched by the lipase and/or the nucleic acid sequence coding for it. However, a lipase that is naturally available from a microorganism of the Thermomyces lanuginosus or Rhizopus oryzae or Mucor javanicus species can be produced by a different organism, but can be quite recombinant in nature.

Lipase is commercially available from a variety of sources, such as Amano Pharmaceuticals under the designations Lipase M-AP10®, Lipase LE®, and Lipase F® (as well as Lipase JV®). Lipase F® is naturally available, for example, in Rhizopus oryzae. Lipase M-AP10® is naturally available, for example, in Mucor javanicus. Lipex® from Novozymes (Denmark) is another non-limiting example of a commercially available lipase enzyme.

The lipase enzyme can be included in the composition in various amounts. In some examples, the lipase can be present in the liquid detergent composition in an amount from about 0.01 wt% to about 1 wt%, or from about 0.05 wt% to about 0.2 wt%.

In some examples, the liquid detergent composition can also include a mannanase enzyme. A mannanase can catalyze the hydrolysis of 1 ,4-beta-D-mannosidic bonds in mannans, galactomannans, glucomannans, and galactoglucomannans, within the scope of their mannanase activity. Said mannanase enzymes can be classified as E.C. 3.2.1 .78 according to the enzyme nomenclature. The mannanase activity of a polypeptide or enzyme can be determined according to the test methods known in the literature. In doing so, a test solution can be placed in 4 mm-diameter holes of an agar plate containing 0.2% by weight AZGL galactomannan (carob), i.e. a substrate for the endo-1 ,4-beta- D-mannanase assay, obtainable from Megazyme.

In some examples, the mannanase enzyme can be obtained or derived from the gram-positive alkalophilic phyla of Bacillus, such as a member of the group consisting of 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. In some specific examples, the mannanse enzyme can be obtained from Bacillus sp. 1633, Bacillus sp. AAI12, Bacillus clausii, Bacillus agaradhaerens, or Bacillus licheniformis. Non-limiting examples of commercially available mannanase enzylnes can be obtained from Novozymes under the name Mannaway®.

Where the liquid detergent composition includes a mannanase, it can generally be present in an amount from 0.01 wt% to 1 .0 wt%. In some additional examples, the mannanse can be present in an amount from 0.02 wt% to 0.5 wt%.

In yet additional examples, the liquid detergent composition can include an amylase enzyme. More specifically, a-amylases (E.C. 3.2.1 .1 ) can hydrolyze internal a-1 ,4-glycosidisic bonds of starch and starch-like polymers as an enzyme. This a-amylase activity can be measured in KNU (Kilo Novo Units), wherein 1 KNU stands for the enzyme quantity that hydrolyzes 5.25 g of starch (obtainable from Merck, Darmstadt, Germany) per hour at 37°C, pH 5.6 and in the presence of 0.0043 M calcium ions. An alternative activity determination method is the so-called DNS method, which is described, for example, in application WO 02/10356 A2. Specifically, the oligosaccharides, disaccharides, and glucose units released during the hydrolysis of starch are verified through oxidation of the reducing ends with dinitrosalicysic acid (DNS). The activity is obtained in μιηοΙ reducing sugar (based on maltose) per min and ml, which can result in activity values in the thousands. The same enzyme can be determined via various methods, wherein the respective conversion factors may vary depending on the enzyme and therefore must be specified by means of a standard. Approximately, it can be stated that 1 KNU is about 50,000 for calculation purposes. A further activity determination method is the measurement using the quick start ^® test kit from Abbott, Abott Park, Illinois, USA.

In some examples, the a-amylases can be active in an alkaline medium. In some further examples, the a-amylases can be primarily produced and secreted by microorganisms, i.e. fungi or bacteria, such as those of the genera Aspergillus and Bacillus. Starting from these natural enzymes, there is a practically incalculable abundance of variants available that have been derived via mutagenesis and have specific advantages depending on the application area.

Non-limiting examples of these are the α-amylases from Bacillus licheniformis, from B.

amyloliquefaciens, and from B. stearothermophilus, as well as those further developments improved for use in detergents or cleaning agents. The enzyme from B. licheniformis can be obtained from Novozymes under the name Termamyl ^® and from Genencor under the name Purastar ^® ST. Further development products of this a-amylase are sold by Novozymes under the trade names Duramyl and Termamylultra, by Genencor under the name PurastarOxAm, and by Daiwa Seiko Inc., in Tokyo, Japan, as Keistase ^® . An α-amylase from B. amyloliquefaciens is sold by Novozymes under the name BAN and derived variants of the α-amylase from B. stearothermophilus are also sold by Novozymes under the names BSG and Novamyl. Examples of further developments of α-amylases from other organisms can include α-amylase from Aspergillus niger and A. oryzae obtainable from Novozymes under the trade name Fungamyl ^® . Another commercial product is, for example, Amylase-LT ^® . Where α-amylase is included in the liquid detergent composition, it can be included in various amounts. For example, α-amylase can be included in the liquid detergent composition in an amount from 0.01 wt% to 3.0 wt%, or from 0.02 wt% to 1.0 wt%.

In additional examples, the liquid detergent composition can include a pectinase enzyme. Pectinases can be used to degrade pectins, which are a family of complex polysaccharides that contain 1 ,4-linked a-D-galactosyluronic acid residues. Pectinases can catalyze the cleavage of (1 ,4)-oD-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends. Thus, the pectinases can cleave pectin into smaller fragments that are easier to remove during washing and can provide additional stain removal properties to the liquid detergent composition. For example, pectinase enzymes can help eliminate stains from fresh fruits, tomato sauces, jams, low-fat dairy products, the like, or combinations thereof.

Where a pectinase is included in the liquid detergent composition, it can be included in various amounts. For example, pectinase can be included in the liquid detergent composition in an amount from 0.01 wt% to 1.0 wt%. In some additional examples, the pectinase can be present in an amount from 0.02 wt% to 0.5 wt%.

In general, the enzymes contained in a composition according to the invention can be adsorbed on carriers and/or embedded in coating substances in order to protect them from premature inactivation.

The enzymes obtained can be added to compositions according to the invention in any form established according to the prior art. These include, particularly, the solid preparations obtained through granulation, extrusion, or lyophilization, advantageously concentrated to the greatest possible extent, with low- moisture, and/or with stabilizers added. In an alternative pharmaceutical form, the enzymes can also be encapsulated, for example through 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 enclosed in a set 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. In the case of overlaid layers, other active substances, such as stabilizers, emulsifiers, pigments, bleaching agents, or dyes, can be additionally applied. Such capsules are applied using inherently known methods, for example through shaking or roll granulation or in fluidized bed processes. Such granulates are advantageously low in dust, for example due to the application of polymeric film-formers, and stable in storage due to the coating.

Besides the components that must necessarily be present according to the invention, the composition according to the invention preferably contain water as a solvent. Compositions that are preferred according to the invention contain water in a quantity between 0 to 80 wt%, particularly from 30 to 80 wt%, each with respect to the total weight of the composition.

Besides the components that must necessarily be present according to the invention, nonaqueous solvents can be added to the liquid composition according to the invention. Suitable nonaqueous solvents include mono- or polyvalent alcohols, alkanolamines, or glycol ethers, provided that they are miscible with water in the indicated concentration range. Preferably, the solvents are selected from among ethanol, n-propanol, i-propanol, butanols, glycol, propanediol, butanediol, methylpropanediol, glycerin, diglycol, propyl diglycol, butyl diglycol, hexylene glycol, ethylene glycol methyl ether, ethylene glycol ethyl ether, ethylene glycol propyl ether, ethylene glycol mono-n-butyl ether, diethylene glycol ethyl 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, as well as mixtures of these solvents. It is preferred, however, that the composition according to the invention contain an alcohol, particularly ethanol and/or glycerin and/or 1 ,2-propanediol, in quantities from 0.5 to 5 wt% with respect to the overall composition.

In addition to the required ingredients, the compositions according to the invention can contain other ingredients that further improve the technical and/or aesthetic characteristics of the detergent. In the context of the present invention, the composition according to the invention preferably also contains one or more substances from the group of the bleaching agents, complexing agents, builders, electrolytes, pH adjusters, perfumes, perfume carriers, fluorescent agents, dyes, hydrotropes, foam inhibitors, silicone oils, antiredeposition agents, shrinkage inhibitors, anti-creasing agents, color transfer inhibitors, antimicrobial agents, germicides, fungicides, antioxidants, preservatives, corrosion inhibitors, antistatic agents, bittering agents, ironing aids, repellents and impregnating agents, swelling and antislip agents, softening components, and UV absorbers.

Any substances can be used as bleaching agents which destroy and/or take up dyes through oxidation, reduction, or adsorption, thereby decolorizing materials. These include inter alia hypohalogenite- containing bleaching agents, hydrogen peroxide, perborate, percarbonate, peracetic acid, diperazelaic acid, diperoxydodecanedioic acid, and oxidative enzyme systems.

Some noteworthy builders that can be contained in the composition according to the invention are particularly silicates, aluminum silicates (particularly zeolites), carbonates, salts of organic di- and polycarboxylic acids, as well as mixtures of these substances.

Organic builders that can be present in the composition according to the invention are the polycarboxylic acids, for example, which can be used in the form of their sodium salts, with polycarboxylic acids being understood as being such carboxylic acids that have 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, aminopolycarboxylic acids, as well as mixtures thereof. Preferred salts are the salts of the polycarboxylic acids such as citric acid, adipic acid, succinic acid, glutaric acid, tartaric acid, sugar acids, and mixtures thereof.

Polymeric polycarboxylates are also suitable as builders. These are the alkali metal salts of polyacrylic acid or of polymethacrylic acid, for example, such as those having a relative molecular mass from 600 to 750,000 g/mol.

Suitable polymers are particularly polyacrylates, which preferably have a molecular mass from 1 ,000 to 15,000 g/mol. Due to their superior solubility, the short-chain polyacrylates, which have molar masses from 1 ,000 to 10,000 g/mol, and especially preferably from 1 ,000 to 5,000 g/mol, can be preferred from this group.

Copolymeric polycarboxylates, particularly those of acrylic acid with methacrylic acid, and acrylic acid or methacrylic acid with maleic acid, are also suitable. To improve water solubility, the polymers can also contain allyl sulfonic acids such as allyloxybenzene sulfonic acid and methallyl sulfonic acid as monomers.

In the liquid compositions according to the invention, soluble builders such as citric acid, for example, or acryl polymers having a molar mass from 1 ,000 to 5,000 g/mol are preferably used.

A second object of the invention is the use of a liquid composition according to the first object of the invention to stabilize the composition upon storage at temperatures below 1 °C.

A third object of the invention is the use of a liquid composition according to the first object of the invention to clean textiles.

A fourth object of the invention is a method for cleaning textiles, comprising the provision of a washing liquor using at least the following components:

(i) at least one composition according to the first object of the invention, (ii) preferably at least one solvent, particularly water, and

(iii) at least one textile.

According to the invention, a washing liquor is at least the total quantity of the components enumerated under (i) and (iii).

Methods for cleaning textiles are generally characterized in that various substances that are active in detergency are applied to the article to be cleaned in several method steps and washed off after the treatment time, or that the article to be cleaned is otherwise treated with a composition according to the first object of the invention or a solution of this composition.

If component (ii) of the method according to the invention is additionally added to the washing liquor, then 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, temperatures of 60 °C or below, 40 °C or below, 30 °C or below, or 20 °C or below, most preferred in a range of 10°C to 40°C, are used in various embodiments of the invention. These temperatures refer to the temperatures used in the washing steps.

Examples

The following formulae were prepared according to standard procedures:

Table 1 : Inventive formula (E1 ) and non-inventive reference (V1 )

The foam results of the inventive formula versus the non-inventive formula show an improvement, since a lower foam level is obtained over the course of the washing process (see fig. 1 ). The higher the boxes in the diagram, the higher the foam of the respective formula.

The wash tests show a superior cleaning power of the inventive formula over the non-inventive formula.

Storage stability tests at 0°C for 6 weeks show that the inventive formula is stable while the reference shows white precipitates.