Stabilized cleaning composition containing EDDS and enzymes and its use

Abstract

The present invention provides for improving the long-term stability of enzymes, comprising: (i) ethylenediamine-N,N'-disuccinic acid (EDDS); (ii) at least one enzyme selected from the group consisting of amylase and protease; (iii) at least one anionic surfactant; and (iv) calcium (Ca 2+ (v) a liquid cleaning composition comprising (v) water, the manufacture of the same, and its use, for example, in laundry or dishwashing.

Description

[Technical Field]

[0001] The present invention relates to a specific cleaning composition comprising ethylenediamine-N,N'-disuccinic acid (EDDS) (abbreviated as "Inventive Component I") and a protease and / or amylase (abbreviated as "Inventive Component II") (in the present invention, the composition is always abbreviated as "Inventive Composition" or "Composition of the Present Invention"), its manufacture, and in particular its use as a laundry detergent composition. [Background technology]

[0002] Detergent and home care product formulations continue to face the challenge of developing improved products for removing a wide range of dirt and stains from fabrics and hard surfaces. Chemically and physicochemically, the diverse spectrum of dirt and stains ranges from polar dirt such as proteinaceous, clay, and inorganic dirt to nonpolar dirt such as soot, carbon black, by-products of incomplete hydrocarbon combustion, and organic dirt such as sebum and starch-based stains. These challenging requirements are made even more difficult in light of the emerging trend of improving the "footprint" of all cleaning products, which includes production efficiency and thus reduction of energy consumption compared to products made from natural or renewable resources or previous products, efficiency of use such as reduction in quantity for the same or higher performance at the same level of use, and sustainability in the natural environment after use, particularly its biodegradability, as recycling is technically very difficult and, along with being economically unattractive.

[0003] As a result of these trends, there is a strong need for novel biodegradable cleaning compositions that offer both superior primary (i.e., stain removal) and secondary (i.e., whiteness maintenance) cleaning benefits for both hydrophobic and hydrophilic stains, as well as improved biodegradability. One step toward sustainable cleaning compositions is the increased use of enzymes. However, the conditions found in cleaning compositions are far from optimal for the long-term storage of enzymes. Cleaning compositions contain surfactants that can interfere with the integrity of enzymes. The same is true for polymer cleaning components. In addition, builders can compete with enzymes for alkaline earth metals, such as calcium or magnesium cations, which are important cofactors for enzymes like amylase and protease. Thus, many standard cleaning components, when applied at their active concentrations, threaten enzymes and their long-term stability. To overcome this problem, cleaning compositions may contain enzyme-stabilizing components such as boric acid, boronic acid, and their derivatives. However, boric acid is registered under the REACH regulation and is suspected of causing harm to fertility and fetuses, which reduces the acceptance of boron-containing enzyme-stabilizing components by authorities and customers. Therefore, there is a need to find improved enzyme-containing cleaning compositions that have a high-performance profile, enhanced consumer safety, and improved biodegradability.

[0004] The following outlines the current knowledge and most relevant publications in the field of this invention, as well as established use of builders or EDDSs in combination with enzymes.

[0005] One class of builder components frequently used in cleaning compositions is polyphosphonates. These synthetic compounds differ from natural phosphonates such as 2-aminoethylphosphonic acid because they are larger, more anionic, and often exist in complex with metals. Biodegradation tests for 1-hydroxyethylidene-1,1-diphosphonic acid (HEDP) and nitrilotris-methylenephosphonic acid (NTMP) showed no signs of degradation. Furthermore, studies of 1-hydroxyethylidene-1,1-diphosphonic acid (HEDP), nitrilotris-methylenephosphonic acid (NTMP), ethylenediamine-tetra(methylenephosphonic acid) (EDTMP), and diethylenetriamine-penta(methylenephosphonic acid) (DTPMP) in standard biodegradation tests also failed to identify any biodegradation. Therefore, with respect to biodegradation, the use of polyphosphonates in cleaning compositions is undesirable.

[0006] Another well-established class of builder compounds used in home care products are aminopolycarboxylate chelators. This class, like polyphosphonates, includes a diverse range of compounds such as ethylenediaminetetraacetic acid (EDTA), nitrilotriacetic acid (NTA), diethylenetriaminepentaacetic acid (DTPA), and tetrasodium-N,N-bis(carboxylatomethyl)-L-glutamate (GLDA). EDTA is the most widely used chelating agent in the world. EDTA's widespread use and its slow removal under many environmental conditions have led to its status as the anthropogenic compound with the highest concentrations in many European surface waters. For this reason, manufacturers are seeking alternative chelating agents with higher biodegradability. NTA, on the one hand, is more biodegradable than EDTA, but can cause irritation to the eyes, skin, and respiratory tract, as well as damage to the kidneys and bladder. In addition, NTA is thought to potentially cause cancer in humans. Furthermore, this application provides experimental evidence that DTPA and GLDA impair the long-term stability of proteases and / or amylases.

[0007] The use of citrate as a builder has been known since the early 1970s, for example, as described in U.S. Patent No. 4028262A. However, this compound also negatively impairs the long-term stability of amylase, as experimentally demonstrated by the inventors, and therefore is not an ideal solution for future washing formulations containing increased amounts of enzyme.

[0008] International Publication No. 9606908 discloses the use of EDDS in detergents together with enzymes such as proteases and amylases. However, detergent formulations containing EDDS and enzymes are not specifically prepared to establish long-term enzyme stability. To achieve this long-term stability, International Publication No. 9606908A describes enzyme stabilizers, preferably boric acid and boronic acid compounds, that are registered under the REACH regulation and have the aforementioned adverse effects of potentially impairing fertility and the fetus. [Overview of the project] [Problems that the invention aims to solve]

[0009] Therefore, there is a need in the art to find a cleaning composition comprising a combination of surfactant, builder, and enzyme that does not contain boric acid or boronic acid, has high biodegradability, and provides long-term enzyme stability and customer safety. [Means for solving the problem]

[0010] The inventors have surprisingly found that the combination of ethylenediamine-N,N'-disuccinic acid (EDDS) with a protease or amylase in specific cleaning composition formulations (e.g., specific anionic surfactants, calcium concentration, pH value, and viscosity) results in cleaning compositions that demonstrate improved consumer safety, high biodegradability, and long-term enzyme stability. Experimental comparisons with other chelating agents such as diethylenetriamine penta(methylenephosphonic acid) (DTPMP), 1-hydroxyethylidene-1,1-diphosphonic acid (HEDP), citrate, diethylenetriamine pentaacetic acid (DTPA), and tetrasodium-N,N-bis(carboxylatomethyl)-L-glutamate (GLDA) demonstrate that EDDS is the only builder that provides biodegradability and protease / amylase stability, and therefore can be used in cleaning compositions without strong enzyme stabilizers such as boric acid or boronic acid.

[0011] Therefore, the object of the present invention is a liquid cleaning composition comprising: (i) ethylenediamine-N,N'-disuccinic acid (EDDS) in an amount ranging from 0.0005% to 20% by weight of the composition; (ii) at least one enzyme selected from the group consisting of amylase and protease in an amount ranging from 0.000001% to 5% by weight of the composition; (iii) at least one anionic surfactant in an amount ranging from 0.1% to 50% by weight of the composition; and (iv) calcium (Ca) in an amount ranging from 0.000001% to 5% by weight of the composition. 2+ The objective is to provide a cleaning composition comprising (v) water and (v) a viscosity in the range of 20 to 10000 mPa*s and a pH value in the range of 4 to 14, as measured by the relevant method according to this specification.

[0012] The liquid cleaning composition of the present invention further comprises at least one element from the group consisting of non-anionic surfactants, amphoteric surfactants, cobuilders, alcohols, biocides, thickeners, water-soluble polymers, mud stain removers / anti-re-adhesion agents, polymer stain release agents, bleaches, bleaching activators, gloss agents, odor suppressants, pigments, dyes, opacifiers, colorants, color transfer inhibitors, anti-foaming agents, corrosion inhibitors, softeners, and fragrances.

[0013] In another embodiment, the liquid cleaning composition of the present invention is used for cleaning a plasterwork.

[0014] Furthermore, a cleaning method comprising bringing the liquid cleaning composition of the present invention into contact with a fabric is also part of the present invention.

[0015] In addition, the present invention relates to a method for producing the liquid cleaning composition of the present invention, comprising contacting components (i) to (v) of the liquid cleaning composition as described above and mixing them. [Modes for carrying out the invention]

[0016] Accordingly, the subject matter of the present invention is the following embodiments 1 to 15, which are defined and further described in the following further embodiments and further illustrated in the experimental section.

[0017] Embodiment 1 A liquid cleaning composition comprising: (i) ethylenediamine-N,N'-disuccinic acid (EDDS) in an amount ranging from 0.0005% to 20% by weight of the composition; (ii) at least one enzyme selected from the group consisting of amylase and protease in an amount ranging from 0.000001% to 5% by weight of the composition; (iii) at least one anionic surfactant in an amount ranging from 0.1% to 50% by weight of the composition; and (iv) calcium (Ca) in an amount ranging from 0.000001% to 5% by weight of the composition. 2+ A cleaning composition comprising (v) water and (v) a viscosity in the range of 20 to 10000 mPa*s and a pH value in the range of 4 to 14, as measured by the relevant method according to this specification.

[0018] As used herein, "liquid" means that the continuous phase or the major part of the composition is liquid and the composition is fluid at 20 °C (i.e., it may contain suspended solids). The term "liquid" includes gels. As used herein, "gel" means a shear-thinning layered gel having an injection viscosity in the range of 100 to 5000 mPa·s (millipascal seconds), more preferably less than 3000 mPa·s, and most preferably less than 1500 mPa·s. A gel can be a thick liquid. Nevertheless, a thick liquid can be a Newtonian fluid, such as honey or syrup, that does not change its viscosity with changes in the flow state. This type of thick liquid is very difficult and troublesome to dispense. Different types of liquid gels are shear-thinning, i.e., they are thick under low shear conditions (e.g., at rest) and thin under high flow conditions. Thus, the cleaning composition includes detergents or automatic dishwashing (ADW) gels.

[0019] As used herein in the same sense, the terms "cleaning composition" or "detergent" refer to all compositions intended to be used in connection with cleaning activities and to enhance the effectiveness of cleaning activities. The term "detergent" includes, but is not limited to, hard surface cleaning compositions (kitchen cleaning compositions, bathroom cleaning compositions, floor cleaning compositions, general household cleaning compositions, glass cleaning compositions), detergents, dishwashing compositions, food cleaning compositions, fabric and fiber cleaning compositions, disinfectants, etc. As used herein, the term "cleaning" refers to activities involving the removal of undesirable residues from a surface, including, in particular, chemical, mechanical and thermal cleaning activities and combinations thereof. Chemical cleaning activities include, for example, the use of a solvent to remove residues from a surface, potentially further involving the use of a surfactant to enhance the compatibility between the residue and the solvent. Chemical cleaning activities further include chemical changes of the residues to improve the ease of removal of the residues. The cleaning composition of the present invention contains at least five components, namely (i) EDDS, (ii) protease and / or amylase, (iii) at least one anionic surfactant, (iv) calcium cation (Ca 2+ ) and (v) water.

[0020] As used herein, "enzyme" refers to any of a number of proteins produced in living cells that naturally accelerate or catalyze the metabolic processes of an organism. Enzymes act on substrates. Substrates bind to the enzyme at a location called the active site immediately before the reaction catalyzed by the enzyme occurs. Enzymes according to the present application include, but are not limited to, amylase or protease, also called inventive compound II. However, the cleaning composition of the present invention may contain, in addition to amylase or protease, lipase, cellulase, mannanase, hemicellulase, phospholipase, esterase, pectinase, lactase, peroxidase, xylanase, cutinase, pectate lyase, keratinase, reductase, oxidase, phenol oxidase, lipoxygenase, ligninase, pullulanase, tannase, pentosanase, malanase, beta-glucanase, arabinosidase, hyaluronidase, chondroitinase, laccase, nuclease, DNase, phosphodiesterase, phytase, carbohydrase, galactanase, xanthanase, xyloglucanase, oxidoreductase, perhydrolase, aminopeptidase, asparaginase, carbohydrase, carboxypeptidase, catalase, chitinase, cyclodextrin glycosyltransferase, alpha-galactosidase, beta-galactosidase, glucoamylase, alpha-glucosidase, beta-glucosidase, invertase, ribonuclease, transglutaminase, and dispersions or combinations thereof.

[0021] As used herein, the term "at least one" includes, but is not limited to, 1, 2, 3, 4, 5, 6, 7, 8, 9, and more.

[0022] Embodiment 2 Ethylenediamine-N,N'-disuccinic acid (EDDS) is present in the liquid cleaning composition according to Embodiment 1 in an amount in the range of 0.001 wt% to 15 wt%, preferably 0.01 wt% to 10 wt%, most preferably 0.1 wt% to 5 wt% of the composition.

[0023] EDDS is given by formula (I): [ka] It has the structure of [the object].

[0024] EDDS has two chirality centers. Therefore, EDDS can appear in three different stereoisomers: [R,R], [R,S] / [S,R], and [S,S]. [S,S]EDDS is fully biodegradable, while meso-EDDS is at least partially biodegradable. The [S,S] stereoisomer is a derivative of the natural amino acid L-aspartic acid, which may be the reason for its good biodegradability. The [R,R] stereoisomer persists in the environment. Therefore, in preferred embodiments of the present invention, EDDS is [S,S]EDDS or meso-EDDS, more preferably [S,S]EDDS.

[0025] EDDS is commercially available, for example, from Sigma-Aldrich (St. Louis, Missouri, USA). Alternatively, it can be prepared using maleic anhydride and ethylenediamine. A preferred biodegradable [S,S] isomer can be prepared by reacting L-aspartic acid with 1,2-dibromoethane. EDDS may also be in salt form, i.e., in which one or more of the four acidic hydrogens are replaced by a water-soluble cation M such as sodium, potassium, ammonium, or triethanolammonium.

[0026] In preferred embodiments, the lower limit of the EDDS concentration is 0.0005% by weight, 0.005% by weight, or 0.05% by weight of the composition of the present invention. In other preferred embodiments, the upper limit of the EDDS concentration is 8% by weight, 7% by weight, or 6% by weight of the composition of the present invention.

[0027] Embodiment 3 The liquid cleaning composition according to Embodiment 1 or 2, wherein at least the enzyme is present in an amount ranging from 0.00001% to 2% by weight, preferably 0.0001% to 1% by weight, and most preferably 0.001% to 0.5% by weight of the composition.

[0028] In a preferred embodiment, the lower limit of the enzyme concentration is 0.00005% by weight or 0.0005% by weight of the composition of the present invention. In another preferred embodiment, the upper limit of the enzyme concentration is 1.7% by weight, 1.3% by weight or 0.8% by weight of the composition of the present invention.

[0029] Embodiment 4 (a) amylase is alpha-amylase and / or (b) protease is subtilisin protease, according to any one of Embodiments 1 to 3.

[0030] The “amylase” (alpha and / or beta) according to the present invention includes those of bacterial or fungal origin (EC 3.2.1.1 and 3.2.1.2, respectively). This term also includes natural amylases, so-called wild-type protein variants and mutants. Preferably, the amylase is selected from the group of alpha-amylases (EC 3.2.1.1). This includes chemically modified or proteologic mutants. The amylase according to the present invention has “starch-degrading activity” or “amylase activity” involving (internal) hydrolysis of glucosidic bonds in polysaccharides. Alpha-amylase activity can be measured by assays for measuring alpha-amylase activity known to those skilled in the art. As an example of an assay for measuring alpha-amylase activity, alpha-amylase activity can be measured by a method using Phadebas tablets (Phadebas Amylase Test, supplied by Magle Life Science) as a substrate. Starch is hydrolyzed by alpha-amylase to give soluble blue fragments. The absorbance of the resulting blue solution, measured spectrophotometrically at 620 nm, is a function of alpha-amylase activity. The measured absorbance is directly proportional to the specific activity (activity / mg of pure alpha-amylase protein) of the alpha-amylase in question under given conditions.

[0031] Alpha-amylase activity can also be measured by a method using ethylidene-4-nitrophenyl-alpha-D-maltoheptaside (EPS). D-maltoheptaside is a block oligosaccharide that can be cleaved by endo-amylase. After cleavage, the alpha-glucosidase contained in the kit digests the substrate, releasing free PNP molecules that are yellow in color, which can then be measured by visible spectrophotometric analysis at 405 nm. The kit containing the EPS substrate and alpha-glucosidase is manufactured by Roche Costum Biotech (cat. No. 10880078103). The slope of the time-dependent absorption curve is directly proportional to the specific activity (activity per 1 mg of enzyme) of the alpha-amylase in question under given conditions.

[0032] Starch-degrading activity can be provided in units per gram of enzyme. For example, one unit of alpha-amylase can release 1.0 mg of maltose from starch in 3 minutes at 20°C and pH 6.9.

[0033] Regardless of the nature of the assay, the amylase variants used in the compositions of the present invention may have at least 40%, at least 60%, at least 70%, at least 80%, at least 90%, at least 100%, or at least 110% of the amylase activity measured for the corresponding wild-type amylase.

[0034] The amylase may be derived from Bacillus licheniformis having Sequence ID No. 2 as described in International Publication No. 95 / 10603, and at least 95% of its mutants. Preferred mutants are described in International Publication No. 95 / 10603 and contain one or more substitutions at the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181, 188, 190, 197, 201, 202, 207, 208, 209, 211, 243, 264, 304, 305, 391, 408, and 444, and have starch-degrading activity. The variants are described in Sequence ID No. 4 of International Publication No. 94 / 02597, International Publication No. 94 / 018314, International Publication No. 97 / 043424, and International Publication No. 99 / 019467.

[0035] The amylase may further be derived from B. stearothermophilus having SEQ ID NO: 6, as disclosed in International Publication No. 02 / 10355, or it may be an amylase optionally having C-terminal shortening beyond the wild-type sequence. Preferred variants of SEQ ID NO: 6 include those containing deletions at positions 179 and / or 181 and / or 182 and / or substitutions at position 193.

[0036] The amylase may further be derived from Bacillus sp. 707 having Sequence ID No. 6 as disclosed in International Publication No. 99 / 19467, and at least 95% of its mutants. Preferred mutants of Sequence ID No. 6 have substitutions, deletions, or insertions at one or more of the following positions: R181, G182, H183, G184, N195, I206, E212, E216, and K269.

[0037] The amylase may further be derived from Bacillus halmapalus having SEQ ID NO: 2 or 7, as described in International Publication No. 96 / 23872, also described herein as SP-722. Preferred variants are described in International Publication Nos. 97 / 3296, 99 / 194671, and 2013 / 001078.

[0038] The amylase may further be derived from Bacillus sp. DSM 12649 having Sequence ID No. 4, as disclosed in International Publication No. 00 / 22103, and at least 95% of its mutants.

[0039] The amylase may further be derived from a Bacillus sp. A 7-7 (DSM 12368) having an amino acid sequence that is at least 95% identical to Sequence ID No. 2, as disclosed in International Publication No. 02 / 10356, particularly in the region of amino acids 32-516 following Sequence ID No. 2.

[0040] The amylase may further be derived from Bacillus strain TS-23 and its variants, which have Sequence ID No. 2 as disclosed in International Publication No. 2009 / 061380.

[0041] The amylase may further be derived from Cytophaga sp. species having Sequence ID No. 1, as disclosed in International Publication No. 2013 / 184577, and at least 95% of its mutants.

[0042] The amylase may further be derived from Bacillus megaterium. DSM 90 having Sequence ID No. 1, as disclosed in International Publication No. 2010 / 104675, and at least 95% of its mutants.

[0043] The amylase may also be derived from Bacillus sp. species containing amino acids 1-485 of Sequence ID No. 2, as described in International Publication No. 00 / 60060, and at least 95% of its mutants.

[0044] The amylase may further be derived from Bacillus amyloliquefaciens or its variants, preferably selected from amylases conforming to Sequence ID No. 3, as described in International Publication No. 2016 / 092009.

[0045] Amylase may have amylase variants including SEQ ID NO: 12, as described in International Publication No. 2006 / 002643, or the substitutions Y295F and M202LITV within SEQ ID NO: 12.

[0046] Amylase may have amylase variants that include substitutions at one or more positions selected from the group consisting of SEQ ID NO: 6, as described in International Publication No. 2011 / 098531, or 193[G, A, S, T, or M], 195[F, W, Y, L, I, or V], 197[F, W, Y, L, I, or V], 198[Q, or N], 200[F, W, Y, L, I, or V], 203[F, W, Y, L, I, or V], 206[F, W, Y, N, L, I, V, H, Q, D, or E], 210[F, W, Y, L, I, or V], 212[F, W, Y, L, I, or V], 213[G, A, S, T, or M], and 243[F, W, Y, L, I, or V] within SEQ ID NO: 6.

[0047] Amylase may have amylase variants that include modifications at two or more positions corresponding to positions G304, W140, W189, D134, E260, F262, W284, W347, W439, W469, G476 and G477 within Sequence ID No. 1, as described in International Publication No. 2013 / 001078.

[0048] Amylase may have amylase variants that include a deletion at position 181+182, 182+183, or 183+184 in Sequence ID No. 2, which optionally includes one or more changes at any of the positions corresponding to W140, W159, W167, Q169, W189, E194, N260, F262, W284, F289, G304, G305, R320, W347, W439, W469, G476, and G477 in Sequence ID No. 2, as described in International Publication No. 2013 / 001087.

[0049] The amylase may be a hybrid alpha-amylase derived from the aforementioned amylase, such as the one described in International Publication No. 2006 / 066594.

[0050] The hybrid amylase may conform to International Publication No. 2014 / 183920, having A and B domains that are at least 90% identical to Sequence ID No. 2 of International Publication No. 2014 / 183920, and a C domain that is at least 90% identical to Sequence ID No. 6 of International Publication No. 2014 / 183920, and the hybrid amylase has starch-degrading activity, preferably the hybrid alpha-amylase is at least 95% identical to Sequence ID No. 23 of International Publication No. 2014 / 183920, and has starch-degrading activity.

[0051] The hybrid amylase may conform to International Publication No. 2014 / 183921, having A and B domains that are at least 75% identical to SEQ ID NO: 2, SEQ ID NO: 15, SEQ ID NO: 20, SEQ ID NO: 23, SEQ ID NO: 29, SEQ ID NO: 26, SEQ ID NO: 32 and SEQ ID NO: 39 as disclosed in International Publication No. 2014 / 183921, and a C domain that is at least 90% identical to SEQ ID NO: 6 of International Publication No. 2014 / 183921, and the hybrid amylase has starch-degrading activity, preferably the hybrid alpha-amylase is at least 95% identical to SEQ ID NO: 30 as disclosed in International Publication No. 2014 / 183921, and has starch-degrading activity.

[0052] The hybrid amylase may conform to International Publication No. 2021 / 032881, comprising A and B domains derived from alpha-amylase from Bacillus sp. A 7-7 (DSM 12368) and a C domain derived from alpha-amylase from Bacillus cereus, preferably the A and B domains being at least 75% identical to the amino acid sequence of SEQ ID NO: 42, and the C domain being at least 75% identical to the amino acid sequence of SEQ ID NO: 44 (both sequences as disclosed in International Publication No. 2021 / 032881), and more preferably the hybrid amylase being at least 80% identical to SEQ ID NO: 54 as disclosed in International Publication No. 2021 / 032881.

[0053] Suitable amylases also include mutants of the above-mentioned amylases having starch-degrading activity. In one embodiment, amylase mutants include those having at least 40-100% identity with the full-length polypeptide sequence of the parent enzyme as disclosed above. In one embodiment, the amylase mutant having starch-degrading activity is at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical to the full-length polypeptide sequence of the parent (wild-type) enzyme as disclosed above.

[0054] In another embodiment, the present invention relates to amylase variants comprising conservative mutations unrelated to the functional domain of each amylase. The amylase variants of this embodiment having starch-degrading activity may be at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% similar to the full-length polypeptide sequence of the parent (wild-type) enzyme.

[0055] In one embodiment, the amylase mutant exhibits increased starch-degrading activity compared to the parent (wild-type) amylase, thereby possessing the starch-degrading activity according to the present invention.

[0056] In one embodiment, an amylase mutant has the starch-degrading activity according to the present invention if the amylase mutant exhibits at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the starch-degrading activity of the respective parent (wild-type) amylase.

[0057] In one embodiment, at least one amylase is selected from commercially available amylases, including but not limited to products marketed under trade names Duramyl™, Teramyl™, Fungamyl™, Stainzyme™, Stainzyme Plus™, Natalase™, Liquozyme X and BAN™, Amplify™, Amplify Prime™ (from Novozymes A / S) and Rapidase™, Purastar™, Powerase™, Effectenz™ (M100 from DuPont), Preferenz™ (S1000, S110 and F1000 from DuPont), PrimaGreen™ (all from DuPont), and Optisize™ (DuPont).

[0058] Enzymes that possess proteolytic activity are called "proteases" or "peptidases." This term includes naturally occurring proteases, so-called wild-type proteins, and their variants and mutants. A protease is an active protein that exhibits "protease activity" or "protein-degrading activity." Protein-degrading activity relates to the rate at which a protease or protease degrades a protein over a given period of time.

[0059] Methods for analyzing proteolytic activity are well-known in the literature (see, e.g., Gupta et al. (2002), Appl. Microbiol. Biotechnol. 60:381-395). Proteolytic activity can be measured by using succinyl-Ala-Ala-Pro-Phe-p-nitroanilide (Suc-AAPF-pNA, abbreviated as AAPF, see, e.g., DelMar et al. (1979), Analytical Biochem 99, 316-320) as a substrate. pNA is cleaved from the substrate molecule by proteolytic cleavage, resulting in the release of yellow free pNA, which can be quantified by measuring OD405.

[0060] Proteolytic activity can be provided in units of 1 gram of enzyme. For example, 1 U of protease may correspond to the amount of protease that releases 1 μmol per minute of forin-positive amino acids and peptides (as tyrosine) at pH 8.0 and 37°C (using casein as a substrate).

[0061] Regardless of the nature of the assay, the protease variants used in the compositions of the present invention may have at least 40%, at least 60%, at least 70%, at least 80%, at least 90%, at least 100%, or at least 110% of the amylase activity measured for the corresponding wild-type protease.

[0062] Proteases are members of class EC3.4. Examples of proteases include aminopeptidase (EC 3.4.11), dipeptidase (EC 3.4.13), dipeptidyl-peptidase and tripeptidyl-peptidase (EC 3.4.14), peptidyl-dipeptidase (EC 3.4.15), serine carboxypeptidase (EC 3.4.16), metallocarboxypeptidase (EC 3.4.17), cysteine ​​carboxypeptidase (EC 3.4.18), omegapeptidase (EC 3.4.19), serine endopeptidase (EC 3.4.21), cysteine ​​endopeptidase (EC 3.4.22), aspartate endopeptidase (EC 3.4.23), and metallo-endopeptidase (EC 3.4.23). Examples include 3.4.24), threonine endopeptidase (EC 3.4.25), or endopeptidase with an unknown catalytic mechanism (EC 3.4.99).

[0063] At least one protease may be selected from metalloendoproteases (EC 3.4.24). The metalloprotease may be another metalloprotease, such as thermolysin from family M4 or from the M5, M7, or M8 families. Metalloproteinases include, in particular, Bacillus amyloliquefaciens as described in International Publication No. 07 / 044993A2, the genera Bacillus, Brevibacillus, Thermoactinomyces, Geobacillus, Paenibacillus, Lysinibacillus or Streptomyces as described in International Publication Nos. 2014194032, 2014194054 and 2014194117, and Kribella allulminosa as described in International Publication No. 2015193488 It may be derived from *Alluminosa* and the genera *Streptomyces* and *Lysobacter* as described in International Publication No. 2016075078.

[0064] More preferably, at least one protease may be selected from serine proteases (EC 3.4.21). Serine proteases or serine peptidases are characterized by having serine in their catalytic active site, which forms a covalent adduct with the substrate during the catalytic reaction. Serine proteases can be selected from the group consisting of chymotrypsin (e.g., EC 3.4.21.1), elastase (e.g., EC 3.4.21.36), elastase (e.g., EC 3.4.21.37 or EC 3.4.21.71), granzyme (e.g., EC 3.4.21.78 or EC 3.4.21.79), kallikrein (e.g., EC 3.4.21.34, EC 3.4.21.35, EC 3.4.21.118 or EC 3.4.21.119), plasmin (e.g., EC 3.4.21.7), trypsin (e.g., EC 3.4.21.4), thrombin (e.g., EC 3.4.21.5), and subtilisin. Subtilisin is also known as subtyropeptidase, e.g., EC3.4.21.62, the latter of which will hereafter be referred to as "subtilisin" in this specification.

[0065] Subtilisin-related serine proteases share a common amino acid sequence that defines three catalytic residues that distinguish them from chymotrypsin-related serine proteases. Both subtilisin and chymotrypsin-related serine proteases have three catalytic residues containing aspartate, histidine, and serine.

[0066] In subtilisin-related proteases, the relative order of these amino acids, read from the amino terminus to the carboxyl terminus, is aspartate-histidine-serine. In chymotrypsin-related proteases, however, the relative order is histidine-aspartate-serine. Therefore, as used herein, subtilisin refers to a serine protease having the three catalytic residues of a subtilisin-related protease. Examples include subtilisins described in International Publication 89 / 06276 and European Patent No. 0283075, International Publication 89 / 06279, International Publication 89 / 09830, International Publication 89 / 09819, International Publication 91 / 06637, and International Publication 91 / 02792.

[0067] The parent proteases of the subtilisin type (EC 3.4.21.62) and mutants may be bacterial proteases. These bacterial proteases include proteases of the genera Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus, Lactococcus, Oceanobacillus, Staphylococcus, Streptococcus, or Streptomyces. These may be ram-positive bacterial polypeptides or gram-negative bacterial polypeptides such as Campylobacter, Escherichia coli, Flavobacterium, Fusobacterium, Helicobacter, Ilyobacter, Neisseria, Pseudomonas, Salmonella, or Ureaplasma proteases. An overview of this family is provided, for example, in "Subtilases: Subtilisin-like proteases" by R. Siezen, pages 75-95 (in "Subtilisin enzymes", edited by R. Bott and C. Betzel, New York, 1996).

[0068] In one aspect of the present invention, the parent enzyme and mutant are Bacillus alcalophilus, Bacillus amyloliquefaciens, Bacillus brevis, Bacillus circulans, Bacillus clausii, Bacillus coagulans, Bacillus firmus, Bacillus gibsonii, Bacillus lautus, Bacillus lentus, Bacillus licheniformis, Bacillus megatherium It may be a protease of Bacillus megaterium, Bacillus pumilus, Bacillus sphaericus, Bacillus stearothermophilus, Bacillus subtilis, or Bacillus thuringiensis.

[0069] For the purposes of the present invention, at least one protease is a subtilisin derived from Bacillus amyloliquefaciens BPN' (described by Vasantha et al. (1984) J. Bacteriol. Volume 159, pp. 811-819 and JA Wells et al. (1983) (Nucleic Acids Research, Volume 11, pp. 7911-7925)), a subtilisin derived from Bacillus licheniformis (subtilisin Carlsberg, EL Smith et al. (1968) (J. Biol Chem, Volume 243, pp. 2184-2191) and Jacobs et al. (1985) (Nucl. Acids Res, Vol. Subtilisin PB92 (disclosed in 13, pp. 8913-8926), subtilisin PB92 (the original sequence of alkaline protease PB92 is described in European Patent Application Publication No. 283075A2), subtilisin 147 and / or 309 (Esperase® and Savinase®, respectively) as disclosed in International Publication No. 89 / 06279, subtilisin derived from Bacillus lentus as disclosed in International Publication No. 91 / 02792, for example, Bacillus lentus DSM 5483 or a variant of Bacillus lentus DSM 5483 as described in International Publication No. 95 / 23221, Bacillus alkalophilus (disclosed in German Patent No. 10064983) Subtilisin derived from *Bacillus alcalophilus* (DSM 11233), subtilisin derived from *Bacillus gibsonii* (DSM 14391) as disclosed in International Publication No. 2003 / 054184, and *Bacillus sp.* species disclosed in International Publication No. 2003 / 056017.The subtilisin is selected from the following: subtilisin derived from (DSM 14390), subtilisin derived from Bacillus sp. (DSM 14392) disclosed in International Publication No. 2003 / 055974, subtilisin derived from Bacillus gibsonii (DSM 14393) disclosed in International Publication No. 2003 / 054184, subtilisin having Sequence ID No. 4 as described in International Publication No. 2005 / 063974, subtilisin having Sequence ID No. 4 as described in International Publication No. 2005 / 103244, subtilisin having Sequence ID No. 7 as described in International Publication No. 2005 / 103244, and subtilisin having Sequence ID No. 2 as described in German Patent Application Publication No. 102005028295.4.

[0070] Suitable proteases include variants of the above-mentioned proteases that have proteolytic activity. In one embodiment, the protease variant is a variant that has at least 40-100% identity with the full-length polypeptide sequence of the parent enzyme as disclosed above. In one embodiment, the protease variant having proteolytic activity is at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identity with the full-length polypeptide sequence of the parent (wild-type) enzyme as disclosed above.

[0071] In other embodiments, the present invention relates to protease variants comprising conservative mutations independent of the functional domain of each protease. The protease variants of this embodiment having proteolytic activity are at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% similar to the full-length polypeptide sequence of the parent (wild-type) enzyme.

[0072] In one embodiment, the protease mutant has the proteolytic activity according to the present invention if the protease mutant exhibits increased proteolytic activity when compared to the parent protease.

[0073] A suitable subtilisine may be at least 80% identical to Sequence ID No. 22 as described in European Patent No. 1921147, and is characterized by containing one amino acid (according to (a) to (h)) or a combination according to (i) with amino acids 101E, 101D, 101N, 101Q, 101A, 101G, or 101S (according to BPN numbering), and has proteolytic activity.

[0074] In one embodiment, the subtilizine is at least 80% identical to Sequence ID No. 22 as described in European Patent No. 1921147, and is characterized by containing the mutation (according to BPN numbering) R101E, or S3T+V4I+V205I, or S3T+V4I+R101E+V205I, or S3T+V4I+V199M+V205I+L217D, and has proteolytic activity.

[0075] In another embodiment, the subtilizine comprises an amino acid sequence that is at least 80% identical to Sequence ID No. 22 as described in European Patent No. 1921147, and is further characterized by comprising S3T+V4I+S9R+A15T+V68A+D99S+R101S+A103S+I104V+N218D (according to BPN numbering), and has proteolytic activity.

[0076] Subtilisine is at least 80% identical to Sequence ID No. 22 as described in European Patent No. 1921147, and is R101E, S156D, L262E, Q137H, S3T, R45E, D, Q, P55N, T58W, Y, L, Q59D, M, N, T, G61D, R, S87E, G97S, A98D, E, R, S106A, W, N117E, H120V, D, K, N, S125M, P129D, E136Q, S14 It may have an amino acid sequence further characterized by including one or more substitutions selected from the group consisting of 4W, S161T, S163A, G, Y171L, A172S, N185Q, V199M, Y209W, M222Q, N238H, V244T, N261T, D and L262N, Q, D (as described in International Publication No. 2016 / 096711 and according to BPN numbering), and possesses proteolytic activity.

[0077] At least one protease is sold under the trade names Alcalase(registered trademark), Blaze(registered trademark), Duralase(trademark), Durazym(trademark), Relase(registered trademark), Relase(registered trademark) Ultra, Savinase(registered trademark), Savinase(registered trademark) Ultra, Primase(registered trademark), Polarzyme(registered trademark), Kannase(registered trademark), Liquanase(registered trademark), Liquanase(registered trademark) Ultra, Ovozyme(registered trademark), Coronase(registered trademark), Coronase(registered trademark) Ultra, Neutrase(registered trademark), Everlase(registered trademark) and Esperase(registered trademark) (Novozymes A / S), as well as Maxatase(registered trademark), Maxacal(registered trademark), Maxapem(registered trademark), Purafect(registered trademark), Purafect(registered trademark) Prime, Purafect MA(registered trademark), Purafect Ox(registered trademark), and Purafect Products may be selected from commercially available products including, but not limited to, OxP®, Puramax®, Properase®, FN2®, FN3®, FN4®, Excellase®, Eraser®, Ultimase®, Opticlean®, Effectenz®, Preferenz®, and Optimase® (Danisco / DuPont), Axapem® (Gist-Brocases NV), Bacillus lentus Alkaline Protease (BLAP, sequence shown in Figure 29 of U.S. Patent No. 5,352,604) and their variants, and KAP (Bacillus alkalophilus subtilisin) manufactured by Kao Corporation.

[0078] Known alignment methods include a variety of methods that can be used to align two given nucleic acids or amino acid sequences and to calculate the degree of identity; see, for example, Arthur Lesk (2008), Introduction to bioinformatics, Oxford University Press, 2008, 3rd edition. In a preferred embodiment, ClustalW software (Larkin, MA, Blackshields, G., Brown, NP, Chenna, R., McGettigan, PA, McWilliam, H., Valentin, F., Wallace, IM, Wilm, A., Lopez, R., Thompson, JD, Gibson, TJ, Higgins, DG (2007): Clustal W and Clustal X version 2.0. Bioinformatics, 23, 2947-2948) is used with default settings applied.

[0079] In preferred embodiments, the amylase and / or protease of the composition of the present invention is a wild-type (naturally occurring) enzyme or a mutant thereof that still binds to calcium.

[0080] In other preferred embodiments, the liquid cleaning composition of the present invention comprises amylase and protease.

[0081] Embodiment 5 The liquid cleaning composition according to Embodiment 4(b), further comprising a protease stabilization system containing peptaldehyde.

[0082] In further embodiments, the liquid cleaning composition of the present invention does not contain boric acid, boronic acid, or derivatives thereof. In even more preferred embodiments, the cleaning composition comprises only one single protease stabilization system, which is a protease stabilization system containing peptaldehyde.

[0083] Preferably, the liquid cleaning compositions described herein contain an enzyme / protease stabilization system in an amount of about 0.001% to about 10% by weight, about 0.005% to about 8% by weight, or about 0.01% to about 6% by weight of the composition. The enzyme / protease stabilization system may be any stabilization system compatible with the enzyme.

[0084] Preferably, the enzyme stabilization system includes at least one compound selected from the group consisting of polyols (preferably 1,3-propanediol, ethylene glycol, glycerol, 1,2-propanediol, or sorbitol), inorganic salts (preferably CaCl2, MgCl2, or NaCl), and short-chain (preferably C1-C3) carboxylic acids or their salts (preferably formic acid, formate (preferably sodium formate), acetic acid, acetate, or lactate). More preferably, the protease stabilization system containing peptaldehyde is a peptaldehyde selected from Z-VAL-H or Z-GAY-H, peptide acetals, and peptaldehyde hydrosulfite adducts. Preferably, the protease stabilization system may include a combination of (i) at least two compounds selected from the group consisting of salts, polyols, and short-chain carboxylic acids, and (ii) one or more compounds selected from the group consisting of peptaldehydes, peptide acetals, and peptaldehyde hydrosulfite adducts.

[0085] Embodiment 6 At least one anionic surfactant, (a) present in an amount ranging from 2% to 40% by weight of the composition, preferably 3% to 30% by weight, most preferably 4% to 25% by weight, and / or (b) A liquid cleaning composition according to any one of Embodiments 1 to 5, selected from the group consisting of linear alkylbenzene sulfonate (LAS), alkyl sulfate (AS), alkyl alkoxy sulfate (AExS), alkyl alkoxycarboxylate, modified alkylbenzene sulfonate (MLAS), methyl ester sulfonate (MES), alkyl sulfosuccinate and alpha-olefin sulfonate (AOS).

[0086] Useful herein - combinations of two or more surfactants may also be used - non-limiting examples of anionic surfactants include C9-C20 linear alkylbenzene sulfonates (LAS), C10-C20 primary, branched, and random alkyl sulfates (AS), C10-C18 secondary (2,3) alkyl sulfates, C10-C18 alkyl alkoxy sulfates (AExS) (wherein x is 1-30), C10-C18 alkyl alkoxycarboxylates containing 1-5 ethoxy units, as discussed in U.S. Patent No. 6,020,303 and U.S. Patent No. 6,060,443. Examples include medium-chain branched alkyl sulfates, medium-chain branched alkylalkoxysulfates as discussed in U.S. Patent No. 6,008,181 and U.S. Patent No. 6,020,303, modified alkylbenzene sulfonates (MLAS), methyl ester sulfonates (MES), and alpha-olefin sulfonates (AOS) as discussed in International Publication No. 99 / 05243, International Publication No. 99 / 05242, and International Publication No. 99 / 05244.

[0087] Preferred examples of suitable anionic surfactants include alkali metal and ammonium salts of soaps such as C8-C12 alkyl sulfates, C12-C18 fatty alcohol ether sulfates, C12-C18 fatty alcohol polyether sulfates, sulfuric acid half-esters of ethoxylated C4-C12 alkylphenols (ethoxylation: 3-50 moles of ethylene oxide / mol), C12-C18 alkyl sulfonic acids, C12-C18 sulfo fatty acid alkyl esters, for example, C12-C18 sulfo fatty acid methyl esters, C10-C18 alkylaryl sulfonic acids, preferably n-C10-C18 alkylbenzene sulfonic acids, C10-C18 alkyl alkoxycarboxylic acids, and soaps such as C8-C24 carboxylic acids. Alkali metal salts of the aforementioned compounds, particularly preferably sodium salts, are preferred.

[0088] In one embodiment of the present invention, the anionic surfactant is selected from n-C10-C18 alkylbenzene sulfonic acids and fatty alcohol polyether sulfates, which, in relation to the present invention, are particularly ethoxylated C12-C18 alkanols (ethoxylation: 1-50 moles of ethylene oxide / mol), preferably sulfuric acid hemiesters of n-C12-C18 alkanols.

[0089] In one embodiment of the present invention, alcohol polyether sulfates derived from branched (i.e., synthetic) C11-C18 alkanols (ethoxylated: 1-50 moles of ethylene oxide / mol) may also be used.

[0090] Preferably, the alkoxylylated group of both types of alkoxylylated alkyl sulfates, whether based on C12-C18 fatty alcohols or branched (i.e., synthetic) C11-C18 alcohols, is an ethoxylated group, and the average degree of ethoxylation of any of the alkoxylylated alkyl sulfates is 1-5, preferably 1-3.

[0091] In further embodiments of the present invention, the anionic surfactant is selected from biosurfactants, preferably rhamnolipids (RL), mannosylerythritol lipids (MEL), trehalose lipids (TL), cellobiose lipids (CL), and / or sophorolipids (SL).

[0092] In preferred embodiments of the present invention, the anionic surfactant is selected from C10-C15 linear alkylbenzene sulfonates, C10-C18 alkyl ether sulfonates having 1-5 ethoxy units, and C10-C18 alkyl sulfonates.

[0093] When the liquid cleaning composition of the present invention contains one or more anionic surfactants, the amount in the range of 2% to 40% by weight, preferably 3% to 30% by weight, and most preferably 4% to 25% by weight of the composition refers to the total amount of all anionic surfactants (i.e., % first anionic surfactant + % second anionic surfactant + ... = % total anionic surfactants).

[0094] Embodiment 7 Calcium (Ca 2+ The liquid cleaning composition according to any one of Embodiments 1 to 6, wherein the component is present in an amount ranging from 0.0001% to 3% by weight, preferably from 0.001% to 1% by weight, of the composition.

[0095] In preferred embodiments, the lower limit of the calcium concentration is 0.0005% by weight, 0.001% by weight, or 0.005% by weight of the composition of the present invention. In other preferred embodiments, the upper limit of the calcium concentration is 2.5% by weight, 2% by weight, or 1.5% by weight of the composition of the present invention.

[0096] In a further embodiment, the above-mentioned calcium (Ca 2+ ) is free calcium. This means that it is not part of a covalent interaction, it does not form salt interactions (in the long term), and it is not complexed by builders (chelating agents).

[0097] Furthermore, in a preferred embodiment, the liquid cleaning composition of the present invention is magnesium (Mg 2+ The composition contains ) in an amount ranging from 0.0001% to 3% by weight, more preferably from 0.001% to 1% by weight.

[0098] In preferred embodiments, the lower limit of the magnesium concentration is 0.0005% by weight, 0.001% by weight, or 0.005% by weight of the composition of the present invention. In other preferred embodiments, the upper limit of the calcium concentration is 2.5% by weight, 2% by weight, or 1.5% by weight of the composition of the present invention.

[0099] In further embodiments, the above-mentioned magnesium (Mg 2+ ) is free calcium. This means that it is not part of a covalent interaction, it does not form salt interactions (in the long term), and it is not complexed by builders (chelating agents).

[0100] Techniques for measuring the concentration of calcium and / or magnesium are well known in the art and include atomic absorption spectroscopy (AA), inductively coupled plasma atomic emission spectroscopy (ICP-AES), and inductively coupled plasma mass spectroscopy (ICP-MS).

[0101] Embodiment 8 A liquid cleaning composition according to any one of Embodiments 1 to 7, wherein the viscosity is in the range of 30 to 3000 mPa*s, preferably 40 to 2500 mPa*s, and most preferably 50 to 2000 mPa*s.

[0102] In a preferred embodiment, the lower limit of viscosity of the composition of the present invention is 35 mPa*s or 45 mPa*s. In another preferred embodiment, the upper limit of viscosity of the composition of the present invention is 2800 mPa*s, 2300 mPa*s, or 2100 mPa*s.

[0103] All of the viscosity values ​​mentioned above are for 20 1 / s and / or 20°C.

[0104] Viscosity can be measured using a viscometer or rheometer, which are well known to those skilled in the art.

[0105] Embodiment 9 A liquid cleaning composition according to any one of Embodiments 1 to 8, wherein the pH value is in the range of 5 to 12, preferably 6 to 10, and most preferably 7 to 9.

[0106] The pH value can be measured using pH paper, a colorimeter, or a fluorophotometer. pH indicators are known in the art and include gentian violet, malachite green, thymol blue, methyl yellow, methylene blue, bromophenol blue, Congo red, methyl orange, shielded methyl orange, bromocresol green, methyl red, methyl purple, azolitmine (litmus), bromocresol purple, bromothymol blue, phenol red, neutral red, naphtholphthalein, cresol red, cresolphthalein, phenolphthalein, thymorphain, alizarin yellow R, and indigo carmine.

[0107] The pH of the composition may be adjusted using pH-modifying components known in the art, and is measured as a 10% by weight product concentration in desalted water at 25°C. For example, NaOH may be used, and the measured weight % of NaOH can be varied to adjust to a desired pH such as pH 8.0. In one embodiment of the present invention, pH above 7 is adjusted by using an amine, preferably an alkanolamine, more preferably a triethanolamine.

[0108] Embodiment 10 A liquid cleaning composition according to any one of Embodiments 1 to 9, which is a detergent composition. Alternatively, the liquid cleaning composition is an automatic dishwashing (ADW) gel.

[0109] As used herein, the term “cleaning composition” includes compositions and formulations designed to clean soiled materials. Such compositions and formulations include those designed to clean any type of soiled material or surface.

[0110] Examples of compositions for "commercial cleaning" include hard surface cleaners for any type of surface, including tiles, carpets, PVC surfaces, wood surfaces, metal surfaces, and lacquered surfaces, and other cleaning compositions designed for use in commercial cleaning to clean any type of soiled material or surface.

[0111] "Compositions for Fabrics and Home Care" include, but are not limited to, laundry cleaning compositions and detergents, fabric softening compositions, fabric performance compositions, fabric cooling compositions, laundry pre-washing agents, laundry pre-treatment agents, laundry additives, spray products, dry cleaning agents or compositions, laundry rinsing agents, cleaning additives, post-rinse fabric treatment agents, ironing aids, dishwashing compositions, hard surface cleaning compositions, unit dose formulations, delayed delivery formulations, detergents contained on or in porous substrates or nonwoven sheets, and other preferred forms that may be apparent to those skilled in the art in view of the teachings herein and which may be further detailed herein when describing the compositions. Such compositions may be used as pre-laundry treatment products, post-laundry treatment products, or may be added during the rinse or wash cycle of a laundry operation, preferably during the wash cycle of a laundry or dishwashing operation, and as further detailed herein.

[0112] The cleaning compositions of the present invention may be in any liquid form, i.e., liquid, paste, pouch, gel, emulsion, type delivered in two or multi-compartment containers, single-phase or multi-phase unit doses, spray or foam detergent, wet-type wiping fibers (i.e., cleaning compositions combined with nonwoven materials, such as those discussed in U.S. Patent No. 6,121,165, Mackey, et al.), and other homogeneous, heterogeneous, single-phase or multi-phase cleaning product forms.

[0113] Embodiment 11 A liquid cleaning composition according to any one of Embodiments 1 to 10, further comprising at least one element from the group consisting of non-anionic surfactants, amphoteric surfactants, cobuilders, alcohols, biocides, thickeners, water-soluble polymers, mud stain removers / anti-re-adhesion agents, polymer stain release agents, bleaches, bleaching activators, gloss agents, odor suppressants, pigments, dyes, opacifiers, colorants, color transfer inhibitors, anti-foaming agents, corrosion inhibitors, softeners, and fragrances.

[0114] In preferred embodiments, the liquid cleaning composition of the present invention comprises further enzymes in addition to amylase and protease. The upper limit of the concentration of the further enzymes is 5% by weight, 3% by weight, 2% by weight, 1% by weight, 0.5% by weight, 0.1% by weight, 0.01% by weight, or even 0% by weight (meaning that the composition of the present invention lacks further enzymes in addition to amylase and protease).

[0115] In preferred embodiments, the liquid cleaning composition of the present invention comprises an additional builder compound in addition to EDDS. The upper limit of the concentration of the additional builder compound is 20% by weight, 15% by weight, 10% by weight, 7% by weight, 5% by weight, 3% by weight, 1% by weight, 0.5% by weight, or even 0% by weight of the composition of the present invention (meaning the composition of the present invention lacks the additional builder compound in addition to EDDS).

[0116] The cleaning composition of the present invention may contain—preferably contain—auxiliary cleaning additives (also abbreviated as “auxiliaries” herein), and such auxiliary agents are preferably added to components (i) to (v) as defined in Embodiment 1.

[0117] Suitable auxiliary cleaning additives include builders, co-builders, structuring agents or thickeners, mud removers / anti-re-adhesion agents, polymer dirt release agents, polymer dispersants, polymer oil cleaners, solubilizers, chelating agents, further enzymes, enzyme stabilizers, further surfactants, bleaching compounds, bleaching agents, bleaching activators, bleaching catalysts, fluorescent whitening agents, odor suppressants, pigments, dyes, opacifiers, colorants, color transfer inhibitors, chelating agents, foaming accelerators, anti-foaming agents (defoamers), colored particles, silver cleaners, anti-tarnish and / or anti-corrosion agents, alkaline sources, pH adjusters, pH buffers, hydrotropes, scrub particles, antimicrobial agents, antioxidants, softeners, carriers, processing aids, fragrance precursors, dye fixatives, and fragrances.

[0118] The liquid cleaning composition may contain rheology control / modifiers, emollients, moisturizers, skin rejuvenating active substances, and solvents.

[0119] Suitable examples of such cleaning aids and levels of use can be found in International Publication No. 99 / 05242, U.S. Patent No. 5,576,282, U.S. Patent No. 6,306,812B1 and U.S. Patent No. 6,326,348B1.

[0120] Those skilled in the art will understand that a cleaning surfactant encompasses any surfactant or mixture of surfactants that provides cleaning, stain removal, or laundry benefits to soiled materials.

[0121] Therefore, the cleaning compositions of the present invention for fabrics and home care products, and formulations for commercial cleaning, more specifically, for example, laundry and manual dishwashing detergents, preferably further comprise components (i) to (v) and preferably further auxiliary agents as described in more detail above and below.

[0122] In addition to anionic surfactants, the liquid cleaning compositions of the present invention may contain additional surfactant systems, which may consist of one surfactant or a combination of surfactants selected from nonionic surfactants, cationic surfactants, zwitterionic surfactants, amphoteric surfactants, and mixtures thereof. Those skilled in the art will understand that surfactant systems for detergents encompass any of the described surfactants or mixtures of surfactants that provide cleaning, stain removal, or laundry benefits to soiled materials.

[0123] The cleaning compositions of the present invention preferably contain a sufficient amount of surfactant system to provide the desired cleaning properties. In some embodiments, the additional cleaning composition contains about 0.1% to about 70% by weight of surfactant system by the weight of the composition. In other embodiments, the liquid cleaning composition contains about 2% to about 60% by weight of surfactant system by the weight of the composition. In further embodiments, the cleaning composition contains about 5% to about 30% by weight of surfactant system by the weight of the composition. The surfactant system may include cleaning surfactants selected from nonionic surfactants, cationic surfactants, zwitterionic surfactants, amphoteric surfactants and mixtures thereof.

[0124] It can also be used in combination with two or more other surfactants - non-limiting examples of nonionic surfactants include C8-C18 alkyl ethoxylates, e.g., Shell's NEODOL® nonionic surfactant, ethylene oxide / propylene oxide blocked alkoxylates such as BASF's PLURONIC®, C14-C22 medium-chain branched alkyl alkoxylates, BAEx (wherein x is 1-30), as discussed in U.S. Patents 6,153,577, 6,020,303 and 6,093,856, and BAEx (wherein x is 1-30). Examples include alkyl polysaccharides, such as those discussed in Llenado's U.S. Patent No. 4,565,647, issued on January 26, 1986; alkyl polyglycosides, particularly those discussed in U.S. Patents No. 4,483,780 and 4,483,779; polyhydroxy fatty acid amides, such as those discussed in U.S. Patent No. 5,332,528; and ether-capped poly(oxyalkylated) alcohol surfactants, such as those discussed in U.S. Patent No. 6,482,994 and International Publication No. 01 / 42408.

[0125] Preferred examples of nonionic surfactants include, specifically, alkoxylated alcohols and alkoxylated fatty alcohols, diblock and multiblock copolymers of ethylene oxide and propylene oxide, reaction products of sorbitan with ethylene oxide or propylene oxide, as well as alkylphenol ethoxylates, alkyl glycosides, and polyhydroxy fatty acid amides (glucamides).

[0126] It can also be used in combination with two or more other surfactants - non-limiting examples of nonionic surfactants include C8-C18 alkyl ethoxylates, e.g., Shell's NEODOL® nonionic surfactant, ethylene oxide / propylene oxide blocked alkoxylates such as BASF's PLURONIC®, C14-C22 medium-chain branched alkyl alkoxylates as discussed in U.S. Patent Nos. 6,153,577, 6,020,303 and 6,093,856, BAEx (wherein x is 1-30), 19 Examples include alkyl polysaccharides, such as those discussed in Llenado's U.S. Patent No. 4,565,647, issued on January 26, 1986; alkyl polyglycosides, particularly those discussed in U.S. Patents No. 4,483,780 and 4,483,779; polyhydroxy fatty acid amides, such as those discussed in U.S. Patent No. 5,332,528; and ether-capped poly(oxyalkylated) alcohol surfactants, such as those discussed in U.S. Patent No. 6,482,994 and International Publication No. 01 / 42408.

[0127] Preferred examples of nonionic surfactants include, specifically, alkoxylated alcohols and alkoxylated fatty alcohols, diblock and multiblock copolymers of ethylene oxide and propylene oxide, reaction products of sorbitan with ethylene oxide or propylene oxide, as well as alkylphenol ethoxylates, alkyl glycosides, and polyhydroxy fatty acid amides (glucamides).

[0128] Preferred examples of alkoxylated alcohols and alkoxylated fatty alcohols include, for example, general formula (A): [ka] (In the formula, the variables are defined as follows: R1 is selected from linear C1-C10 alkyl groups, preferably ethyl, and particularly preferably methyl. R2 is selected from C8-C22 alkyl groups, for example, n-C8H17, n-C10H21, n-C12H25, n-C14H29, n-C16H33, or n-C18H37. R3 is selected from C1-C10-alkyl, methyl, ethyl, n-propyl, isopropyl, n-butyl, isobutyl, sec-butyl, tert-butyl, n-pentyl, isopentyl, sec-pentyl, neopentyl, 1,2-dimethylpropyl, isoamyl, n-hexyl, isohexyl, sec-hexyl, n-heptyl, n-octyl, 2-ethylhexyl, n-nonyl, n-decyl, or isodecyl. (m and n are in the range of 0 to 300, and the sum of n and m is at least 1.) It is a compound of [the compound].

[0129] Preferably, m is in the range of 1 to 100, and n is in the range of 0 to 30.

[0130] In this specification, the compound of general formula (A) may be a block copolymer or a random copolymer, with block copolymers being preferred.

[0131] Other preferred examples of alkoxylated alcohols and alkoxylated fatty alcohols include, for example, general formula (B): [ka] (In the formula, the variables are defined as follows: R1 is either the same or different, selected from linear C1-C4 alkyl groups, preferably the same in each case, and is ethyl, particularly preferably methyl. R4 is selected from C6-C20 alkyl groups, specifically n-C8H17, n-C10H21, n-C12H25, n-C14H29, n-C16H33, and n-C18H37. a is a number in the range of 0 to 6, preferably 1 to 6. b is a number in the range of 0 to 20, preferably 4 to 20. (d is a number in the range of 4 to 25) It is a compound of [the compound].

[0132] Preferably, at least one of a and b is greater than zero.

[0133] In this specification, the compound of general formula (B) may be a block copolymer or a random copolymer, with block copolymers being preferred.

[0134] Further preferred nonionic surfactants are selected from diblock and multiblock copolymers composed of ethylene oxide and propylene oxide. Further preferred nonionic surfactants are selected from ethoxylated or propoxylated sorbitan esters. Alkylphenol ethoxylates, alkyl polyglycosides, or polyhydroxy fatty acid amides (glucamides) are similarly preferred. An overview of further preferred nonionic surfactants can be found in European Patent Application Publication No. 0851023A and German Patent Application Publication No. 19819187A.

[0135] Naturally, mixtures of two or more different nonionic surfactants can also exist.

[0136] In preferred embodiments of the present invention, the nonionic surfactant is selected from C12 / 14 and C16 / 18 fatty alcohol alkoxylates, C13 / 15 oxo alcohol alkoxylates, C13 alcohol alkoxylates, and 2-propylheptyl alcohol alkoxylates, each of which has 3 to 15 ethoxy units, preferably 4 to 10 ethoxy units or 1 to 3 propoxy units and 2 to 15 ethoxy units.

[0137] Combinations of two or more other surfactants may also be used. Non-limiting examples of amphoteric surfactants include water-soluble amine oxides containing one alkyl moiety of about 8 to about 18 carbon atoms and two moieties selected from the group consisting of alkyl moieties and hydroxyalkyl moieties containing about 1 to about 3 carbon atoms, and water-soluble sulfoxides containing one alkyl moiety of about 10 to about 18 carbon atoms and a moiety selected from the group consisting of alkyl moieties and hydroxyalkyl moieties containing about 1 to about 3 carbon atoms. See International Publication No. 01 / 32816, U.S. Patent No. 4,681,704 and U.S. Patent No. 4,133,779. Thus, suitable surfactants include so-called amine oxides, such as lauryldimethylamine oxide ("lauramine oxide").

[0138] A preferred example of an amphoteric surfactant is an amine oxide. Preferred amine oxides are alkyldimethylamine oxide or alkylamidopropyldimethylamine oxide, more preferably alkyldimethylamine oxide, and especially coconut oil dimethylamino oxide. Amine oxides may have a linear or mid-branched alkyl moiety. Typical linear amine oxides include water-soluble amine oxides containing one R1=C8-18 alkyl moiety and two R2 and R3 moieties selected from the group consisting of C1-C3 alkyl groups and C1-C3 hydroxyalkyl groups. Preferably, the amine oxide has the formula: R1-N(R2)(R3)-O (In the formula, R1 is a C8-18 alkyl group, and R2 and R3 are selected from the group consisting of methyl, ethyl, propyl, isopropyl, 2-hydroxyethyl, 2-hydroxypropyl, and 3-hydroxypropyl.) Characterized by the following: Examples of linear amine oxide surfactants include linear C10-C18 alkyldimethylamine oxides and linear C8-C12 alkoxyethyl dihydroxyethylamine oxides. Preferred amine oxides include linear C10, linear C10-C12, and linear C12-C14 alkyldimethylamine oxides. As used herein, “internal branching” means that the amine oxide has one alkyl moiety having n1 carbon atoms, and one alkyl branch on this alkyl moiety having n2 carbon atoms. This alkyl branch is located on the alpha carbon of the nitrogen of the alkyl moiety. This type of branching for amine oxides is also known in the art as internal amine oxides. The sum of the number of carbon atoms of n1 and n2 is 10-24 carbon atoms, preferably 12-20, more preferably 10-16. The number of carbon atoms of one alkyl moiety (n1) needs to be approximately the same as the number of carbon atoms of one alkyl branch (n2) so that this alkyl moiety and one alkyl branch are symmetrical. As used herein, “symmetric” means that at least 50% by weight, more preferably at least 75% to 100% by weight of the internally branched amine oxide for use herein, (n1-n2) is 5 or less, preferably 4, most preferably 0 to 4 carbon atoms. The amine oxide further comprises two portions independently selected from C1-C3 alkyl, C1-C3 hydroxyalkyl, or polyethylene oxide groups comprising about 1 to about 3 ethylene oxide groups on average. Preferably, these two portions are selected from C1-C3 alkyl, more preferably both are selected as C1 alkyl.

[0139] In preferred embodiments of the present invention, the amphoteric surfactant is selected from C8-C18 alkyl-dimethylamine oxide and C8-C18 alkyl-di(hydroxyethyl)amine oxide.

[0140] The cleaning composition may also contain zwitterionic surfactants, which can be used in combination with two or more other surfactants.

[0141] Suitable zwitterionic surfactants include betaines such as alkyl betaines, alkylamide betaines, amidazolinium betaines, sulfobetaines (sultaine in INCI), and phosphobetaines. Examples of suitable betaines and sulfobetaines are listed below (as shown according to INCI): almondamidopropyl betaine, apricotamidopropyl betaine, avocadoamidopropyl betaine, babassuamidopropyl betaine, behenamidopropyl betaine, behenyl betaine, canolaamidopropyl betaine, capryl / capramidopropyl betaine, carnitine, cetyl betaine, cocamidoethyl betaine, cocamidopropyl betaine, cocamidopropyl hydroxysulfopropyl betaine. Betaine, Cocobetaine, Cocohydroxysultaine, Coco / Oleamidopropyl Betaine, Cocosultaine, Decyl Betaine, Dihydroxyethyl Oleyl Glycinate, Dihydroxyethyl Soybean Alkyl Glycinate, Dihydroxyethyl Stearyl Glycinate, Dihydroxyethyl Beef Tallow Glycinate, Dimethicone Propyl PG Betaine, Elcamidopropyl Hydroxysultaine, Hydrogenated Beef Tallow Betaine, Isostearamidopropyl Betaine, Lauramidopropyl Betaine, These include lauryl betaine, lauryl hydroxysultaine, lauryl sultaine, milk fat fatty acid amidopropyl betaine, mink oil fatty acid amidopropyl betaine, myristamidopropyl betaine, myristyl betaine, oleamidopropyl betaine, oleamidopropyl hydroxysultaine, oleyl betaine, olive amidopropyl betaine, palm oil fatty acid amidopropyl betaine, palmitamidopropyl betaine, palmitoyl carnitine, palm kernel oil fatty acid amidopropyl betaine, polytetrafluoroethylene acetoxypropyl betaine, ricinoleic acid amidopropyl betaine, sesamidopropyl betaine, soybean oil fatty acid amidopropyl betaine, stearamidopropyl betaine, stearyl betaine, beef tallow fatty acid amidopropyl betaine, beef tallow fatty acid amidopropyl hydroxysultaine, beef tallow betaine, beef tallow dihydroxyethyl betaine, undecylenamidopropyl betaine, and wheat germ oil fatty acid amidopropyl betaine.

[0142] Preferred betaines are, for example, C12-C18 alkyl betaines and sulfobetaines. The zwitterionic surfactant is preferably a betaine surfactant, more preferably a cocamidopropyl betaine surfactant. Non-limiting examples of cationic surfactants that can also be used in combination with two or more other surfactants include quaternary ammonium surfactants that may have up to 26 carbon atoms, such as alkoxylated quaternary ammonium (AQA) surfactants as discussed in U.S. Patent No. 6,136,769, dimethylhydroxyethyl quaternary ammonium as discussed in U.S. Patent No. 6,004,922, dimethylhydroxyethyl laurylammonium chloride, and brochures 98 / 35002, 98 / 35003, and 98 / 35 Examples include polyamine cationic surfactants as discussed in Brochure 004, International Publication No. 98 / 35005, and International Publication No. 98 / 35006; cationic ester surfactants as discussed in U.S. Patent Nos. 4,228,042, 4,239,660, 4,260,529, and 6,022,844; and amino surfactants as discussed in U.S. Patent No. 6,221,825 and International Publication No. 00 / 47708, specifically amidopropyldimethylamine (APA).

[0143] The compositions according to the present invention may or may not include an additional builder to the EDDS. In relation to the present invention, there will be no distinction between a builder and a component that may otherwise be called a "cobuilder." Examples of builders are complexing agents, also known as ion exchange compounds and precipitating agents. Builders are selected from citrates, phosphates, silicates, carbonates, phosphonates, aminocarboxylates, and polycarboxylates.

[0144] In a preferred embodiment, the additional builder is diethylenetriamine penta(methylenephosphonic acid) (DTPMP).

[0145] The formulation according to the present invention may contain one or more alkali carriers. The alkali carrier ensures a pH of at least 9, for example, when an alkaline pH is desired. For example, alkali metal carbonates, alkali metal bicarbonates, and alkali metal metasilicates mentioned above, as well as alkali metal hydroxides, are also preferred. In any case, the preferred alkali metal is potassium, with sodium being particularly preferred. In one embodiment of the present invention, the pH is adjusted to greater than 7 by using an amine, preferably an alkanolamine, and more preferably a triethanolamine.

[0146] In one embodiment of the present invention, the composition or laundry formulation according to the present invention further comprises at least one enzyme in addition to amylase and protease.

[0147] In a more preferred embodiment, calcium and / or magnesium are not cofactors or are not required for the catalytic activity of the additional enzyme.

[0148] Preferably, at least one additional enzyme is a detergent enzyme.

[0149] In one embodiment, the additional enzyme is classified as an oxidoreductase (EC 1), transferase (EC 2), hydrolase (EC 3), lyase (EC 4), isomerase (EC 5), or ligase (EC 6). The EC numbering follows the Enzyme Nomenclature, Recommendations (1992) of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology, including its supplements published between 1993 and 1999. Preferably, the enzyme is a hydrolase (EC 3).

[0150] In preferred embodiments, additional enzymes include proteases, amylases, lipases, cellulases, mannanases, hemicellulases, phospholipases, esterases, pectinases, lactases, peroxidases, xylanases, cutinases, pectinate lyases, keratinases, reductases, oxidases, phenol oxidases, lipoxygenases, ligninases, pullulanases, tanases, pentosanases, maranases, beta-glucanases, arabinosidases, hyaluronidases, chondroitinases, laccases, nucleases, DNases, phosphodiesterases, and phyta The enzyme is selected from the group consisting of -ase, carbohydrase, galactanase, xanthanase, xyloglucanase, oxidoreductase, perhydrolase, aminopeptidase, asparaginase, carbohydrase, carboxypeptidase, catalase, chitinase, cyclodextrin glycosyltransferase, alpha-galactosidase, beta-galactosidase, glucoamylase, alpha-glucosidase, beta-glucosidase, invertase, ribonuclease, transglutaminase, and dispersin, as well as combinations of at least two of the aforementioned types. More preferably, the enzyme is selected from the group consisting of protease, amylase, lipase, cellulase, mannanase, xylanase, DNase, dispersin, pectinase, oxidoreductase, and cutinase, as well as combinations of at least two of the aforementioned types. Most preferably, the additional enzyme is mannans and / or lipase.

[0151] Additional enzymes may be incorporated into the composition in a quantity sufficient to provide an effective amount for achieving beneficial effects, preferably a primary washing effect and / or a secondary washing effect such as an anti-graying or anti-pilling effect (e.g., in the case of cellulase). Preferably, the additional enzymes are present in the composition at a level of enzyme protein of about 0.00001% to about 5% by weight, preferably about 0.00001% to about 2% by weight, more preferably about 0.0001% to about 1% by weight, or even more preferably about 0.001% to about 0.5% by weight of the composition.

[0152] The compositions according to the present invention may contain one or more bleaching agents. Preferred bleaches are selected from sodium perborate in anhydrous form or, for example, as monohydrate, tetrahydrate, or so-called dihydrate, sodium percarbonate in anhydrous form or, for example, as monohydrate, and sodium persulfate, where the term "persulfate" in any case includes salts of peracid H2SO5 and also peroxodisulfate.

[0153] In this regard, the alkali metal salt may also be an alkali metal bicarbonate, alkali metal hydrogen perborate, or alkali metal hydrogen persulfate. However, in all cases, a dialkali metal salt is preferred.

[0154] The formulation according to the present invention may contain one or more bleaching catalysts. The bleaching catalyst can be selected from oxaziridinium-based bleaching catalysts, bleaching-promoting transition metal salts or transition metal complexes, such as manganese-, iron-, cobalt-, ruthenium-, or molybdenum-salen complexes or carbonyl complexes. In addition to complexes of manganese, iron, cobalt, ruthenium, molybdenum, titanium, vanadium, and copper with nitrogen-containing tripod ligands, cobalt-, iron-, copper-, and ruthenium-amine complexes can also be used as bleaching catalysts.

[0155] The formulation according to the present invention may contain one or more bleaching agents, such as tetraacetylethylenediamine, tetraacetylmethylenediamine, tetraacetylglycoluryl, tetraacetylhexylenediamine, acylated phenol sulfonates such as n-nonanoyl- or isononanoyloxybenzene sulfonate, (S)NOBS, LOBS, DOBA, PAP, N-methylmorpholinium acetonitrile salt ("MMA salt"), trimethylammonium acetonitrile salt, N-acylimide such as N-nonanoylsuccinimide, 1,5-diacetyl-2,2-dioxohexahydro-1,3,5-triazine ("DADHT"), or nitrile quat (trimethylammonium acetonitrile salt).

[0156] As precursors to H2O2, peroxides, i.e., any compounds that can produce hydrogen peroxide in aqueous solution, such as organic and inorganic peroxides known in the literature and commercially available, which are conventionally used to bleach textile materials at washing temperatures of, for example, 10-95°C, will be considered.

[0157] However, inorganic peroxides, such as persulfates, perborates, percarbonates, and / or persilicates, are preferably used. They are typically used in amounts of 2 to 80% by weight, preferably 4 to 30% by weight, based on the weight of the composition.

[0158] Typically, equation (I) [ka] The compound is present in the composition in an amount of 0.05 to 15% by weight, preferably 0.1 to 10% by weight, based on the weight of the total composition, as will be described in more detail below.

[0159] Suitable examples of inorganic peroxides include sodium perborate tetrahydrate or sodium perborate monohydrate, sodium percarbonate, and inorganic peracid compounds, such as potassium persulfate (MPS). When organic or inorganic peracids are used as peracid compounds, their amount will usually be in the range of about 2 to 80% by weight, preferably 4 to 30% by weight, based on the weight of the composition.

[0160] Organic peroxides include, for example, mono- or poly-peroxides, urea peroxides, combinations of C1-C4 alkanol oxidases and C1-C4 alkanols (such as methanol oxidase and ethanol as described in International Publication No. 95 / 07972), and alkyl hydroxyperoxides such as cumene hydroperoxide and t-butyl hydroperoxide.

[0161] Peroxides can exist in various crystalline forms and have different water content, and they can also be used in combination with other inorganic or organic compounds to improve their storage stability.

[0162] As an oxidizing agent, peroxy acids can also be used. One example is formula (1)

Chemical formula

[0163] Preferred monoperoxy acids and their salts are of the formula

Chemical formula

[0164] In some cases, the use of additional bleaching agents may be advantageous.

[0165] The term "bleaching activator" is often used synonymously with "peracid bleach precursor." All of the peroxy compounds mentioned above can be used alone or in combination with peracid bleach precursors.

[0166] Such precursors are the corresponding carboxylic acid, or the corresponding carboxylic acid anhydride, or the corresponding carbonyl chloride, or amide, or ester, which can form peracids by hyperhydrolysis. Such reactions are generally known.

[0167] Peracid bleaching agent precursors are known and described in detail in documents such as British Patent Nos. 836988, 864,798, 907,356, 1,003,310 and 1,519,351; German Patent No. 3,337,921; European Patent Publication No. 0185522A, 0174132A and 0120591A; and U.S. Patent Nos. 1,246,339, 3,332,882, 4,128,494, 4,412,934 and 4,675,393.

[0168] Suitable bleaching agents include those having O- and / or N-acyl groups and / or unsubstituted or substituted benzoyl groups. These include polyacylated alkylenediamines, particularly tetraacetylethylenediamine (TAED), acylated glycoluryls, particularly tetraacetylglycolurea (TAGU), N,N-diacetyl-N,N-dimethylurea (DDU), sodium 4-benzoyloxybenzenesulfonate (SBOBS), sodium 1-methyl-2-benzoyloxybenzene-4-sulfonate, sodium 4-methyl-3-benzoloxybenzoate, trimethylammonium toluyloxybenzenesulfonate, acylated triazine derivatives, particularly 1,5-diacetyl-2,4-dioxohexahydro-1,3,5-triazine (DADHT), formula (10): [ka] (In the formula, R 22 R is a sulfonate group, a carboxylic acid group, or a carboxylate group. 21 is linear or branched (C7~C 15 (It is alkyl.) The compounds, particularly activators known as SNOBS, SLOBS, and DOBA, acylated polyhydric alcohols, particularly triacetin, ethylene glycol diacetate, and 2,5-diacetoxy-2,5-dihydrofuran, as well as acetylated sorbitol and mannitol, and acylated sugar derivatives, particularly pentaacetylglucose (PAG), sucrose polyacetate (SUPA), pentaacetylfructose, tetraacetylxylose, and octaacetyllactose, as well as acetylated and optionally N-alkylated glucamine and gluconolactone are preferred. It is also possible to use combinations of conventional bleaching activators known from German Patent Application No. 4443177A. Nitrile compounds that form perimic acid with peroxides are also under consideration as bleaching activators.

[0169] Other useful classes of peracid bleaching precursors are cationic, i.e., quaternary ammonium-substituted peracid precursors, as disclosed in U.S. Patent Nos. 4,751,015 and 4,397,757, and in European Patent Publication Nos. 0284292A and 331,229A. Examples of peracid bleaching precursors in this class include 2-(N,N,N-trimethylammonium)ethylsodium-4-sulfonphenyl carbonate chloride (SPCC), N-octyl-N,N-dimethyl-N10-carbophenoxydecylammonium chloride (ODC), 3-(N,N,N-trimethylammonium)propylsodium-4-sulfophenylcarboxylate, and N,N,N-trimethylammonium toluyloxybenzene sulfonate.

[0170] It is also possible to use additional bleaching catalysts, such as transition metal complexes, which are generally known and disclosed, for example, in European Patent No. 1194514, European Patent No. 1383857, or in International Publication No. 04 / 007657.

[0171] The formulation according to the present invention may contain one or more corrosion inhibitors. In this case, this is understood to include compounds that inhibit metal corrosion. Examples of suitable corrosion inhibitors include, for example, triazoles, particularly benzotriazoles, bisbenzotriazoles, aminotriazoles, alkylaminotriazoles, and phenol derivatives, such as hydroquinone, pyrocatechol, hydroxyhydroquinone, gallic acid, phloroglucinol, or pyrogallol.

[0172] In one embodiment of the present invention, the formulation according to the present invention contains a corrosion inhibitor in the range of 0.1 to 1.5% by weight.

[0173] The formulation according to the present invention may also include a cleaning polymer and / or a dirt-releasing polymer.

[0174] Examples of detergency polymers include, without limitation, "polyfunctional alkoxylated polyethyleneimines" (e.g., BASF's Sokalan® HP20), "polyfunctional alkoxylated diamines" (e.g., BASF's Sokalan® HP96), BASF's Sokalan® SR400 A, and Clariant's TexCare® products such as TexCare® SRN 170, TexCare® SRN 172, TexCare® SRN 260, TexCare® SRN 260 SG Terra, and TexCare® SRA 300, as well as all different combinations of the aforementioned polymers and terephthalic acid-based polyesters.

[0175] A suitable polyfunctional alkoxylated polyethyleneimine is typically an ethoxylated polyethyleneimine with a weight-average molecular weight Mw in the range of 3,000 to 250,000, preferably 5,000 to 200,000, more preferably 8,000 to 100,000, more preferably 8,000 to 50,000, more preferably 10,000 to 30,000, and most preferably 10,000 to 20,000 g / mol. A suitable polyfunctional alkoxylated polyethyleneimine has ethylene oxide side chains in the range of 80% to 99% by weight, preferably 85% to 99% by weight, more preferably 90% to 98% by weight, and most preferably 93% to 97% or 94% to 96% by weight, based on the total weight of the material. The ethoxylated polyethyleneimine is typically based on a polyethyleneimine core and a polyethylene oxide shell. A suitable polyethyleneimine core molecule is a polyethyleneimine with a weight-average molecular weight Mw in the range of 500 to 5000 g / mol. A molecular weight of 500 to 1000 g / mol is preferably used, and an Mw of 600 to 800 g / mol is more preferable. In this case, the ethoxylated polymer has an average of 5 to 50, preferably 10 to 35, and more preferably 20 to 35 ethylene oxide (EO) units per NH functional group.

[0176] Suitable polyfunctional alkoxylated diamines are typically ethoxylated C2-C12 alkylenediamines, preferably hexamethylenediamines, which are further quaternized and optionally sulfated. Typical polyfunctional alkoxylated diamines have a weight-average molecular weight Mw in the range of 2000-10000, more preferably 3000-8000, and most preferably 4000-6000 g / mol. In preferred embodiments of the present invention, further quaternized and sulfated ethoxylated hexamethylenediamines may be used, which contain an average of 10-50, preferably 15-40, and more preferably 20-30 ethylene oxide (EO) groups per NH group, and preferably have two cationic ammonium groups and two anionic sulfate groups.

[0177] In preferred embodiments of the present invention, the cleaning composition may contain at least one polyfunctional alkoxylated polyethyleneimine and / or at least one polyfunctional alkoxylated diamine to improve the cleaning performance of the laundry detergent, for example preferably to improve stain removal ability, and in particular to improve primary cleaning ability of particulate stains on polyester fabrics. The above-mentioned polyfunctional polyethyleneimine or polyfunctional diamine or mixture thereof may be added to the laundry detergent and cleaning composition in an amount as low as generally 0.05 to 15% by weight, preferably 0.1 to 10% by weight, more preferably 0.25 to 5% by weight, and even less than 2% by weight, based on a specific overall composition containing the other components and water and / or solvent.

[0178] In another preferred embodiment of the present invention, the cleaning composition may contain at least one terephthalic acid-based polyester used as a dirt-releasing polymer to improve the whiteness of the fabric after cleaning, particularly the whiteness of polyester fabrics.

[0179] Accordingly, one aspect of the present invention is a laundry detergent composition, a liquid laundry detergent, comprising at least one compound selected from polyfunctional alkoxylated polyethyleneimine, polyfunctional alkoxylated diamine, terephthalic acid-based polyester, and mixtures thereof.

[0180] The cleaning composition of the present invention may also contain at least one antimicrobial agent (often also referred to as a "preservative").

[0181] This composition may contain one or more antimicrobial agents and / or preservatives as listed on pages 35-39 of International Publication No. 2021 / 115912A1.

[0182] In particular, the following antimicrobial and / or preservatives are of interest: 4,4'-dichloro-2-hydroxydiphenyl ether (CAS No. 3380-30-1), also known as 5-chloro-2-(4-chlorophenoxy)phenol, Diclosan, DCPP, commercially available as a 30% by weight solution of 4,4'-dichloro-2-hydroxydiphenyl ether in 1,2-propylene glycol under the trade name Tinosan® HP 100 (BASF); 2-phenoxyethanol (CAS No. 122-99-6, also known as phenoxyethanol, methylphenyl glycol, phenoxetol, ethylene glycol phenyl ether, ethylene glycol monophenyl ether, Protectol® PE); 2-bromo-2-nitropropane-1,3-diol (CAS No. 52-51-7, also known as 2-bromo-2-nitro-1,3-propanediol, Bronopol®, Protectol® BN, Myacide Glutaraldehyde (CAS No. 111-30-8, also known as 1-5-pentanedial, pentane-1,5-dial, glutaraldehyde, Protectol® GA, Protectol® GA) 50, Myacide (registered trademark) GA), Glyoxal (CAS number 107-22-2, also known as ethanedial, oxylaldehyde, 1,2-ethanedial, Protectol (registered trademark) GL), 2-butyl-benzo[d]isothiazol-3-one (BBIT, CAS number 4299-07-4), 2-methyl-2H-isothiazol-3-one (MIT, CAS number 2682-20-4), 2-octyl-2H-isothiazol-3-one (OIT, CAS number 26530-20-1), 5-chloro-2-methyl-2H-isothiazol-3-one (CIT, CMIT, CAS number 26172-55-4), 5-chloro-2-methyl-2H-isothiazol-3-one (CMIT, EINECS) A mixture of 247-500-7) and 2-methyl-2H-isothiazole-3-one (MIT, EINECS 220-239-6) (CMIT / MIT mixture, CAS number 55965-84-9), 1,2-benzoisothiazole-3(2H)-one (BIT, CAS number 2634-33-5), hexa-2,4-Dienoic acid (sorbic acid, CAS number 110-44-1) and its salts, e.g., calcium sorbate, sodium sorbate, (E,E)-hexa-2,4-dienoic acid potassium (potassium sorbate, CAS number 24634-61-5), lactic acid and its salts, L-(+)-lactic acid (CAS number 79-33-4), benzoic acid and its sodium salts (CAS numbers 65-85-0, CAS numbers 532-32-1) and benzoic acid salts, e.g., ammonium benzoate, calcium benzoate, magnesium benzoate, MEA benzoate, potassium benzoate, salicylic acid and its salts, e.g., calcium salicylate, magnesium salicylate, MEA salicylate, sodium salicylate, potassium salicylate, salicylic acid TEA saccharate, chloride, bromide, and benzalkonium saccharate, such as benzalkonium chloride, benzalkonium bromide, benzalkonium saccharate (CAS numbers 8001-54-5, 63449-41-2, 91080-29-4, 68989-01-5, 68424-85-1, 68391-01-5, 61789-y71-7, 85409-22-9), didecyldimethylammonium chloride (DDAC, CAS numbers 68424-95-3 and 7173-51-5), N-(3-aminopropyl)-N-dodecylpropane-1,3-diamine (diamine, CAS number 2372-82-9), peracetic acid (CAS number 79-21-0), hydrogen peroxide (CAS number 7722-84-1).

[0183] The antibacterial agent is added to the composition at a concentration of 0.001 to 10% by weight relative to the total weight of the composition.

[0184] Preferably, the composition contains 2-phenoxyethanol at a concentration of 0.1 to 2% by weight, or 4,4'-dichloro-2-hydroxydiphenyl ether (DCPP) at a concentration of 0.005 to 0.6% by weight.

[0185] Accordingly, the present invention further encompasses a method for protecting an aqueous (liquid) composition according to the present invention from bacterial contamination or growth, the method comprising the addition of 2-phenoxyethanol. Accordingly, the present invention further encompasses a method for providing an antimicrobial effect to textile products after treatment or rinsing with solid laundry detergents (e.g., powders, granules, capsules, tablets, rods, etc.), liquid laundry detergents, or fabric softeners containing 4,4'-dichloro-2-hydroxydiphenyl ether (DCPP).

[0186] In further embodiments, the present invention also includes compositions further comprising an antimicrobial agent selected from the group preferably consisting of 2-phenoxyethanol, as disclosed below, more preferably containing the antimicrobial agent in an amount ranging from 2 ppm to 5% by weight of the composition, and even more preferably containing 0.1 to 2% by weight of phenoxyethanol.

[0187] As used herein, the term “dye fixative” refers to compounds that reduce or completely eliminate color bleeding of colored fabrics during the washing process. Examples of dye fixatives include, but are not limited to, cationic dye fixatives, crosslinking fixatives, and formaldehyde-based fixatives. Those skilled in the art are familiar with these compounds and can purchase them commercially from BASF SE, Huntsman, Archroma, Fineotex, Biotex Malaysia, or Dystar. Examples of, but not limited to, dye fixatives include Basilen Fixing Agent F-RP, Albafix ECO, Finofix NF, poly DADMAC, and Polyamine (DCDA-DETA, Epichloro-DMA, Epichloro-DETA, etc.). Formulations according to the present invention may also include water and / or additional organic solvents, such as ethanol or propylene glycol.

[0188] Further optional components may include, but are not limited to, viscosity modifiers, foaming promoters or defoaming inhibitors, fragrances, dyes, fluorescent whitening agents, and color transfer inhibitors.

[0189] Embodiment 12 Use of the liquid cleaning composition according to any one of Embodiments 1 to 11 for cleaning fabrics.

[0190] As used herein, the term “fabric” applies to any type of cloth or textile product, including but not limited to interior decorating materials and carpets, including natural and / or synthetic materials.

[0191] Embodiment 13 A cleaning method comprising bringing a liquid cleaning composition according to any one of Embodiments 1 to 11 into contact with a fabric.

[0192] As used herein, the term “washing” means performing or assisting any removal of dirt, bleaching, reduction of microbial populations, or a combination thereof. This includes rinsing fabrics with water or washing fabrics with the liquid washing composition of the present invention using a washing machine, automatic dishwasher, or manually. Washing is preferably carried out at a temperature of 60°C or less, more preferably 40°C or less, and most preferably 30°C or less. In other preferred embodiments, the washing method is carried out under water-saving conditions. This means that 60%, 70%, 80%, 90%, or 95% or less of the water generally recommended for a given washing procedure is used for the washing method of the present invention.

[0193] Embodiment 14 A method for producing a liquid cleaning composition, comprising contacting components (i) to (v) of Embodiment 1 and mixing them.

[0194] As used herein, the terms “to bring into contact” or “to bring into contact” refer to the act of bringing together two or more components, preferably all components (i) to (v), by dissolving, suspending, blending, slurring, or stirring. As used herein, the term “to mix” means blending, dispersing, or emulsifying components (i) to (v) of the liquid cleaning composition of the present invention to obtain a random or substantially equal distribution of all components (i) to (v). One or both of the above steps may be carried out in a solid state. Alternatively, two or more components, preferably all components (i) to (v), are “in contact” and “mixed” in a liquid, preferably in water.

[0195] General cleaning compositions and formulations The following compositions, including those listed in the table, disclose specific types of general cleaning compositions, which correspond to typical compositions that correlate with typical cleaning conditions commonly used in various parts and countries around the world.

[0196] If a composition shown does not contain at least one of components (i) to (v), particularly EDDS, then such a composition is a comparative composition. If it contains all of components (i) to (v) in the amounts described herein, then such a composition is considered to fall within the scope of the present invention.

[0197] It has a viscosity in the range of 20 to 10000 mPa*s and a pH value in the range of 4 to 14, and contains calcium (Ca) in the range of 0.000001% to 5% by weight of the composition. 2+ The liquid laundry detergent according to the present invention having an amount of, 0.0005-20% EDDS, 0.1-50% anionic surfactant, 0.1-40% of other builders, co-builders and / or chelating agents, 0.000001-5% protease or amylase or protease and amylase, 0.1-50% of other adjuvants, Water that makes up 100% in total It consists of.

[0198] It has a viscosity in the range of 30 to 3000 mPa*s and a pH value in the range of 5 to 12, and contains calcium (Ca) in the range of 0.0001% to 3% by weight of the composition. 2+ A preferred liquid laundry detergent according to the present invention having the following amount: 0.001-15% EDDS, An anionic surfactant selected from C10-C18 alkyl ether sulfates containing 2-40% C10-C15-LAS (alkylbenzenesulfonic acid) and / or 1-5 ethoxy units. A nonionic surfactant selected from C10-C18 alkyl ethoxylates containing 1.5-10% of 3-10 ethoxy units. 2-20% of soluble organic builders / cobuilders selected from C10-C18 fatty acids, di- and tricarboxylic acids, hydroxy-di- and hydroxytricarboxylic acids, and polycarboxylic acids. 0.0001-1% protease or amylase or protease and amylase, 0.5-20% mono- or diol selected from ethanol, isopropanol, ethylene glycol, or propylene glycol, 0.1-20% of other adjuvants, Water that makes up 100% in total It consists of.

[0199] In a preferred embodiment, the bacteria according to the present invention are used in a manual dishwashing detergent.

[0200] The liquid manual dishwashing detergent according to the present invention is 0.05-10% EDDS, 1-50% surfactant, 0.1-50% of other adjuvants, Water that makes up 100% in total It consists of.

[0201] A preferred liquid manual dishwashing detergent according to the present invention is: 0.2-5% EDDS, An anionic surfactant selected from C10-C18 alkyl ether sulfates and C10-C18 alkyl sulfates containing 5-40% C10-C15-LAS, 1-5 ethoxy units, 0-10% cocamidopropyl betaine, 0-10% lauramine oxide, 0-2% nonionic surfactant, preferably C10 gerbet alcohol alkoxylate, 0-5% enzyme, preferably amylase and preferably an enzyme stabilization system. 0.5-20% mono- or diol selected from ethanol, isopropanol, ethylene glycol, or propylene glycol, 0.1-20% of other adjuvants, Water that makes up 100% in total It consists of.

[0202] Both of the above liquid manual dishwashing detergents have a viscosity in the range of 30 to 3000 mPa*s and a pH value in the range of 5 to 12, and contain 0.0001% to 3% by weight of calcium (Ca) in the composition. 2+ ) has a quantity.

[0203] ADW gel formulation In further embodiments, the compositions according to the present invention are used in automatic dishwashing (ADW) gel formulations.

[0204] A preferred ADW gel formulation according to the present invention is 0.05-20% EDDS, 0.1-0.5% anionic surfactant, 1-20% nonionic surfactant, 0.1-50% builder, co-builder and / or chelating agent, 0.1-50% of other adjuvants, Water that makes up 100% in total It consists of.

[0205] A preferred ADW gel according to the present invention is 0.2-20% EDDS, 0.1-0.5% of an anionic surfactant selected from linear alkylbenzene sulfonates (LAS), alkyl sulfates (AS), alkyl alkoxy sulfates (AES), modified alkylbenzene sulfonates (MLAS), methyl ester sulfonates (MES), and alpha-olefin sulfonates (AOS), 1-5% nonionic surfactant selected from hydroxy mixed ethers, alcohol ethoxylates, and alcohol alkoxylates. 1-7% polymer (e.g., polyacrylate, polyacrylate having a sulfo group-containing monomer, biodegradable polymer (polyaspa, PESA, biograft polymer)), 2-20% citrate, methylglycine diacetic acid, chelating agents such as GLDA, An enzyme system, protease and amylase system, containing 0.05 to 5% of at least one enzyme suitable for detergent applications, and preferably an enzyme stabilization system. 0.1-50% of other auxiliary agents (parahumic acid, solvents, thickeners, preservatives, colorants, polyethyleneimine, amphoteric polymers, sodium formate, calcium chloride, sodium sulfate, sodium hydroxide, sodium carbonate, sodium silicate, sodium bicarbonate, sodium chloride, zinc salts, benzothiazoline), Water that makes up 100% in total It consists of.

[0206] Both of the above automatic dishwashing (ADW) gel formulations have a viscosity in the range of 30 to 3000 mPa*s and a pH value in the range of 5 to 12, and contain calcium (Ca) in the range of 0.0001% to 3% by weight of the composition. 2+ ) has a quantity.

[0207] The components (i) to (v) described in claim 1 and other components of the cleaning composition may be separated by compounding them in different compartments, for example, in different compartments of a multi-chamber pouch or bottle having different chambers, from which liquid is dispensed simultaneously in predetermined amounts to ensure that the appropriate amount of each component from each chamber is applied per individual point of use. Such multi-compartment pouches and bottles are also known to those skilled in the art.

[0208] The table below shows common cleaning compositions of specific types, corresponding to typical compositions that correlate with typical cleaning conditions commonly used in various regions and countries around the world.

[0209] [Table 1]

[0210] [Table 2]

[0211] [Table 3]

[0212] [Table 4]

[0213] [Table 5]

[0214] The following embodiments further illustrate the present invention without limiting its scope.

[0215] The specific embodiments described throughout this disclosure are incorporated into the Invention as part of the Invention, and the various further options disclosed herein as “optional,” “preferred,” “more preferred,” “even more preferred,” or “most preferred” (or “preferred,” etc.) options of a particular embodiment may be selected individually and independently (unless such independent selection is impossible due to the nature of its features or unless such independent selection is expressly excluded), and then combined within any of the other embodiments (unless such independent selection is impossible due to the nature of its features or unless such independent selection is expressly excluded, and unless other such options and priorities may also be selected individually and independently), and each and every such possible combination is included as an individual embodiment as part of the Invention. [Examples]

[0216] I) Storage experiments using amylase Storage stability amylase was measured by an enzyme activity assay in liquid detergent after storage at 38°C for up to 28 days.

[0217] To test the storage stability of amylase, liquid laundry test formulation F15 was prepared using 1 or 2.2% EDDS, 2.2% GLDA, 2.2% citrate, 2.2% DTPA, and a mixture of 1.5% citrate and 0.7% GLDA. Table 3 shows the liquid laundry detergents used to conduct application tests to measure the effect of builders on enzyme stability by testing amylase activity. All formulations were stored at 38°C for 1, 2, 7, 14, or 28 days.

[0218] [Table 6]

[0219] [Table 7]

[0220] The liquid detergent formulation was stored at a temperature of 38°C for up to 4 weeks. 4 weeks of storage is said to be equivalent to approximately 9 months at room temperature or more than 15 months at 8°C.

[0221] The amylase activity after storage was quantitatively measured by the release of the chromophore para-nitrophenol (pNP) from the substrate ethylidene-blocked-pNPG7 (Roche Applied Science, material no. 10880078103). Alpha-amylase breaks down the substrate into smaller molecules and is added in excess compared to α-amylase. α-glucosidase (Roche Applied Science, material no. 11626329103) processes these smaller products until pNP is released, which is measured by an increase in absorption at 405 nm. The release of pNP is directly proportional to the α-amylase activity of the sample. Amylase standard: Termamyl 120 L (Sigma 3403). Starch degradation activity was measured before and after storage.

[0222] The residual enzyme activity corresponds to the remaining enzyme activity when compared to the initial enzyme activity available before storage at time 0.

[0223] [Table 8]

[0224] The standard error for each of the above values ​​is 2.5% or less. Therefore, the compositions of the present invention, including EDDS, show a significant advantage in terms of enzyme stability.

[0225] II) Storage application experiments using amylase and protease The storage stability of proteases and amylases was measured by their residual cleaning performance in liquid detergents after storage at 37°C for up to 28 days.

[0226] To test the storage stability of protease and amylase, liquid laundry test formulation F16 was prepared using no builder, 1 or 2% EDDS, 1 or 2% GLDA, 0.5 or 1% HEDP and 0.5 or 1% DTPMP. Table 4 shows the liquid laundry detergents used to conduct application tests to measure the effect of builders on enzyme stability by testing primary wash performance. All formulations were stored at 37 °C for 7, 14 or 28 days. After storage, the formulations were washed using two different methods.

[0227]

Table 9

[0228] A) Application test in HTS (High Throughput System), small scale The wash performance for the formulations was measured as follows.

[0229] The L*, a*b* values of a single stain are measured with MACH 5 from CFT / Colour consult before washing. Then the fabric is washed in the detergent formulation at 30 °C. After washing, the fabric is rinsed and dried.

[0230] The wash performance for a single stain is measured by measuring the L*, a*b* values with MACH 5 from CFT / Colour consult after drying. The dE value is calculated from the single values before and after washing. The value is the average of 3 replicates. The higher this value, the better the performance.

[0231]

Table 10

[0232]

Table 11

[0233]

Table 12

[0234]

Table 13

[0235] The measurement error is ±0.5 delta E units. Thus, any value above 0.5 (delta delta E) means that the EDDS (in relation to the test composition) shows a directional visible contribution to the overall stability of each detergent formulation.

[0236] B) Application test with Launder-O-meter, large scale The washing performance for the formulations was measured as follows.

[0237] The L*, a*b* values of a single stain on a multi-stain monitor (8 different protease relative stains) are measured with MACH 5 from CFT / Colour consult before washing. The fabric is then washed in a detergent formulation at 30 °C together with cotton ballast fabric and 20 steel balls. After washing, the fabric is rinsed, centrifuged and dried in air.

[0238] The washing performance for a single stain is measured by measuring the L*, a*b* values with MACH 5 from CFT / Colour consult after drying. The dE value is calculated from the single values before and after washing. The total of all 8 stains from the monitor is summed. The higher this value, the better the performance.

[0239]

Table 14

[0240]

Table 15

[0241] The measurement error is ±2 Delta E units. Therefore, any value greater than 2 (total Delta E) means that EDDS (in relation to the test composition) shows a directional, visible contribution to the overall stability of each detergent formulation. Any value greater than 4 (total Delta E) means that EDDS (in relation to the test composition) even shows a significant contribution to the overall stability of the enzyme used.

Claims

1. A liquid cleaning composition, (i) an amount of ethylenediamine-N,N'-disuccinic acid (EDDS) in the range of 0.0005% to 20% by weight of the composition, (ii) At least one enzyme in an amount ranging from 0.000001% to 5% by weight of the composition, selected from the group consisting of amylase and protease, (iii) At least one anionic surfactant in an amount ranging from 0.1% to 50% by weight of the composition, (iv) Calcium (Ca) in an amount ranging from 0.000001% to 5% by weight of the composition ２＋ )and, (v) water and A liquid cleaning composition comprising, having a viscosity in the range of 20 to 10,000 mPa*s and a pH value in the range of 4 to 14, as measured by the relevant method according to this specification.

2. The liquid cleaning composition according to claim 1, wherein ethylenediamine-N,N'-disuccinic acid (EDDS) is present in an amount ranging from 0.001% to 15% by weight, preferably 0.01% to 10% by weight, and most preferably 0.1% to 5% by weight of the composition.

3. The liquid cleaning composition according to claim 1 or 2, wherein the at least enzyme is present in an amount of 0.00001% to 2% by weight, preferably 0.0001% to 1% by weight, and most preferably 0.001% to 0.5% by weight of the composition.

4. (a) The amylase is alpha-amylase and / or (b) The liquid cleaning composition according to any one of claims 1 to 3, wherein the protease is a subtilisin protease.

5. The liquid cleaning composition according to claim 4(b), further comprising a protease stabilization system containing peptaldehyde.

6. The aforementioned at least one anionic surfactant is (a) present in an amount ranging from 2% to 40% by weight, preferably 3% to 30% by weight, most preferably 4% to 25% by weight of the composition, and / or (b) A liquid cleaning composition according to any one of claims 1 to 5, selected from the group consisting of linear alkylbenzene sulfonate (LAS), alkyl sulfate (AS), alkyl alkoxy sulfate (AES), alkyl alkoxycarboxylate, modified alkylbenzene sulfonate (MLAS), methyl ester sulfonate (MES), alkyl sulfosuccinate and alpha-olefin sulfonate (AOS).

7. Calcium (Ca ２＋ The liquid cleaning composition according to any one of claims 1 to 6, wherein the above is present in an amount of 0.0001% to 3% by weight, preferably 0.001% to 1% by weight of the composition.

8. The liquid cleaning composition according to any one of claims 1 to 7, wherein the viscosity is in the range of 30 to 3000 mPa*s, preferably 40 to 2500 mPa*s, and most preferably 50 to 2000 mPa*s.

9. The liquid cleaning composition according to any one of claims 1 to 8, wherein the pH value is in the range of 5 to 12, preferably 6 to 10, and most preferably 7 to 9.

10. A liquid cleaning composition according to any one of claims 1 to 9, which is a detergent composition.

11. A liquid cleaning composition according to any one of claims 1 to 10, further comprising at least one element from the group consisting of non-anionic surfactants, amphoteric surfactants, cobuilders, alcohols, biocides, thickeners, water-soluble polymers, mud stain removers / anti-re-adhesion agents, polymer stain release agents, bleaches, bleach activators, gloss agents, odor suppressants, pigments, dyes, opacifiers, colorants, color transfer inhibitors, anti-foaming agents, corrosion inhibitors, softeners, and fragrances.

12. Use of the liquid cleaning composition according to any one of claims 1 to 11 for cleaning fabrics.

13. A cleaning method comprising bringing a liquid cleaning composition according to any one of claims 1 to 11 into contact with a fabric.

14. A method for producing a liquid cleaning composition, comprising contacting components (i) to (v) described in claim 1 and mixing them.

Images