Stable cleaning composition comprising EDDS and enzyme and use thereof

Abstract

The present invention relates to a liquid cleaning composition comprising (i) ethylenediamine-N, N '-disuccinic acid (EDDS), (ii) at least one enzyme selected from the group consisting of amylases and proteases, (iii) at least one anionic surfactant, (iv) calcium (Ca2 +) and (v) water for enhancing the long-term stability of enzymes, their manufacture and use, for example in laundry or dishwashing.

Description

[0001] This invention relates to specific cleaning compositions comprising ethylenediamine-N,N'-disuccinic acid (EDDS) (abbreviated as "component I of the invention") and protease and / or amylase (abbreviated as "component II of the invention"), their manufacture, and their use, particularly as a laundry detergent composition.

[0002] Detergent and household care product formulators are constantly faced with the task of developing improved products to remove a broad spectrum of dirt and stains from fabrics and hard surfaces. Chemically and physicochemically, the spectrum of dirt and stains ranges from polar dirt such as proteins, clays, and inorganic dirt to non-polar dirt such as cooking fumes, carbon black, and byproducts of incomplete combustion of hydrocarbons, as well as organic dirt like sebum and starch-based stains. Given the emerging trend of improving the “footprint” of any cleaning product, these challenging needs become even more demanding, whether in terms of its source (e.g., from natural or renewable resources), production efficiency compared to previous products (and thus reduced energy consumption), usage efficiency (e.g., reduced amount of performance at the same level or improved performance at the same dosage), persistence in the natural environment after use, and especially biodegradability, as recycling is technically very challenging and therefore not economically attractive.

[0003] Due to these trends, there is a strong need for new biodegradable cleaning compositions that offer excellent primary (i.e., dirt removal) and secondary (i.e., whiteness maintenance) cleaning benefits for both hydrophobic and hydrophilic stains, along with improved biodegradability. A step towards 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 enzyme integrity. This also applies to polymeric cleaning components. Furthermore, 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. Therefore, many standard cleaning components pose a threat to enzymes and their long-term stability when applied at their active concentrations. To overcome this problem, cleaning compositions can contain enzyme-stabilizing components such as boric acid, boric acid, and their derivatives. However, boric acid is registered under REACH regulations and is suspected of impairing fertility and harming unborn children, reducing the acceptance of boron-containing enzyme-stabilizing components by authorities and customers. Therefore, there is a need to find improved enzyme-containing cleaning compositions with high performance characteristics, enhanced consumer safety, and improved biodegradability.

[0004] The following provides an overview of the current knowledge in the field of the invention and the most relevant disclosures, as well as identified uses of detergents or EDDS in combination with enzymes.

[0005] Polyphosphonates are a class of building blocks frequently used in cleaning compositions. These synthetic compounds differ from natural phosphonates such as 2-aminoethylphosphonic acid because they are larger and anionic, and often exist as metal complexes. Biodegradation tests for 1-hydroxyethylidene-1,1-diphosphonic acid (HEDP) and nitroxytrimethylmethylenephosphonic acid (NTMP) showed no signs of degradation. Furthermore, studies on 1-hydroxyethylidene-1,1-diphosphonic acid (HEDP), nitroxytrimethylmethylenephosphonic acid (NTMP), ethylenediaminetetra(methylenephosphonic acid) (EDTMP), and diethylenetriaminepenta(methylenephosphonic acid) (DTPMP) in standard biodegradation tests also failed to confirm any biodegradation. Therefore, the use of polyphosphonates in cleaning compositions is undesirable regarding biodegradability.

[0006] Another class of confirmed building block compounds used in home care products are aminopolycarboxylic acid chelating agents. Like polyphosphonates, this class includes a wide variety of compounds such as ethylenediaminetetraacetic acid (EDTA), nitrotriacetic acid (NTA), diethylenetriaminepentaacetic acid (DTPA), and tetrasodium N,N-bis(carboxymethyl)-L-glutamate (TETRANATRIUM-N,N-BIS(CARBOXYLATOMETHYL)-L-GLUTAMAT) (GLDA). EDTA is the most widely used chelating agent in the world. Its widespread use and slow removal under many environmental conditions have resulted in it being one of the most concentrated anthropogenic compounds in surface waters in many European countries. For this reason, manufacturers are seeking alternative chelating agents with higher biodegradability. NTA, on the other hand, has better biodegradability than EDTA but can cause eye, skin, and respiratory irritation, as well as kidney and bladder damage. Additionally, NTA is considered a potential carcinogen 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 detergent builder has been known since the early 1970s, as described, for example, in US4028262 A. However, this compound also negatively impairs the long-term stability of amylase, as demonstrated experimentally by the inventors of this invention, and therefore does not represent an ideal solution for future cleaning formulations containing increased amounts of the enzyme.

[0008] WO 9606908 A discloses the use of EDDS in detergents with enzymes such as proteases and amylases. However, there is no specific preparation of detergent formulations containing EDDS and enzymes to establish long-term enzyme stability. To achieve this long-term stability, WO 9606908 A describes enzyme stabilizers, preferably compounds based on boric acid and boronicacid, which have the aforementioned negative effects registered under REACH regulations and suspected of impairing fertility and unborn children.

[0009] Therefore, there is a need in the art to find cleaning compositions comprising a combination of surfactants, builders, and enzymes, wherein the cleaning composition is free of boric acid or boronic acid, has high biodegradability, and provides long-term enzyme stability and customer safety.

[0010] The inventors of this invention have unexpectedly discovered that the combination of ethylenediamine-N,N'-disuccinic acid (EDDS) with proteases or amylases in specific cleaning composition formulations (e.g., specific anionic surfactants and calcium concentrations, pH values, and viscosities) produces cleaning compositions exhibiting improved consumer safety, high biodegradability, and providing long-term enzyme stability. Experimental comparisons with other chelating agents such as diethylenetriaminepenta(methylenephosphonic acid) (DTPMP), 1-hydroxyethylene-1,1-diphosphonic acid (HEDP), citrate, diethylenetriaminepentaacetic acid (DTPA), and tetrasodium N,N-bis(carboxymethyl)-L-glutamate (GLDA) show that EDDS is the only detergent builder that provides both 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 to provide a novel liquid cleaning composition comprising (i) an amount ranging from 0.0005% to 20% by weight of the composition of ethylenediamine-N,N'-disuccinic acid (EDDS); (ii) an amount ranging from 0.000001% to 5% by weight of the composition of at least one enzyme, wherein the at least one enzyme is selected from the group consisting of amylase and protease; (iii) an amount ranging from 0.1% to 50% by weight of the composition of at least one anionic surfactant; and (iv) an amount ranging from 0.000001% to 5% by weight of the composition of calcium (Ca). 2+ (v) and (v) water, wherein the cleaning composition has a viscosity ranging from 20 to 10000 mPa*s and a pH value ranging from 4 to 14, as measured by relevant methods according to the instructions.

[0012] The liquid cleaning composition of the present invention may further comprise at least one element from the group consisting of: nonionic surfactants, amphoteric surfactants, co-cleaning agents, alcohols, biocides, thickeners, water-soluble polymers, clay stain removers / anti-redeposition agents, polymer detergents, bleaching agents, bleach activators, brighteners, odor control agents, pigments, dyes, opacifiers, toning agents, dye transfer inhibitors, defoamers, corrosion inhibitors, softeners, and fragrances.

[0013] In another aspect, the liquid cleaning composition of the present invention is used for cleaning fabrics.

[0014] Furthermore, cleaning methods that bring the liquid cleaning composition of the present invention into contact with fabrics are also part of the present invention.

[0015] Furthermore, the present invention relates to a method for manufacturing the liquid cleaning composition of the present invention, the method comprising contacting and mixing the components (i) to (v) of the liquid cleaning composition as described above.

[0016] Therefore, the subject matter of the present invention is the following embodiments 1 to 15, as defined below and further explained by other examples and illustrated further in the experimental section:

[0017] Example 1

[0018] 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 in an amount ranging from 0.000001% to 5% by weight of the composition, wherein the at least one enzyme is 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; and (iv) calcium (Ca) in an amount ranging from 0.000001% to 5% by weight of the composition. 2+ (v) and (v) water, wherein the cleaning composition has a viscosity ranging from 20 to 10000 mPa*s and a pH value ranging from 4 to 14, as measured by relevant methods according to the instructions.

[0019] As used herein, “liquid” means that the continuous phase or main component of a composition is liquid, and that the composition is flowable at 20°C (i.e., may include suspended solids). The term “liquid” also includes gels. As used herein, “gel” means a shear-thinned lamellar gel having a pour 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. Gels can be viscous liquids. However, viscous liquids can be Newtonian fluids whose viscosity does not change with flow conditions, such as honey or syrup. Dispensing this type of viscous liquid is very difficult and messy. Different types of liquid gels are shear-thinned, i.e., viscous under low shear conditions (e.g., at rest) and thin under high flow conditions. Thus, cleaning compositions include detergents or automatic dishwashing (ADW) gels.

[0020] As may be used interchangeably herein, the terms “cleaning composition” or “cleaning agent” refer to all compositions intended for use in conjunction with cleaning activities and to enhance the effectiveness of cleaning activities. The term “cleaning agent” 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, cloth and fiber cleaning compositions, disinfectants, etc. As used herein, the term “cleaning” refers to those activities involving the removal of unwanted residues from surfaces, and particularly includes activities such as chemical, mechanical, and thermal cleaning activities and combinations thereof. Chemical cleaning activities include, for example, the use of solvents to remove residues from surfaces, potentially further involving the use of surfactants to improve the compatibility between residues and solvents. Chemical cleaning activities further include chemical alterations to residues to improve ease of removal. The cleaning compositions of the present invention comprise at least five components, namely (i) EDDS, (ii) proteases and / or amylases, (iii) at least one anionic surfactant, and (iv) calcium cations (Ca). 2+ ) and (v) water.

[0021] As used herein, “enzyme” refers to any of a number of naturally occurring proteins produced in living cells that accelerate or catalyze metabolic processes in organisms. Enzymes act on substrates. Before an enzyme-catalyzed reaction occurs, the substrate binds to the enzyme at a site known as the active site. Enzymes according to this application include, but are not limited to, amylases or proteases, also referred to as Compound II of the present invention. However, the cleaning compositions of the present invention may also contain other enzymes besides amylases or proteases, which may be selected from the group consisting of: lipases, cellulases, mannanases, hemicellulases, phospholipases, esterases, pectinases, lactases, peroxidases, xylanases, keratinases, pectic acid lyases, keratinases, reductases, oxidases, phenol oxidases, lipoxygenases, ligninases, amylopectinases, tanninases, pentosanases, melanases, β-glucanases, arabinosidases, hyaluronidases, Chondroitinase, laccase, nuclease, deoxyribonuclease, phosphodiesterase, phytase, carbohydrate enzyme, galactanase, xanthan gumase, xyloglucanase, oxidoreductase, hydrolase, aminopeptidase, asparaginase, carbohydrate enzyme, carboxypeptidase, catalase, chitinase, cyclodextrin glycosyltransferase, α-galactosidase, β-galactosidase, glucosylamylase, α-glucosidase, β-glucosidase, invertase, ribonuclease, transglutaminase, and dispersin, or combinations thereof.

[0022] As used herein, the term "at least one" includes, but is not limited to, 1, 2, 3, 4, 5, 6, 7, 8, 9 or more.

[0023] Example 2

[0024] According to the liquid cleaning composition of Example 1, ethylenediamine-N,N'-disuccinic acid (EDDS) is present in an amount ranging from 0.001% to 15%, preferably from 0.01% to 10%, and most preferably from 0.1% to 5% by weight of the composition.

[0025] EDDS has the structure of formula (I):

[0026] (I)

[0027] EDDS have two chiral centers. Therefore, EDDS can occur in three different stereoisomers: [R,R], [R,S] / [S,R], and [S,S]. [S,S] EDDS are completely biodegradable, while meso-EDDS are at least partially biodegradable. The [S,S] stereoisomer is a derivative of the natural amino acid L-aspartic acid, and this source is likely the reason for its good biodegradability. The [R,R] stereoisomer persists in the environment. Therefore, in a preferred embodiment of the invention, the EDDS is [S,S] EDDS or meso-EDDS, more preferably [S,S] EDDS.

[0028] 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 can be in its 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, triethanolamine, etc.).

[0029] In a preferred embodiment, the lower limit of the EDDS concentration is 0.0005%, 0.005%, 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%, 7%, or 6% by weight of the composition of the present invention.

[0030] Example 3

[0031] According to the liquid cleaning composition of Example 1 or 2, the at least one enzyme is present in an amount ranging from 0.00001% to 2%, preferably from 0.0001% to 1%, and most preferably from 0.001% to 0.5% by weight of the composition.

[0032] In a preferred embodiment, the lower limit of the enzyme concentration is 0.00005% or 0.0005% by weight of the composition of the present invention. In other preferred embodiments, the upper limit of the enzyme concentration is 1.7%, 1.3%, or 0.8% by weight of the composition of the present invention.

[0033] Example 4

[0034] The liquid cleaning composition according to any one of Examples 1 to 3, wherein (a) the amylase is α-amylase; and / or (b) the protease is subtilisin protease.

[0035] The term "amylase" (α and / or β) according to the present invention includes amylases of bacterial or fungal origin (EC 3.2.1.1 and 3.2.1.2, respectively). The term also includes variants and mutants of naturally occurring amylases, so-called wild-type proteins. Preferably, the amylase is selected from the α-amylase group (EC 3.2.1.1). This includes chemically modified or protein-engineered mutants. The amylase according to the present invention has "starch-degrading activity" or "amylase activity," involving the (endo-hydrolysis) of glycosidic bonds in polysaccharides. α-amylase activity can be determined by assays known to those skilled in the art to measure α-amylase activity. Examples of assays for measuring α-amylase activity are:

[0036] α-Amylase activity can be determined using Phadebas tablets as a substrate (Phadebas amylase assay, Magle Life Science). Starch is hydrolyzed by α-amylase, producing a soluble blue fragment. The absorbance of the resulting blue solution (measured spectrophotometrically at 620 nm) is a function of α-amylase activity. The measured absorbance is directly proportional to the specific activity of the α-amylase under given conditions (activity / mg pure α-amylase protein).

[0037] α-Amylase activity can also be determined using ethylidene-4-nitrophenyl-α-D-maltoheptaglycoside (EPS). D-maltoheptaglycoside is a blocked oligosaccharide that can be cleaved by endoamylase. After cleavage, the α-glucosidase contained in the kit digests the substrate, releasing yellow free PNP molecules, which can therefore be measured at 405 nm by visible spectrophotometry. The kit containing EPS substrate and α-glucosidase is manufactured by Roche Costum Biotech (catalog number 10880078103). The slope of the time-dependent absorption curve is directly proportional to the specific activity (activity / mg enzyme) of the α-amylase under given conditions.

[0038] Starch-degrading activity can be provided in units per gram of enzyme. For example, 1 unit of α-amylase can release 1.0 mg of maltose from starch in 3 min at 20°C and pH 6.9.

[0039] Regardless of the nature of the assay, the amylase variant 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 against the corresponding wild-type amylase.

[0040] Amylases can be derived from Bacillus licheniformis having SEQ ID NO:2 as described in WO 95 / 10603 and variants that are at least 95% identical thereto. Suitable variants described in WO 95 / 10603 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, which have starch-degrading activity. Variants are described in SEQ ID NO:4 of WO 94 / 02597, WO 94 / 018314, WO 97 / 043424 and WO 99 / 019467.

[0041] The amylase may further be derived from *Bacillus stearothermophilus* having SEQ ID NO:6 as disclosed in WO 02 / 10355, or optionally from an amylase having a C-terminal truncated compared to the wild-type sequence. Suitable variants of SEQ ID NO:6 include variants containing deletions at positions 179 and / or 181 and / or 182 and / or substitutions at position 193.

[0042] The amylase may further be derived from Bacillus species 707 having SEQ ID NO:6 disclosed in WO 99 / 19467 and variants that are at least 95% identical thereto. Preferred variants of SEQ NO:6 are those having substitutions, deletions, or insertions at one or more of the following locations: R181, G182, H183, G184, N195, I206, E212, E216, and K269.

[0043] The amylase may further be derived from Bacillus halmapalus having SEQ ID NO:2 or SEQ ID NO:7 as described in WO 96 / 23872, also described herein as SP-722. Preferred variants are described in WO97 / 3296, WO 99 / 194671 and WO 2013 / 001078.

[0044] The amylase may further be derived from Bacillus species DSM 12649 having SEQ ID NO:4 disclosed in WO 00 / 22103 and at least 95% identical variants thereof.

[0045] The amylase may further be derived from Bacillus species A7-7 (DSM 12368) that has an amino acid sequence that is at least 95% identical to SEQ ID NO:2, particularly to the region of amino acids 32 to 516 according to SEQ ID NO:2, as disclosed in WO 02 / 10356.

[0046] The amylase may further be derived from Bacillus strain TS-23 having SEQ ID NO:2 and its variants as disclosed in WO 2009 / 061380.

[0047] Amylase can further be derived from Cytophaga species having SEQ ID NO:1 disclosed in WO 2013 / 184577 and variants that are at least 95% identical to it.

[0048] The amylase may further be derived from Bacillus megaterium DSM 90, which has SEQ ID NO:1 disclosed in WO 2010 / 104675 and is at least 95% identical to the variant thereon.

[0049] The amylase may further be derived from a Bacillus species containing amino acids 1 to 485 of SEQ ID NO:2 as described in WO 00 / 60060 and variants thereof that are at least 95% identical to those of the Bacillus species.

[0050] The amylase may further be derived from Bacillus amyloliquefaciens or a variant thereof, preferably selected from the amylase according to SEQ ID NO: 3 as described in WO 2016 / 092009.

[0051] Amylases may have SEQ ID NO:12 as described in WO 2006 / 002643, or amylase variants thereof, which contain the substituted Y295F and M202LITV within SEQ ID NO:12.

[0052] Amylases may have SEQ ID NO:6 as described in WO 2011 / 098531, or amylase variants that contain substitutions at one or more positions selected from the group consisting of: 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].

[0053] Amylases may have SEQ ID NO:1 as described in WO 2013 / 001078, or amylase variants that include changes at two or more positions (several) corresponding to positions G304, W140, W189, D134, E260, F262, W284, W347, W439, W469, G476, and G477 within SEQ ID NO:1.

[0054] The amylase may have SEQ ID NO:2 as described in WO 2013 / 001087, or amylase variants that contain the deletion of positions 181+182, 182+183, or 183+184 within SEQ ID NO:2, and optionally include one or two or more modifications at any position corresponding to W140, W159, W167, Q169, W189, E194, N260, F262, W284, F289, G304, G305, R320, W347, W439, W469, G476, and G477 within SEQ ID NO:2.

[0055] The amylase may be a hybrid α-amylase derived from the above-mentioned amylases, for example, as described in WO 2006 / 066594.

[0056] According to WO 2014 / 183920, a heterozygous amylase may have A and B domains and a C domain, wherein the A and B domains have at least 90% identity with SEQ ID NO:2 of WO 2014 / 183920, and the C domain has at least 90% identity with SEQ ID NO:6 of WO 2014 / 183920, wherein the heterozygous amylase has starch-degrading activity; preferably, the heterozygous α-amylase has at least 95% identity with SEQ ID NO:23 of WO 2014 / 183920 and has starch-degrading activity.

[0057] According to WO 2014 / 183921, a heterozygous amylase may have A and B domains and a C domain, wherein the A and B domains have at least 75% identity with 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 disclosed in WO 2014 / 183921, and the C domain has at least 90% identity with SEQ ID NO: 6 of WO 2014 / 183921, wherein the heterozygous amylase has starch-degrading activity; preferably, the heterozygous α-amylase has at least 95% identity with SEQ ID NO: 30 disclosed in WO 2014 / 183921 and has starch-degrading activity;

[0058] According to WO 2021 / 032881, a heterozygous amylase may comprise A and B domains derived from α-amylase (derived from Bacillus species A7-7 (DSM 12368)) and a C domain derived from α-amylase (from Bacillus cereus); preferably, the A and B domains have at least 75% identity with the amino acid sequence of SEQ ID NO: 42, and the C domain has at least 75% identity with the amino acid sequence of SEQ ID NO: 44—both sequences are as disclosed in WO 2021 / 032881; more preferably, the heterozygous amylase has at least 80% identity with SEQ ID NO: 54 as disclosed in WO 2021 / 032881.

[0059] Suitable amylases also include those variants of the aforementioned amylases having starch-degrading activity. In one embodiment, the amylase variant includes a variant having at least 40% to 100% identity with the full-length polypeptide sequence of the parental enzyme as disclosed above. In one embodiment, the amylase variant 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 parental (wild-type) enzyme as disclosed above.

[0060] In another embodiment, the present invention relates to amylase variants comprising conserved mutations that do not involve the functional domains of the corresponding amylase. The amylase variants of this embodiment having starch-degrading activity may be at least 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% similar to the full-length polypeptide sequence of the parental (wild-type) enzyme.

[0061] In one embodiment, the amylase variant exhibits enhanced starch-degrading activity when compared to the parental (wild-type) amylase, wherein the amylase variant has starch-degrading activity according to the invention.

[0062] In one embodiment, the amylase variant has starch-degrading activity according to the invention when it 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 corresponding parent (wild-type) amylase.

[0063] In one embodiment, at least one amylase is selected from commercially available amylases, including but not limited to products marketed under trade names such as Duramyl™, Termamyl™, Fungamyl™, Stainzyme™, Stainzyme Plus™, Natalase™, Liquozyme X and BAN™, Amplify™, Amplify Prime™ (from Novozymes A / S), and Rapidase™, Purastar™, Powerase™, Effectenz™ (from DuPont M100), Preferenz™ (S1000, S110 and F1000; from DuPont), PrimaGreen™ (ALL; DuPont), and Optisize™ (DuPont).

[0064] Enzymes exhibiting proteolytic activity are called "proteases" or "peptidases." The term also includes variants and mutants of naturally occurring proteases, so-called wild-type proteins. A protease is an active protein that exhibits "proteolytic activity" or "proteinolytic activity." Proteolytic activity is related to the rate at which a protein is degraded by a protease or proteolytic enzyme over a defined time period.

[0065] The methods used to analyze proteolytic activity are well-known in the literature (see, for example, Gupta et al. (2002), Appl. Microbiol. Biotechnol. 60: 381-395). Proteolytic activity can be determined by using succinyl-Ala-Ala-Pro-Phe-p-nitroaniline (Suc-AAPF-pNA, abbreviated as AAPF; see, for example, DelMar et al. (1979), Analytical Biochem 99, 316-320) as a substrate. Cleavage of pNA from the substrate molecule via proteolytic hydrolysis results in the release of free, yellow pNA, which can be quantified by measuring OD405.

[0066] Proteolytic activity can be provided in units per gram of enzyme. For example, 1 U of protease can correspond to the amount of protease that releases 1 µmol of Folin-positive amino acids and peptides (as tyrosine) per minute at pH 8.0 and 37°C (with casein as substrate).

[0067] Regardless of the nature of the assay, the protease variant 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 against the corresponding wild-type protease.

[0068] Proteases are members of class EC 3.4. Proteases include aminopeptidases (EC 3.4.11), dipeptidases (EC 3.4.13), dipeptidyl peptidases and tripeptidyl peptidases (EC 3.4.14), peptidyl dipeptidases (EC 3.4.15), serine carboxypeptidases (EC 3.4.16), metallocarboxypeptidases (EC 3.4.17), cysteine ​​carboxypeptidases (EC 3.4.18), ω-peptidases (EC 3.4.19), serine endopeptidases (EC 3.4.21), cysteine ​​endopeptidases (EC 3.4.22), aspartate endopeptidases (EC 3.4.23), metalloendopeptidases (EC 3.4.24), threonine endopeptidases (EC 3.4.25), or endopeptidases with unknown catalytic mechanisms (EC 3.4.99).

[0069] At least one protease may be selected from metalloendopeptidases (EC 3.4.24). The metalloproteinase may be, for example, a thermophilic bacterial protease from family M4 or another metalloproteinase, such as those from families M5, M7 or M8. Metalloproteinases can be derived in particular from Bacillus amyloliquefaciens as described in WO 07 / 044993 A2, from the genera Bacillus, Brevibacillus, Thermoactinomyces, Geobacillus, Paenibacillus, Lysinibacillus, or Streptomyces spp. as described in WO 2014194032, WO 2014194054 and WO 2014194117, from Kribella alluminosa as described in WO2015193488, and from the genera Streptomyces and Lysobacter as described in WO 2016075078.

[0070] More preferably, at least one protease may be selected from serine proteases (EC 3.4.21). A serine protease or serine peptidase is characterized by having a serine residue at its catalytically active site, which forms a covalent adduct with the substrate during the catalytic reaction. The serine proteases may 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 subtilisinase, for example, EC 3.4.21.62, which is also referred to as "subtilisin" below.

[0071] Substantialmin-related serine proteases share a common amino acid sequence defining their catalytic triad, which distinguishes them from chymotrypsin-related serine proteases. Both substantialmin and chymotrypsin-related serine proteases possess a catalytic triad comprising aspartic acid, histidine, and serine.

[0072] In subtilisin-associated proteases, the relative sequence of these amino acids, read from the amino terminus to the carboxyl terminus, is aspartic-histidine-serine. However, in chymotrypsin-associated proteases, the relative sequence is histidine-aspartic-serine. Therefore, subtilisin in this document refers to serine proteases possessing the catalytic triad of subtilisin-associated proteases. Examples include subtilisin as described in WO 89 / 06276 and EP 0283075, WO 89 / 06279, WO 89 / 09830, WO 89 / 09819, WO 91 / 06637, and WO 91 / 02792.

[0073] The parent protease and variants of the subtilis protease type (EC 3.4.21.62) can be bacterial proteases. The bacterial protease may be a Gram-positive bacterial polypeptide, such as Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus, Lactococcus, Oceanobacillus, Staphylococcus, Streptococcus, or Streptomyces protease, or a Gram-negative bacterial polypeptide, such as Campylobacter, Escherichia coli, Flavobacterium, Fusobacterium, Helicobacter, Lyobacter, Neisseria, Pseudomonas, Salmonella, or Ureaplasma protease. A review of this family is provided, for example, R. Siezen’s “Subtilases: Subtilisin-like Proteases”, and R. Bott and C. Betzel’s edited “Subtilisin enzymes”, pp. 75–95, New York, 1996.

[0074] In one aspect of the invention, the parent enzyme and variants may be *Bacillus salcalophilus*, *Bacillus amyloliquefaciens*, *Bacillus brevis*, *Bacillus circulans*, *Bacillus clausii*, *Bacillus coagulans*, *Bacillus firmus*, *Bacillus gibsonii*, *Bacillus lautus*, *Bacillus lentus*, *Bacillus licheniformis*, *Bacillus megaterium*, *Bacillus pumilus*, *Bacillus sphaericus*, *Bacillus stearothermophilus*, and *Bacillus subtilis*. The protease is either subtilis or Bacillus thuringiensis.

[0075] For the purposes of this invention, at least one protease may be selected from the following: subtilisin from Bacillus amyloliquefaciens BPN' (described by Vasantha et al. (1984) J. Bacteriol. [Journal of Bacteriology] Vol. 159, pp. 811-819 and JA Wells et al. (1983) in Nucleic Acids Research [Nucleic Acids Research], Vol. 11, pp. 7911-7925); subtilisin from Bacillus licheniformis (subtilisin Carlsberg [Bacillus subtilisin]; disclosed in EL Smith et al. (1968) J. Biol Chem [Journal of Biochemistry], Vol. 243, pp. 2184-2191 and Jacobs et al. (1985) Nucl. Acids Res [Nucleic Acids Research], Vol. 13, pp. 8913-8926); subtilisin PB92 (the original sequence of alkaline protease PB92 is described in EP... (As described in 283075A2); subtilisin 147 and / or 309 (Esperase® and Savinase®, respectively) disclosed in WO 89 / 06279; subtilisin from Bacillus tarda disclosed in WO 91 / 02792, such as Bacillus tarda DSM 5483 or variants of Bacillus tarda DSM 5483 as described in WO 95 / 23221; subtilisin from Bacillus alkalophilus (DSM 11233) disclosed in DE10064983; subtilisin from Bacillus gigantea (DSM 14391) disclosed in WO 2003 / 054184; subtilisin from Bacillus spp. (DSM 14390) disclosed in WO 2003 / 056017; and subtilisin from WO The following are disclosed: Bacillus subtilis protease from the genus Bacillus (DSM14392) as disclosed in WO 2003 / 055974; Bacillus subtilis protease from Bacillus giganteus (DSM 14393) as disclosed in WO 2003 / 054184; Bacillus subtilis protease having SEQ ID NO: 4 as described in WO 2005 / 063974; Bacillus subtilis protease having SEQ ID NO: 4 as described in WO 2005 / 103244; Bacillus subtilis protease having SEQ ID NO: 7 as described in WO 2005 / 103244; and Bacillus subtilis protease having SEQ ID NO: 2 as described in application DE 102005028295.4.

[0076] Suitable proteases also include those variants of the proteases described above that have proteolytic activity. In one embodiment, the protease variant includes a variant having at least 40% to 100% identity with the full-length polypeptide sequence of the parental enzyme as disclosed above. In one embodiment, the proteolytic protease variant 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 parental (wild-type) enzyme as disclosed above.

[0077] In another embodiment, the present invention relates to protease variants comprising conserved mutations that do not involve the functional domains of the corresponding protease. The protease variants of this embodiment having proteolytic activity may be at least 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% similar to the full-length polypeptide sequence of the parental (wild-type) enzyme.

[0078] In one embodiment, the protease variant has proteolytic activity according to the invention when it exhibits enhanced proteolytic activity compared to the parent protease.

[0079] Suitable Bacillus subtilis proteases may be at least 80% identical to SEQ ID NO:22 as described in EP 1921147, and are characterized by containing one amino acid (according to (a)-(h)) or according to (i) a combination of amino acids 101E, 101D, 101N, 101Q, 101A, 101G or 101S (according to BPN' number), and having proteolytic activity.

[0080] In one embodiment, the subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921147, and is characterized by containing the mutation (according to BPN' number) R101E, or S3T + V4I + V205I, or S3T + V4I + R101E + V205I or S3T + V4I + V199M + V205I + L217D, and has proteolytic activity.

[0081] In another embodiment, the subtilisin contains an amino acid sequence that is at least 80% identical to SEQ ID NO:22 as described in EP 1921147, and is further characterized by containing S3T + V4I + S9R + A15T + V68A + D99S + R101S + A103S + I104V + N218D (according to BPN' number) and having proteolytic activity.

[0082] The subtilisin may have an amino acid sequence that is at least 80% identical to that of SEQ ID NO:22 as described in EP 1921147, and is further characterized by comprising R101E, and one or more substitutions selected from the group consisting of: S156D, L262E, Q137H, S3T, R45E, D, Q, P55N, T58W, Y, L, Q59D, M, N, T, G61 D,R,S87E,G97S,A98D,E,R,S106A,W,N117E,H120V,D,K,N,S125M,P129D,E136Q,S144W,S161T,S163A,G,Y171L,A172S,N185Q,V199M,Y209W,M222Q,N238H,V244T,N261T,D andL262N,Q,D (as described in WO 2016 / 096711 and according to BPN' number), and possessing proteolytic activity.

[0083] At least one protease may be selected from those commercially available, including but not limited to those marketed under the trade names Alcalase®, Blaze®, Duralase™, Durazym™, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Primase®, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Coronase® Ultra, Neutrase®, Everlase®, and Esperase® (Novozymes A / S), and those marketed under the trade names Maxatase®, Maxacal®, Maxapem®, Purafect®, Purafect® Prime, PurafectMA®, Purafect Ox®, and Purafect OxP®, Puramax®, Properase®, FN2®, FN3®, FN4®, Excellase®, Eraser®, Ultimase®, Opticlean®, Effectenz®, Preferenz®, and Optimase® (those sold by Danisco / DuPont, Axapem™ (Gist-Brocases N.V.)), Bacillus subtilis alkaline protease (BLAP; as shown in Figure 29 of US 5,352,604) and its variants, as well as KAP (Alkaliophilic Bacillus subtilis protease) from Kao Corporation.

[0084] Known alignment methods include a variety of methods that can be used to align two given nucleic acid or amino acid sequences and calculate the degree of identity, see, for example, Arthur Lesk (2008), Introduction to bioinformatics, Oxford University Press, 3rd edition. In a preferred embodiment, the default settings are applied using 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).

[0085] In a preferred embodiment, the amylase and / or protease of the composition of the present invention are wild-type (naturally occurring) enzymes or mutants thereof that still bind calcium.

[0086] In other preferred embodiments, the liquid cleaning composition of the present invention comprises amylase and protease.

[0087] Example 5

[0088] The liquid cleaning composition according to Example 4(b) further comprises a protease stabilizing system comprising a peptide aldehyde.

[0089] In another embodiment, the liquid cleaning composition of the present invention does not contain boric acid, boric acid, or their derivatives. In an even more preferred embodiment, the cleaning composition contains only a single protease stabilization system, which is a protease stabilization system containing a peptide aldehyde.

[0090] Preferably, the liquid cleaning composition described herein comprises about 0.001% to about 10%, about 0.005% to about 8%, or about 0.01% to about 6% by weight of the composition an enzyme / protease stabilizing system. The enzyme / protease stabilizing system can be any stabilizing system compatible with the enzyme.

[0091] Preferably, the enzyme stabilizing system comprises 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), 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 stabilizing system comprising peptidaldehyde is a peptidaldehyde, peptidaldehyde acetal, or peptidaldehyde bisulfite adduct selected from Z-VAL-H or Z-GAY-H. Preferably, the protease stabilizing system may comprise a combination of at least two compounds selected from the group consisting of: (i) compounds selected from the group consisting of salts, polyols, and short-chain carboxylic acids, and (ii) compounds selected from the group consisting of peptidaldehyde, peptidaldehyde acetal, and peptidaldehyde bisulfite adduct.

[0092] Example 6

[0093] The liquid cleaning composition according to any one of Examples 1 to 5, wherein the at least one anionic surfactant

[0094] (a) present in an amount ranging from 2% to 40%, preferably 3% to 30%, and most preferably 4% to 25% by weight of the composition; and / or

[0095] (b) Select from the group consisting of: linear alkylbenzene sulfonates (LAS), alkyl sulfates (AS), alkylalkoxy sulfates (AExS), alkylalkoxycarboxylates, modified alkylbenzene sulfonates (MLAS), methyl ester sulfonates (MES), alkyl sulfosuccinates and α-olefin sulfonates (AOS).

[0096] Non-limiting examples of anionic surfactants that can be used herein—which can be used in combinations of more than one surfactant—include C9-C20 linear alkylbenzene sulfonates (LAS), C10-C20 main-chain, branched, and random alkyl sulfates (AS); C10-C18 secondary (2,3)alkyl sulfates; C10-C18 alkylalkoxy sulfates (AExS), where x is 1 to 30; C10-C18 alkylalkoxycarboxylates containing 1 to 5 ethoxy units; medium-chain branched alkyl sulfates, as discussed in US 6,020,303 and US 6,060,443; medium-chain branched alkylalkoxy sulfates, as discussed in US 6,008,181 and US 6,020,303; and modified alkylbenzene sulfonates (MLAS), such as WO 99 / 05243, WO 99 / 05242, and WO The methyl ester sulfonate (MES) and α-olefin sulfonate (AOS) discussed in 99 / 05244.

[0097] Preferred examples of suitable anionic surfactants are the following alkali metal and ammonium salts: C8-C12-alkyl sulfates, C12-C18-fatty alcohol ether sulfates, C12-C18-fatty alcohol polyether sulfates, ethoxylated C4-C12-alkylphenol (ethoxylation: 3 to 50 mol / mol ethylene oxide), C12-C18-alkyl sulfonic acids, C12-C18-alkyl sulfosuccinates, C12-C18-sulfoalkyl fatty acid esters, such as C12-C18-sulfomethyl fatty acid esters, C10-C18-alkylaryl sulfonic acids, preferably n-C10-C18-alkylbenzene sulfonic acids, C10-C18-alkylalkoxycarboxylic acid esters, and soaps such as C8-C24-carboxylic acids. Alkali metal salts of the above compounds are preferred, and sodium salts are particularly preferred.

[0098] In one embodiment of the invention, the anionic surfactant is selected from n-C10-C18-alkylbenzene sulfonic acid and fatty alcohol polyether sulfate, particularly, within the context of the invention, ethoxylated C12-C18-alkanol (preferably n-C12-C18-alkanol) sulfate half esters (ethoxylation: 1 to 50 mol ethylene oxide / mol).

[0099] In one embodiment of the invention, alcohol polyether sulfates derived from branched (i.e., synthetic) C11-C18-alkanols may also be used (ethoxylation: 1 to 50 mol of ethylene oxide / mol).

[0100] Preferably, the alkoxylation group of either type of alkoxylated alkyl sulfate based on C12-C18-fatty alcohol or based on branched (i.e., synthetic) C11-C18-alcohol is an ethoxylation group, and the average degree of ethoxylation of any alkoxylated alkyl sulfate is 1 to 5, preferably 1 to 3.

[0101] In another embodiment of the invention, the anionic surfactant is selected from biosurfactants, preferably rhamnolipid (RL), mannose erythritol lipolipid (MEL), trehalose lipolipid (TL), cellobiose lipolipid (CL) and / or sophorolipid (SL).

[0102] In a preferred embodiment of the present invention, the anionic surfactant is selected from C10-C15 linear alkylbenzene sulfonates, C10-C18 alkyl ether sulfates having 1-5 ethoxy units, and C10-C18 alkyl sulfates.

[0103] In the case where the liquid cleaning composition of the present invention contains more than one anionic surfactant, the amount ranging from 2% to 40%, preferably 3% to 30%, 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 surfactant).

[0104] Example 7

[0105] The liquid cleaning composition according to any one of Examples 1 to 6, wherein calcium (Ca 2+ It is present in an amount ranging from 0.0001% to 3%, preferably from 0.001% to 1%, based on the weight of the composition.

[0106] In a preferred embodiment, the lower limit of the calcium concentration is 0.0005%, 0.001%, 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%, 2%, or 1.5% by weight of the composition of the present invention.

[0107] In another embodiment, the above-mentioned calcium (Ca) 2+ It is free calcium. This means that it is neither part of a covalent interaction, nor forms a (long-term) salt interaction, nor is it complexed by a builder (chelating agent).

[0108] Furthermore, in a preferred embodiment, the liquid cleaning composition of the present invention contains an amount of magnesium (Mg) ranging from 0.0001% to 3%, more preferably from 0.001% to 1% by weight of the composition. 2+ ).

[0109] In preferred embodiments, the lower limit of magnesium concentration is 0.0005%, 0.001%, or 0.005% by weight of the composition of the present invention. In other preferred embodiments, the upper limit of calcium concentration is 2.5%, 2%, or 1.5% by weight of the composition of the present invention.

[0110] In another embodiment, the above-mentioned magnesium (Mg) 2+ It is free calcium. This means that it is neither part of a covalent interaction, nor forms a (long-term) salt interaction, nor is it complexed by a builder (chelating agent).

[0111] Techniques for measuring calcium and / or magnesium concentrations are well known in the art and include atomic absorption spectrometry (AA), inductively coupled plasma atomic emission spectrometry (ICP-AES), and inductively coupled plasma mass spectrometry (ICP-MS).

[0112] Example 8

[0113] The liquid cleaning composition according to any one of Examples 1 to 7, wherein the viscosity range is 30 to 3000 mPa*s, preferably 40 to 2500 mPa*s, and most preferably 50 to 2000 mPa*s.

[0114] In a preferred embodiment, the lower limit of the viscosity of the composition of the present invention is 35 mPa*s or 45 mPa*s. In other preferred embodiments, the upper limit of the viscosity of the composition of the present invention is 2800 mPa*s, 2300 mPa*s, or 2100 mPa*s.

[0115] All the viscosity values ​​mentioned above are at 20 1 / s and / or 20°C.

[0116] Viscosity can be measured using a viscometer or rheometer, which are well known to those skilled in the art.

[0117] Example 9

[0118] The liquid cleaning composition according to any one of Examples 1 to 8, wherein the pH value ranges from 5 to 12, preferably from 6 to 10, and most preferably from 7 to 9.

[0119] pH values ​​can be measured using pH paper, a colorimeter, or a spectrophotometer. 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, screened methyl orange, bromocresol green, methyl red, methyl violet, litmus (litmus), bromocresol violet, bromothymol blue, phenol red, neutral red, naphtholphthalein, cresol red, cresolphthalein, phenolphthalein, thymolphthalein, alizarin yellow R, and indigo carmine.

[0120] The pH of the composition can be adjusted using pH-modifying agents known in the art and measured at 25°C in demineralized water at a 10% product concentration. For example, NaOH can be used, and the actual weight percentage of NaOH can be varied and adjusted to a desired pH, such as pH 8.0. In one embodiment of the invention, the pH is adjusted to > 7 by using an amine, preferably an alkanolamine, more preferably triethanolamine.

[0121] Example 10

[0122] The liquid cleaning composition according to any one of Examples 1 to 9, wherein the cleaning composition is a detergent composition. Alternatively, the liquid cleaning composition is an automatic dishwashing (ADW) gel.

[0123] As used herein, the phrase "cleaning composition" includes compositions and formulations designed for cleaning soiled materials. Such compositions and formulations include those designed for cleaning any kind of soiled material or surface.

[0124] Compositions for “industrial and institutional cleaning” include such cleaning compositions designed for use in industrial and institutional cleaning, such as cleaning compositions for cleaning any kind of soiled materials or surfaces, such as hard surface cleaners for any kind of surfaces (including tile, carpet, PVC-coated surfaces, wood surfaces, metal surfaces, and painted surfaces).

[0125] "Compositions for fabric and household care" include cleaning compositions and formulations, including but not limited to laundry cleaning compositions and detergents, fabric softening compositions, fabric reinforcing compositions, fabric cleaning compositions, laundry pre-wash agents, laundry pretreatment agents, laundry additives, spray products, drying cleaners or compositions, laundry rinsing additives, washing 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 suitable forms that will be apparent to those skilled in the art in light of the teachings herein and are detailed below in the description of the compositions. Such compositions can be used as pre-wash treatments, post-wash treatments, or can be added during the rinsing or washing cycle of a washing operation, preferably during the washing cycle of a laundry or dishwashing operation, as further detailed below.

[0126] The cleaning compositions of the present invention can be in any liquid form, i.e., in the following forms: liquid, paste, sachet, gel; emulsion; delivered in a two- or multi-compartment container; single-phase or multi-phase unit dose; spray or foam detergent; pre-wet wipes (i.e., cleaning compositions combined with nonwoven materials, such as those discussed in US 6,121,165, Mackey, etc.); and other homogeneous, non-homogeneous, or single-phase or multi-phase cleaning product forms.

[0127] Example 11

[0128] The liquid cleaning composition according to any one of Examples 1 to 10, wherein the cleaning composition further comprises at least one element from the group consisting of: nonionic surfactants, amphoteric surfactants, co-cleaning agents, alcohols, biocides, thickeners, water-soluble polymers, clay stain removers / anti-redeposition agents, polymer detergents, bleaching agents, bleach activators, brighteners, odor control agents, pigments, dyes, opacifiers, toners, dye transfer inhibitors, defoamers, corrosion inhibitors, softeners, and fragrances.

[0129] In a preferred embodiment, the liquid cleaning composition of the present invention contains an enzyme other than amylase and protease. The upper limit of the concentration of the one or more additional enzymes is 5%, 3%, 2%, 1%, 0.5%, 0.1%, 0.01% or even 0% by weight of the composition of the present invention (meaning that the composition of the present invention does not contain any enzyme other than amylase and protease).

[0130] In a preferred embodiment, the liquid cleaning composition of the present invention comprises additional detergent-building compounds other than EDDS. The upper limit of the concentration of the one or more additional detergent-building compounds is 20%, 15%, %, 10%, 7%, 5%, 3%, 1%, 0.5% or even 0% by weight of the composition of the present invention (meaning that the composition of the present invention does not contain any additional detergent-building compounds other than EDDS).

[0131] The cleaning compositions of the present invention may—and preferably do—contain auxiliary cleaning additives (also referred to herein as “auxiliaries”), which are preferably in addition to components (i) to (v) as defined in Example 1.

[0132] Suitable auxiliary cleaning additives include detergent builders, co-detergent builders, structuring agents or thickeners, clay stain removers / anti-redeposition agents, polymer detergents, dispersants such as polymer dispersants, polymer grease cleaners, solubilizers, additional enzymes, enzyme stabilizers, additional surfactants, bleaching compounds, bleaching agents, bleaching activators, bleaching catalysts, brighteners, odor control agents, pigments, dyes, opacifiers, toners, dye transfer inhibitors, chelating agents, foaming agents, defoaming agents, color specks, silver care products, anti-discoloration agents and / or preservatives, alkalinity sources, pH adjusters, pH buffers, water-soluble additives, detergent granules, antibacterial agents, antioxidants, softeners, carriers, processing aids, fragrance precursors, dye fixatives, and fragrances.

[0133] Liquid cleaning compositions may contain rheology control agents / modifiers, emollients, humectants, skin rejuvenating actives, and solvents.

[0134] Suitable examples and levels of use of such cleaning aids can be found in WO 99 / 05242, U.S. Patent Nos. 5,576,282, 6,306,812 B1 and 6,326,348 B1.

[0135] Those skilled in the art will understand that detergency surfactants encompass any surfactant or mixture of surfactants that provides cleaning, stain removal, or washing benefits to soiled materials.

[0136] Therefore, the cleaning compositions of the present invention, such as fabric and household care products, and formulations for industrial and institutional cleaning, more specifically such as laundry detergents and hand dishwashing detergents, preferably additionally contain components (i) to (v), and preferably also contain additional adjuvants, such as those described above and below in more detail.

[0137] In addition to anionic surfactants, the liquid cleaning compositions of the present invention may contain an additional surfactant system, which may consist of a single surfactant or a combination of surfactants selected from nonionic surfactants, cationic surfactants, amphoteric surfactants, amphoteric surfactants, and mixtures thereof. Those skilled in the art will understand that surfactant systems for detergents encompass any of the mentioned surfactants or mixtures of surfactants that provide cleaning, stain removal, or washing benefits to soiled materials.

[0138] The cleaning compositions of the present invention preferably comprise an amount of surfactant system sufficient to provide the desired cleaning properties. In some embodiments, the additional cleaning composition comprises about 0.1% to about 70% of the surfactant system by weight of the composition. In other embodiments, the liquid cleaning composition comprises about 2% to about 60% of the surfactant system by weight of the composition. In still other embodiments, the cleaning composition comprises about 5% to about 30% of the surfactant system by weight of the composition. The surfactant system may comprise detergency surfactants selected from nonionic surfactants, cationic surfactants, amphoteric surfactants, amphoteric surfactants, and mixtures thereof.

[0139] Non-limiting examples of nonionic surfactants—which may also be used in combination with more than one other surfactant—include: C8-C18 alkyl ethoxylates, such as NEODOL® nonionic surfactants from Shell; ethylene oxide / propylene oxide block alkoxylates as PLURONIC® from BASF; C14-C22 medium-chain branched alkyl alkoxylates, BAEx, where x is 1 to 30, as discussed in US 6,153,577, US 6,020,303 and US 6,093,856; alkyl polysaccharides, as discussed in US 4,565,647, published January 26, 1986 in Llenado; specifically, alkyl polyglycosides, as discussed in US 4,483,780 and US 4,483,779; and polyhydroxy fatty acid amides, such as US The same applies to those discussed in 5,332,528; and to ether-terminated poly(oxyalkylated) alcohol surfactants, such as those discussed in US6,482,994 and WO 01 / 42408.

[0140] Preferred examples of nonionic surfactants include, in particular, alkoxylated alcohols and alkoxylated fatty alcohols, diblock and multiblock copolymers of ethylene oxide and propylene oxide, and reaction products of sorbitol with ethylene oxide or propylene oxide, as well as alkylphenol ethoxylates, alkyl glycosides, and polyhydroxy fatty acid amides (glucosamides).

[0141] Non-limiting examples of nonionic surfactants—which may also be used in combination with more than one other surfactant—include: C8-C18 alkyl ethoxylates, such as NEODOL® nonionic surfactants from Shell; ethylene oxide / propylene oxide block alkoxylates as PLURONIC® from BASF; C14-C22 medium-chain branched alkyl alkoxylates, BAEx, where x is 1 to 30, as discussed in US 6,153,577, US 6,020,303 and US 6,093,856; alkyl polysaccharides, as discussed in US 4,565,647, published January 26, 1986 in Llenado; and specifically, alkyl polyglycosides, such as US 4,483,780 and US 6,483,780. The following are discussed in 4,483,779; polyhydroxy fatty acid amides, such as those discussed in US 5,332,528; and ether-terminated poly(oxyalkylated) alcohol surfactants, such as those discussed in US 6,482,994 and WO01 / 42408.

[0142] Preferred examples of nonionic surfactants include, in particular, alkoxylated alcohols and alkoxylated fatty alcohols, diblock and multiblock copolymers of ethylene oxide and propylene oxide, and reaction products of sorbitol with ethylene oxide or propylene oxide, as well as alkylphenol ethoxylates, alkyl glycosides, and polyhydroxy fatty acid amides (glucosamides).

[0143] Preferred examples of alkoxylated alcohols and alkoxylated fatty alcohols are, for example, compounds having the general formula (A).

[0144] [Formula (A)]

[0145] The variables are defined as follows:

[0146] R1 is selected from straight-chain C1-C10-alkyl, preferably ethyl, and particularly preferably methyl.

[0147] R2 is selected from C8-C22-alkyl groups, such as n-C8H17, n-C10H21, n-C12H25, n-C14H29, n-C16H33, or n-C18H37.

[0148] 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, isopentyl, n-hexyl, isohexyl, sec-hexyl, n-heptyl, n-octyl, 2-ethylhexyl, n-nonyl, n-decyl, or isodel.

[0149] m and n are in the range of 0 to 300, where the sum of n and m is at least one.

[0150] Preferably, m is in the range of 1 to 100 and n is in the range of 0 to 30.

[0151] Here, the compound having the general formula (A) can be a block copolymer or a random copolymer, preferably a block copolymer.

[0152] Other preferred examples of alkoxylated alcohols and alkoxylated fatty alcohols are, for example, compounds having the general formula (B).

[0153] [Formula (B)]

[0154] The variables are defined as follows:

[0155] R1 may be the same or different and is selected from straight-chain C1-C4-alkyl groups, preferably the same in each case and is ethyl, and particularly preferably methyl.

[0156] R4 is selected from C6-C20 alkyl groups, particularly n-C8H17, n-C10H21, n-C12H25, n-C14H29, n-C16H33, and n-C18H37.

[0157] a is a number in the range of zero to 6, preferably 1 to 6.

[0158] b is a number in the range of zero to 20, preferably 4 to 20.

[0159] d is a number in the range of 4 to 25.

[0160] Preferably, at least one of a and b is greater than zero.

[0161] Here, the compound having the general formula (B) can be a block copolymer or a random copolymer, preferably a block copolymer.

[0162] Other suitable nonionic surfactants are selected from diblock and multiblock copolymers of ethylene oxide and propylene oxide. Other suitable nonionic surfactants are selected from ethoxylated or propoxylated sorbitol esters. Alkylphenol ethoxylates, alkyl polyglycosides, or polyhydroxy fatty acid amides (glucosamides) are also suitable. An overview of suitable other nonionic surfactants can be found in EP-A 0 851 023 and DE-A 198 19 187.

[0163] Of course, a mixture of two or more different nonionic surfactants can also exist.

[0164] In a preferred embodiment of the invention, the nonionic surfactant is selected from C12 / 14 and C16 / 18 fatty alcohol alkoxylates, C13 / 15 oxoalkanol alkoxylates, C13-alkanol alkoxylates, and 2-propylheptyl alcohol alkoxylates, each of which has 3-15 ethoxy units, preferably 4-10 ethoxy units, or has 1-3 propoxy units and 2-15 ethoxy units.

[0165] Non-limiting examples of amphoteric surfactants—which may also be used in combination with more than one other surfactant—include: a water-soluble amine oxide comprising an alkyl moiety having about 8 to about 18 carbon atoms and two portions selected from the group consisting of an alkyl moiety having about 1 to about 3 carbon atoms and a hydroxyalkyl moiety; and a water-soluble sulfoxide comprising an alkyl moiety having about 10 to about 18 carbon atoms and a portion selected from the group consisting of an alkyl moiety having about 1 to about 3 carbon atoms and a hydroxyalkyl moiety. See WO 01 / 32816, US 4,681,704 and US 4,133,779. Thus, suitable surfactants include so-called amine oxides, such as lauryl dimethylamine oxide (“laurylamine oxide”).

[0166] Preferred examples of amphoteric surfactants are amine oxides. Preferred amine oxides are alkyl dimethylamine oxides or alkylamidopropyl dimethylamine oxides, more preferably alkyl dimethylamine oxides, and especially cocoyl dimethylamino oxides. Amine oxides can have straight-chain or intermediate-branched alkyl moieties. Typical straight-chain amine oxides include water-soluble amine oxides containing an 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 is characterized by the following formula:

[0167] R1-N(R2)(R3)-O

[0168] Wherein 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. Linear-chain amine oxide surfactants may in particular include linear C10-C18 alkyl dimethylamine oxides and linear C8-C12 alkoxyethyl dihydroxyethylamine oxides. Preferred amine oxides include linear C10, linear C10-C12, and linear C12-C14 alkyl dimethylamine oxides. As used herein, “intermediate branch” means that the amine oxide has an alkyl moiety having n1 carbon atoms, wherein an alkyl branch is present on the alkyl moiety having n2 carbon atoms. The alkyl branch is located on the α-carbon of the nitrogen from the alkyl moiety. This type of branching of amine oxides is also referred to in the art as internal amine oxides. The sum of n1 and n2 is 10 to 24, preferably 12 to 20, and more preferably 10 to 16 carbon atoms. The number of carbon atoms (n1) of the alkyl moiety should be substantially the same as the number of carbon atoms (n2) of the alkyl branch, such that the alkyl moiety and the alkyl branch are symmetrical. As used herein, "symmetrical" means that in at least 50 wt.-% and more preferably at least 75 wt.-% to 100 wt.-% of the intermediate branched amine oxide used herein, (n1-n2) is less than or equal to 5, preferably 4, and most preferably 0 to 4 carbon atoms. The amine oxide further comprises two moieties, each independently selected from C1-C3 alkyl groups, C1-C3 hydroxyalkyl groups, or polyethylene oxide groups containing an average of about 1 to about 3 ethylene oxide groups. Preferably, both moieties are selected from C1-C3 alkyl groups, more preferably both are C1 alkyl groups.

[0169] In a preferred embodiment of the present invention, the amphoteric surfactant is selected from C8-C18 alkyl-dimethylamino oxide and C8-C18 alkyl-di(hydroxyethyl)amino oxide.

[0170] The cleaning composition may also contain amphoteric surfactants – which may also be used in combination with more than one other surfactant.

[0171] Suitable zwitterionic surfactants include betaines, such as alkyl betaines, alkylamidobetaines, imidazolinium betaines, sulfobetaine (INCI sulfobetaine), and phosphate betaines. Examples of suitable betaines and sulfobetaines are as follows (according to INCI nomenclature): Almond amidopropyl betaine, Apricotamidopropyl betaine, Avocadoamidopropyl betaine, Babassu oleamidopropyl betaine, Betaine amamidopropyl betaine, Betaine betaine, Low erucic acid amidopropyl betaine, Capryloyl / Decanamidopropyl betaine, Carnitine, Cetyl betaine, Cocamidoethyl betaine, Cocamidopropyl ... Aminopropylhydroxysulfonyl betaine, cocobetaine, cocobetaine hydroxysulfonyl betaine, coco / oleamidopropyl betaine, cocobetaine sulfonyl betaine, decyl betaine, oleylglycine dihydroxyethyl ester, daidzeinylglycine dihydroxyethyl ester, stearylglycine dihydroxyethyl ester, tallow glycine dihydroxyethyl ester, polydimethylsiloxanepropyl PG-betaine, erucamide propylhydroxysulfonyl betaine, hydrogenated tallow betaine, isostearamide propyl betaine, Laurylamidopropyl betaine, lauryl betaine, lauryl hydroxysulfonyl betaine, lauryl sulfonyl betaine, milk amamidopropyl betaine, mink oil amamidopropyl betaine, myristoyl amamidopropyl betaine, myristyl betaine, oleamidopropyl betaine, oleamidopropyl hydroxysulfonyl betaine, oil-based betaine, olive oil amamidopropyl betaine, palm oil amamidopropyl betaine, palmitoyl carnitine Palm kernel oleamidopropyl betaine, polytetrafluoroethylene acetoxypropyl betaine, castor oil oleamidopropyl betaine, sesame oil oleamidopropyl betaine, soybean oil oleamidopropyl betaine, stearamidopropyl betaine, stearyl betaine, butteramidopropyl betaine, butteramidopropyl hydroxysulfonyl betaine, butter betaine, butter dihydroxyethyl betaine, undecenoylamidopropyl betaine, and wheat germ oleamidopropyl betaine.

[0172] 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.

[0173] Non-limiting examples of cationic surfactants—which may also be used in combination with more than one other surfactant—include: quaternary ammonium surfactants that may have up to 26 carbon atoms, including: alkoxylated quaternary ammonium (AQA) surfactants as discussed in US 6,136,769; dimethylhydroxyethyl quaternary ammonium as discussed in US 6,004,922; dimethylhydroxyethyl lauryl ammonium chloride; polyamine cationic surfactants as discussed in WO 98 / 35002, WO 98 / 35003, WO 98 / 35004, WO 98 / 35005, and WO 98 / 35006; cationic ester surfactants as discussed in US Patent Nos. 4,228,042, 4,239,660, 4,260,529, and US 6,022,844; and cationic ester surfactants as discussed in US The amino surfactant discussed in 6,221,825 and WO00 / 47708 is specifically amamidopropyl dimethylamine (APA).

[0174] The compositions according to the invention may or may not contain an additional building agent besides EDDS. In the context of this invention, no distinction will be made between building agents and such components elsewhere referred to as "co-building agents". Examples of building agents are complexing agents, also referred to hereinafter as complexing agents, ion exchange compounds, and precipitants. Building agents are selected from citrates, phosphates, silicates, carbonates, phosphonates, aminocarboxylates, and polycarboxylates.

[0175] In a preferred embodiment, the additional builder is diethylenetriaminepenta (methylenephosphonic acid) (DTPMP).

[0176] The formulations according to the invention may contain one or more basic carriers. For example, if an alkaline pH is desired, the basic carrier ensures a pH of at least 9. Suitable carriers include, for example, the alkali metal carbonates, alkali metal bicarbonates, and alkali metal metasilicates mentioned above, and additionally, alkali metal hydroxides. In each case, the preferred alkali metal is potassium, and particularly preferred is sodium. In one embodiment of the invention, the pH is adjusted to > 7 by using an amine, preferably an alkanolamine, more preferably triethanolamine.

[0177] In one embodiment of the invention, in addition to amylase and protease, the composition or laundry product according to the invention additionally contains at least one enzyme.

[0178] In even more preferred embodiments, calcium and / or magnesium are not cofactors for the additional catalytic activity of the enzyme or otherwise required.

[0179] Preferably, the at least one additional enzyme is a detergent enzyme.

[0180] In one embodiment, additional enzymes are classified as oxidoreductases (EC 1), transferases (EC 2), hydrolases (EC 3), lyases (EC 4), isomerases (EC 5), or ligases (EC 6). EC numbers are based on the enzyme nomenclature recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (1992), including its supplements published between 1993 and 1999. Preferably, the enzyme is a hydrolase (EC 3).

[0181] In a preferred embodiment, the additional enzyme is selected from the group consisting of:

[0182] Protease, amylase, lipase, cellulase, mannanase, hemicellulase, phospholipase, esterase, pectinase, lactase, peroxidase, xylanase, keratinase, pectic acid lyase, keratinase, reductase, oxidase, phenol oxidase, lipoxygenase, ligninase, amylopectinase, tanninase, pentosanase, malic acid lyase, β-glucanase, arabinoside lyase, hyaluronidase, chondroitinase, laccase, nuclease, deoxyribonuclease, phosphodiester The enzyme comprises phytase, carbohydrate enzyme, galactanase, xanthan gumase, xyloglucanase, oxidoreductase, hydrolase, aminopeptidase, asparaginase, carbohydrate enzyme, carboxypeptidase, catalase, chitinase, cyclodextrin glycosyltransferase, α-galactosidase, β-galactosidase, glucosylamylase, α-glucosidase, β-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, deoxyribonuclease, dispersin, pectinase, oxidoreductase, and keratinase, as well as combinations of at least two of the aforementioned types. Most preferably, the additional enzyme is mannanase and / or lipase.

[0183] Additional enzymes may be incorporated into the composition in an effective amount sufficient to provide beneficial effects, preferably for primary and / or secondary washing effects, such as anti-ashing or anti-pilling effects (e.g., in the case of cellulase). Preferably, the additional enzyme is present in the composition at a level of about 0.00001% to about 5% by weight of the composition, more preferably about 0.00001% to about 2%, more preferably about 0.0001% to about 1%, or even more preferably about 0.001% to about 0.5% of the enzyme protein.

[0184] The compositions according to the present invention may contain one or more bleaching agents (bleach).

[0185] Preferred bleaching agents are selected from sodium perborate, anhydrous or, for example, as a monohydrate or as a tetrahydrate or so-called dihydrate, sodium percarbonate, anhydrous or, for example, as a monohydrate, and sodium persulfate, wherein the term "persulfate" in each case includes salts of persulfate H2SO5 as well as perdisulfate.

[0186] In view of this, the alkali metal salt can also be an alkali metal bicarbonate, an alkali metal perborate, or an alkali metal persulfate in each case. However, in each case, a dialkali metal salt is preferred.

[0187] The formulations according to the invention may contain one or more bleaching catalysts. The bleaching catalysts may 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. Manganese, iron, cobalt, ruthenium, molybdenum, titanium, vanadium, and copper complexes having nitrogen-containing tripod ligands, as well as cobalt-, iron-, copper-, and ruthenium-amine complexes, may also be used as bleaching catalysts.

[0188] The formulations according to the invention may contain one or more bleaching activators, such as tetraacetylethylenediamine, tetraacetylmethylenediamine, tetraacetylglycolurea, tetraacetylhexanediamine, acylated phenol sulfonates such as n-nonanoyloxybenzenesulfonate or isonanoyloxybenzenesulfonate, (S)NOBS, LOBS, DOBA, PAP, N-methylmorpholinium acetonitrile (“MMA salt”), trimethylammonium acetonitrile, N-imides such as N-nonanoylsuccinimide, 1,5-diacetyl-2,2-dioxohexahydro-1,3,5-triazine (“DADHT”), or nitrile quaternary ammonium (trimethylammonium acetonitrile).

[0189] As a precursor to H2O2, consider peroxides, which are every compound capable of producing hydrogen peroxide in aqueous solution, such as the organic and inorganic peroxides known in the literature and commercially available, which bleach textiles at conventional washing temperatures, such as 10°C to 95°C.

[0190] However, inorganic peroxides, such as persulfates, perborates, percarbonates, and / or persilicates, are preferably used. These peroxides are typically used in amounts of 2 wt% to 80 wt%, preferably 4 wt% to 30 wt%, based on the weight of the composition.

[0191] Typically, the following describes it in more detail as having equation (1) The compound is present in the composition in an amount of 0.05 wt% to 15 wt% based on the total weight of the composition, preferably 0.1 wt% to 10 wt%.

[0192] Examples of suitable inorganic peroxides are sodium perborate tetrahydrate or sodium perborate monohydrate, sodium percarbonate, and inorganic peroxyacid compounds, such as potassium persulfate (MPS). If an organic or inorganic peroxyacid is used as the peroxide compound, its amount is typically in the range of about 2 wt% to 80 wt%, preferably 4 wt% to 30 wt%, based on the weight of the composition.

[0193] Organic peroxides are, for example, single or multiple peroxides, urea peroxides, combinations of C1-C4 alkanol oxidases and C1-C4 alkanols (such as methanol oxidase and ethanol as described in WO 95 / 07972), and alkyl hydroxy peroxides, such as cumene hydroperoxide and tert-butyl hydroperoxide.

[0194] These peroxides can exist in various crystalline forms and have different water contents, and they can also be used with other inorganic or organic compounds to improve their storage stability.

[0195] Peroxyacids can also be used as oxidizing agents. One example is that which has formula (1). Organic monoperacid,

[0196] in

[0197] M represents hydrogen or a cation.

[0198] R 19 Indicates unsubstituted C1-C 18 Alkyl; Substituted C1-C 18 Alkyl; unsubstituted aryl; substituted aryl; -(C1-C6 alkylene)-aryl, wherein the alkylene and / or the alkyl group may be substituted; and phthalimide C1-C8 alkylene, wherein the phthalimide and / or the alkylene group may be substituted.

[0199] Preferred single organic peroxy acids and their salts are those having the formula Those,

[0200] in

[0201] M represents hydrogen or an alkali metal, and

[0202] R' 19 This indicates unsubstituted C1-C4 alkyl; phenyl; -C1-C2 alkylene-phenyl or

[0203] Phthalimide C1-C8 alkylene group.

[0204] CH3COOOH and its alkali metal salts are particularly preferred.

[0205] ε-phthalimide peroxyhexanoic acid and its alkali metal salt (PAP) are particularly preferred.

[0206] Also suitable are diperoxic acids, such as 1,12-disperoxydodecanoic acid (DPDA), 1,9-disperoxyazeloic acid, diperoxadecanoic acid, diperoxadecanoic acid, diperoxisophthalic acid, 2-decyldisperoxybutane-1,4-diacid and 4,4'-sulfonylbisperoxybenzoic acid.

[0207] In some cases, the use of additional bleach activators can be advantageous.

[0208] The term bleaching activator is often used synonymously with peroxy acid bleaching precursor. All of the above-mentioned peroxy compounds can be used alone or in combination with peroxy acid bleaching precursors.

[0209] These precursors are the corresponding carboxylic acids, carboxylic anhydrides, carbonyl chlorides, amides, or esters, which can form peroxyacids upon hydrolysis. Such reactions are generally known.

[0210] Peroxyacid bleaching precursors are known and described in detail in the literature, such as in British Patents 836988; 864,798; 907,356; 1,003,310 and 1,519,351; German Patents 3,337,921; EP-A-0185522; EP-A-0174132; EP-A-0120591; and US Patents 1,246,339; 3,332,882; 4,128,494; 4,412,934 and 4,675,393.

[0211] Suitable bleaching activators include those with O- and / or N-acyl groups and / or unsubstituted or substituted benzoyl groups. Preferred are polyacylated alkylene diamines, especially tetraacetylethylenediamine (TAED); acylated glycoureas, especially tetraacetyldiol urea (TAGU), N,N-diacetyl-N,N-dimethylurea (DDU); sodium 4-benzoyloxybenzenesulfonate (SBOBS); sodium 1-methyl-2-benzoyloxybenzene-4-sulfonate; sodium 4-methyl-3-benzoyloxybenzoate; trimethylammonium tolueneoxybenzenesulfonate; acylated triazine derivatives, especially 1,5-diacetyl-2,4-dioxohexahydro-1,3,5-triazine (DADHT); compounds having formula (10):

[0212]

[0213] Where R 22 It is a sulfonate group, a carboxylic acid group, or a carboxylic ester group, and wherein R 21 Is it a straight chain or a branched chain (C7-C)? 15Alkyl groups, especially activators known by the names SNOBS, SLOBS, and DOBA; acylated polyols, especially triacetin, ethylene glycol diacetate, and 2,5-diacetoxy-2,5-dihydrofuran; and also acetylated sorbitol and mannitol and acylated sugar derivatives, especially pentaacetyl glucose (PAG), sucrose polyacetate (SUPA), pentaacetylfructose, tetraacetylxylose, and octaacetyllactose, as well as acetylated, optionally N-alkylated glucosamine and gluconolactone. Combinations of conventional bleaching activators known from German patent application DE-A-44 43 177 may also be used. Nitrile compounds that form perimino acids with peroxides are also considered as bleaching activators.

[0214] Another class of useful peroxyacid bleaching precursors are cationic ones, namely quaternary ammonium-substituted peroxyacid precursors, such as those disclosed in U.S. Patent Nos. 4,751,015 and 4,397,757, EP-A0284292 and EP-A-331,229. Examples of such peroxyacid bleaching precursors are: 2-(N,N,N-trimethylammonium)ethyl-4-sulfophenyl carbonate sodium chloride-(SPCC), N-octyl,N,N-dimethyl-N10-carboxyphenoxydecyl ammonium chloride-(ODC), 3-(N,N,N-trimethylammonium)propyl-4-sulfophenylcarboxylate sodium salt, and N,N,N-trimethylammonium tolueneoxybenzenesulfonate.

[0215] Additional bleaching catalysts may also be used, such as transition metal complexes disclosed in EP1194514, EP 1383857 or WO 04 / 007657.

[0216] Formulations according to the invention may contain one or more corrosion inhibitors. In this case, this should be understood to include those compounds that inhibit the corrosion of metals. Examples of suitable corrosion inhibitors are triazoles, particularly benzotriazole, bisbenzotriazole, aminotriazole, alkylaminotriazole, and phenol derivatives, such as hydroquinone, pyrocatechol, hydroxyhydroquinone, gallic acid, phloroglucinol, or pyroglucinol.

[0217] In one embodiment of the invention, the formulation according to the invention comprises a total of 0.1% to 1.5% corrosion inhibitor by weight.

[0218] The formulations according to the present invention may also contain cleaning polymers and / or stain-removing polymers.

[0219] Clean polymers may include, but are not limited to: "multifunctional alkoxylated polyethyleneimine" (e.g., BASF's Sokalan® HP20), "multifunctional alkoxylated diamine" (e.g., BASF's Sokalan® HP96), BASF's Sokalan® SR400 A, and terephthalic acid-based polyesters, such as Clariant's TexCare®, including TexCare® SRN 170, TexCare® SRN 172, TexCare® SRN 260, TexCare® SRN260 SG Terra, and TexCare® SRA 300, as well as different combinations of all the aforementioned polymers.

[0220] Suitable polyfunctional alkoxylated polyethyleneimines are typically ethoxylated polyethyleneimines having 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. Suitable polyfunctional alkoxylated polyethyleneimines have ethylene oxide side chains of 80 wt.-% to 99 wt.-%, preferably 85 wt.-% to 99 wt.-%, more preferably 90 wt.-% to 98 wt.-%, and most preferably 93 wt.-% to 97 wt.-% or 94 wt.-% to 96 wt.-% based on the total weight of the material. Ethoxylated polyethylidene imines are typically based on a polyethylidene core and a polyethylene oxide shell. A suitable polyethyleneimine core molecule is a polyethyleneimine having a weight-average molecular weight Mw in the range of 500 to 5000 g / mol. Preferably, a molecular weight of 500 to 1000 g / mol is used, and even more preferably, a Mw of 600 to 800 g / mol is used. Then, the ethoxylated polymer has an average of 5 to 50, preferably 10 to 35, and even more preferably 20 to 35 ethylene oxide (EO) units / NH-functional groups.

[0221] Suitable polyfunctional alkoxylated diamines are typically ethoxylated C2 to C12 alkylene diamines, preferably hexamethylene diamines, which are further quaternized and optionally sulfated. Typical polyfunctional alkoxylated diamines have a weight-average molecular weight (Mw) in the range of 2000 to 10000, more preferably 3000 to 8000, and most preferably 4000 to 6000 g / mol. In a preferred embodiment of the invention, ethoxylated hexamethylene diamines that are further quaternized and sulfated can be used, which contain an average of 10 to 50, preferably 15 to 40, and even more preferably 20 to 30 ethylene oxide (EO) groups / NH-functional groups, and preferably have two cationic ammonium groups and two anionic sulfate groups.

[0222] In a preferred embodiment of the invention, the cleaning composition may contain at least one polyfunctional alkoxylated polyethyleneimine and / or at least one polyfunctional alkoxylated diamine to improve cleaning performance, such as preferably improving stain removal ability, especially the primary detergency of laundry detergents on particulate stains on polyester fabrics. The polyfunctional polyethyleneimine or polyfunctional diamine or mixture thereof described above may be added to the laundry detergent and cleaning composition in an amount typically 0.05 wt.-% to 15 wt.-%, preferably 0.1 wt.-% to 10 wt.-%, more preferably 0.25 wt.-% to 5 wt.-%, and even as low as up to 2 wt.% based on the specific total composition (containing other components and water and / or solvent).

[0223] In another preferred embodiment of the invention, the cleaning composition may contain at least one terephthalic acid-based polyester as a stain-removing polymer to improve the whiteness of the fabric after washing, especially the whiteness of polyester fabrics.

[0224] Therefore, one aspect of the present invention is a laundry detergent composition, the liquid laundry detergent comprising at least one compound selected from polyfunctional alkoxylated polyethyleneimine, polyfunctional alkoxylated diamine and terephthalic acid-based polyester, and mixtures thereof.

[0225] The cleaning composition of the present invention may also contain at least one antimicrobial agent (also commonly referred to as a preservative).

[0226] The composition may contain one or more antimicrobial agents and / or preservatives as listed on pages 35 to 39 of patent WO 2021 / 115912 A1.

[0227] Of particular interest are the following antimicrobial agents and / or preservatives:

[0228] 4,4'-Dichloro-2-hydroxydiphenyl ether (CAS No. 3380-30-1), also known as 5-chloro-2-(4-chlorophenoxy)phenol, diclosan, DCPP, is commercially available as a 30 wt% solution of 4,4'-dichloro-2-hydroxydiphenyl ether in 1,2-propanediol under the trade name Tinosan® HP 100 (BASF); 2-phenoxyethanol (CAS No. 122-99-6, also known as phenoxyethanol, methylphenyl glycol, phenoxyethanol, 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). AS); Glutaraldehyde (CAS No. 111-30-8, other names: 1-5-glutaraldehyde, pentyl-1,5-dialdehyde, glutaral, glutardialdehyde, Protectol® GA, Protectol® GA 50, Myacide® GA); Glyoxal (CAS No. 107-22-2; other names: ethandial, oxylaldehyde, 1,2-glyoxal, Protectol® GL); 2-Butyl-benzo[d]isothiazol-3-one (BBIT, CAS No. 4299-07-4); 2-Methyl-2H-isothiazol-3-one (MIT, CAS No. 2682-20-4); 2-Octyl-2H-isothiazol-3-one (OIT, CAS No. 26530-20-1); 5-Chloro-2-methyl-2H-isothiazol-3-one (CIT, CMIT, CAS No. 26172-55-4); 5-Chloro-2-methyl-2H-isothiazol-3-one (CMIT, EINECS 247-500-7) and 2-Methyl-2H-isothiazol-3-one (MIT, EINECS Mixtures of 220-239-6 (a mixture of CMIT / MIT, CAS No. 55965-84-9); 1,2-benzisothiazol-3(2H)-one (BIT, CAS No. 2634-33-5); hexano-2,4-dienoic acid (sorbic acid, CAS No. 110-44-1) and its salts, such as calcium sorbate, sodium sorbate, potassium (E,E)-hexano-2,4-dienoic acid (potassium sorbate, CAS No. 24634-61-5); lactic acid and its salts; L-(+)-lactic acid (CAS No. 79-33-4).Benzoic acid and its sodium salts (CAS No. 65-85-0, CAS No. 532-32-1) and benzoates, such as ammonium benzoate, calcium benzoate, magnesium benzoate, MEA-benzoate, potassium benzoate; salicylic acid and its salts, such as calcium salicylate, magnesium salicylate, MEA salicylate, sodium salicylate, potassium salicylate, TEA salicylate; benzalkonium chloride, benzalkonium bromide and benzalkonium saccharin, such as benzalkonium chloride, benzalkonium bromide, benzalkonium saccharin (CAS Nos. 8001-54-5, 63449-41-2, 91080-29-4). 68989-01-5, 68424-85-1, 68391-01-5, 61789-y71-7, 85409-22-9; Didecyl dimethyl ammonium chloride (DDAC, CAS No. 68424-95-3 and CAS No. 7173-51-5); N-(3-aminopropyl)-N-dodecylpropane-1,3-diamine (diamine, CAS No. 2372-82-9); Peracetic acid (CAS No. 79-21-0); Hydrogen peroxide (CAS No. 7722-84-1).

[0229] The antimicrobial agent is added to the composition at a concentration of 0.001% to 10% relative to the total weight of the composition.

[0230] Preferably, the composition contains 0.1% to 2% of 2-phenoxyethanol or 0.005% to 0.6% of 4,4'-dichloro-2-hydroxydiphenyl ether (DCPP).

[0231] Therefore, the present invention further covers a method for preserving an aqueous (liquid) composition according to the invention against microbial contamination or growth, the method comprising adding 2-phenoxyethanol. The present invention also further covers a method for providing antimicrobial action to textiles after treatment with a solid laundry detergent (e.g., powder, granules, capsules, tablets, sticks, etc.), liquid laundry detergent, softener, or post-rinse agent containing 4,4'-dichloro-2-hydroxydiphenyl ether (DCPP).

[0232] In another embodiment, the invention also covers a composition further comprising an antimicrobial agent disclosed below (preferably selected from the group consisting of 2-phenoxyethanol), more preferably comprising an amount of the antimicrobial agent ranging from 2 ppm to 5% by weight of the composition; and even more preferably comprising 0.1% to 2% phenoxyethanol.

[0233] As used herein, the term "dye fixative" refers to compounds that reduce or even stop dye penetration into colored fabrics during the washing process. Dye fixatives include, but are not limited to, cationic dye fixatives, crosslinking fixatives, and formaldehyde-based fixatives. These compounds are well-known to those skilled in the art and are commercially available from BASF SE, Huntsman, Archroma, Fineotex, Biotex Malaysia, or Dystar. Exemplary but not limiting dye fixatives include Basilen fixative F-RP, Albafix ECO, Finofix NF, poly DADMAC, and polyamines (DCDA-DETA, epichlorohydrin-DMA, epichlorohydrin-DETA, etc.).

[0234] The formulations according to the invention may also contain water and / or additional organic solvents, such as ethanol or propylene glycol.

[0235] Other optional ingredients may include, but are not limited to, viscosity modifiers, foam promoters or defoamers, fragrances, dyes, optical brighteners and dye transfer inhibitors.

[0236] Example 12

[0237] Use of the liquid cleaning composition according to any one of Examples 1 to 11 for cleaning fabrics.

[0238] As used herein, the term "fabric" applies to any type of cloth or textile that contains natural and / or synthetic materials, such as, but not limited to, upholstery and carpets.

[0239] Example 13

[0240] A cleaning method comprising contacting a fabric with a liquid cleaning composition according to any one of Examples 1 to 11.

[0241] As used herein, the term "cleaning" refers to any act of removing dirt, bleaching, reducing microbial communities, or a combination thereof. This includes washing fabrics by means of a washing machine, an automatic dishwashing machine, or by hand rinsing with water or washing fabrics with the liquid cleaning composition of the present invention. Preferably, cleaning is performed at a temperature of 60°C or lower, more preferably at 40°C or lower, and most preferably at 30°C or lower. In other preferred embodiments, the cleaning method is performed under water-saving conditions. This means that no more than 60%, 70%, 80%, 90%, or 95% of the water generally recommended for a given cleaning procedure is used in the cleaning method of the present invention.

[0242] Example 14

[0243] A method for manufacturing a liquid cleaning composition, the method comprising contacting and mixing the components (i) to (v) of Example 1.

[0244] As used interchangeably herein, the terms "contacting" or "bringing into contact" refer to the act of combining two or more components, preferably all components (i) to (v), together by dissolving, suspending, blending, slurrying, or stirring. As used herein, the term "mixing" means blending, dispersing, or emulsifying components (i) to (v) of the liquid cleaning composition of the invention to obtain a random or substantially equal distribution of all components (i) to (v). One or both of the above steps can be performed in a solid state. Alternatively, two or more components, preferably all components (i) to (v), are "contacted" and "mixed" in a liquid, preferably water.

[0245] General cleaning compositions and formulations

[0246] The following compositions (including those in the table) disclosed below disclose certain types of general-purpose cleaning compositions that correspond to typical compositions associated with typical washing conditions typically used in regions and countries around the world.

[0247] A composition shown is a comparative composition when it does not contain at least one of the components (i) to (v), especially EDDS. A composition is considered to fall within the scope of the invention when it contains all the components (i) to (v) in the amounts described herein.

[0248] The liquid laundry detergent according to the invention contains calcium (Ca) in the range of 0.000001% to 5% by weight of the composition. 2+ This liquid laundry detergent, having a viscosity ranging from 20 to 10000 mPa*s and a pH value between 4 and 14, is composed of the following:

[0249] 0.0005% - 20% of EDDS

[0250] 0.1% - 50% anionic surfactants

[0251] 0.1% - 40% of other builders, co-builders and / or chelating agents

[0252] 0.000001% - 5% of protease or amylase or a combination of protease and amylase

[0253] 0.1% - 50% other adjuvants

[0254] Replenish water to 100%.

[0255] The preferred liquid laundry detergent according to the invention has a calcium content ranging from 0.0001% to 3% by weight of the composition. 2+ This liquid laundry detergent, having a viscosity ranging from 30 to 3000 mPa*s and a pH value between 5 and 12, is composed of the following:

[0256] 0.001% - 15% of EDDS

[0257] 2% - 40% anionic surfactants selected from C10-C15-LAS (alkylbenzene sulfonic acid) and / or C10-C18 alkyl ether sulfates containing 1-5 ethoxy units.

[0258] 1.5% - 10% of nonionic surfactants selected from C10-C18-alkylethoxylates containing 3-10 ethoxy units.

[0259] 2% - 20% soluble organic building blocks / co-building blocks, selected from C10-C18 fatty acids, dicarboxylic acids and tricarboxylic acids, hydroxydicarboxylic acids and hydroxytricarboxylic acids, and polycarboxylic acids.

[0260] 0.0001% - 1% of protease or amylase or a combination of protease and amylase

[0261] 0.5% - 20% of mono- or di-ols, selected from ethanol, isopropanol, ethylene glycol, or propylene glycol.

[0262] 0.1% - 20% other adjuvants

[0263] Replenish water to 100%.

[0264] In a preferred embodiment, the composition according to the invention is used in a detergent for manual dishwashing.

[0265] The liquid manual dishwashing detergent according to the present invention comprises the following:

[0266] 0.05% - 10% of EDDS

[0267] 1% - 50% surfactant

[0268] 0.1% - 50% of other adjuvants

[0269] Replenish water to 100%.

[0270] The preferred liquid manual dishwashing detergent according to the present invention comprises the following:

[0271] 0.2% - 5% of EDDS

[0272] 5% - 40% anionic surfactants selected from C10-C15-LAS, C10-C18 alkyl ether sulfates containing 1-5 ethoxy units, and C10-C18 alkyl sulfates.

[0273] 0-10% cocamidopropyl betaine

[0274] 0% - 10% laurylamine oxide

[0275] 0% - 2% of nonionic surfactant, preferably C10-Gelbert alcohol alkoxylate.

[0276] 0% - 5% enzyme, preferably amylase, and preferably also an enzyme stabilizing system.

[0277] 0.5% - 20% of mono- or di-ols, selected from ethanol, isopropanol, ethylene glycol, or propylene glycol.

[0278] 0.1% - 20% other adjuvants

[0279] Replenish water to 100%.

[0280] The two liquid manual dishwashing detergents mentioned above contain calcium (Ca) in the range of 0.0001% to 3% by weight of the composition. 2+ It has a viscosity ranging from 30 to 3000 mPa*s and a pH value ranging from 5 to 12.

[0281] ADW Gel Formulation

[0282] In another embodiment, the composition according to the invention is used in an automatic dishwashing (ADW) gel formulation.

[0283] The preferred ADW gel formulation according to the present invention comprises the following:

[0284] 0.05% - 20% of EDDS

[0285] 0.1% - 0.5% anionic surfactant

[0286] 1% - 20% nonionic surfactants

[0287] 0.1-50% of detergent builders, co-builders, and / or chelating agents

[0288] 0.1-50% of other adjuvants

[0289] Up to a total of 100% water.

[0290] The preferred ADW gel according to the present invention comprises the following:

[0291] 0.2% - 20% of EDDS

[0292] 0.1% - 0.5% of anionic surfactants selected from linear alkylbenzene sulfonates (LAS), alkyl sulfates (AS), alkylalkoxy sulfates (AES), modified alkylbenzene sulfonates (MLAS), methyl ester sulfonates (MES), and α-olefin sulfonates (AOS).

[0293] 1% - 5% of nonionic surfactants selected from hydroxyl mixed ethers, alcohol ethoxylates, and alcohol alkoxylates.

[0294] 1%-7% of polymers (e.g., polyacrylates, polyacrylates with sulfonated monomers, biodegradable polymers (polyaspartic acid, PESA, biografted polymers)).

[0295] 2% - 20% chelating agents, such as citrate, methylglycine diacetic acid, GLDA

[0296] An enzyme system of 0.05% - 5%, containing at least one enzyme suitable for detergent applications and preferably an enzyme stabilizing system; a protease and amylase system.

[0297] 0.1-50% of other auxiliary agents (fragrances, 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)

[0298] Replenish water to 100%.

[0299] The two automatic dishwashing (ADW) gel formulations described above contain calcium (Ca) in the range of 0.0001% to 3% by weight of the composition. 2+ It has a viscosity ranging from 30 to 3000 mPa*s and a pH value ranging from 5 to 12.

[0300] Components (i) to (v) according to claim 1, and other components of the cleaning composition, can be separated by formulation in different compartments, such as in different compartments of a multi-compartment bag or bottle with different chambers, wherein the liquid is dispensed simultaneously from these different compartments to ensure that a predetermined amount of each component from each compartment is applied at each individual point of use. Such multi-compartment bags and bottles are also known to those skilled in the art.

[0301] The following describes certain types of general-purpose cleaning compositions, corresponding to typical compositions used under typical washing conditions in regions and countries around the world.

[0302] Table 1: General formula of laundry detergent compositions according to the present invention, having calcium (Ca) in the range of 0.000001% to 5% by weight of the composition. 2+ The content has a viscosity ranging from 20 to 10000 mPa*s and a pH value ranging from 4 to 14.

[0303]

[0304] Table 2: Liquid Washing Frame Accessories:

[0305]

[0306] *Preparations without EDDS are used as comparative examples.

[0307] Table 2 - Continued: Liquid washing frame preparations according to the present invention:

[0308]

[0309] *Preparations without EDDS are used as comparative examples.

[0310] The following examples are intended to further illustrate the invention but do not limit its scope.

[0311] This invention encompasses the specific embodiments described throughout this disclosure as part of the invention; various additional options are disclosed in the specification as “optional,” “preferred,” “more preferred,” “even more preferred,” or “most preferred” (or “preferred,” etc.), and options of specific embodiments may be selected individually and independently (unless such independent selection is impossible due to the nature of the feature or if such independent selection is explicitly excluded) and then combined with any other embodiment (where other such options and preferences may also be selected individually and independently, unless such independent selection is impossible due to the nature of the feature or if such independent selection is explicitly excluded), wherein each and any and all such possible combinations are included as separate embodiments as part of the invention. Example

[0312] I) Storage experiment of amylase

[0313] Storage stability of amylase was determined by enzyme activity assay in liquid detergent after storage at 38°C for up to 28 days.

[0314] To test the storage stability of amylase, liquid laundry test formulation F15 was prepared using a mixture of 1% or 2.2% EDDS, 2.2% GLDA, 2.2% citrate, 2.2% DTPA, 1.5% citrate, and 0.7% GLDA. Table 3 shows the liquid laundry detergents that have been used for application tests to determine the effect of builder on enzyme stability by testing amylase activity. All formulations were stored at 38°C for 1, 2, 7, 14, or 28 days.

[0315] Table 1: Composition of liquid detergent formulations used to test amylase stability

[0316]

[0317] LAS: Anionic surfactant; linear dodecylbenzenesulfonic acid (CAS 27176-87-0): Biosoft® D-40 (approximately 38% active ingredient) (Stepan)

[0318] AES (alkyl ether sulfate); anionic surfactant; poly(oxy-1,2-ethanediyl), α.-sulfonyl-ω.-hydroxy-, C 12-14 -Alkyl ether, sodium salt (CAS 68891-38-3): Standapol® ES-3 K (approximately 28% active ingredient)

[0319] AEO (Alcohol Ethoxylate): Nonionic surfactant; C 12 C 14 Fatty alcohol (6.5 EO): Lutensol® A 65N (approximately 100% active ingredient)

[0320] Chelates: sodium citrate dihydrate, DTPA (Trilon® C liquid, approximately 42% active substance), EDDS (approximately 35% active substance), GLDA (Dissolvine® GL-47-S, approximately 47% active substance) (Nouryon), or combinations thereof.

[0321] Protease product: Lavergy® Pro 106 LS

[0322] Liquid detergent formulations should be stored at 38°C for up to 4 weeks. 4 weeks of storage is considered equivalent to approximately 9 months at room temperature or > 15 months at 8°C.

[0323] Post-storage amylase activity was quantitatively measured by releasing the chromophore p-nitrophenol (pNP) from the substrate Ethyliden-capped pNPG7 (Roche Applied Science, Material No. 10880078103). α-Amylase degrades the substrate into smaller molecules, and these smaller products are treated with an excess of α-glucosidase (Roche Applied Science, Material No. 11626329103) compared to α-amylase until pNP is released; the release of pNP, measured by an increase in absorbance at 405 nm, is proportional to the α-amylase activity of the sample. Amylase standard: Termamyl 120 L (Sigma 3403). Starch-degrading activity was determined before and after storage.

[0324] Residual enzyme activity corresponds to the enzyme activity remaining when compared to the initial enzyme activity available at time 0 before storage.

[0325] Test Results

[0326] Amylase % relative activity in enzyme assay

[0327]

[0328] The standard error of each of the above values ​​is 2.5% or less. Therefore, the compositions of the present invention containing EDDS exhibit significant benefits for enzyme stability.

[0329] II) Storage and Application Experiments of Amylase and Protease

[0330] Storage stability of protease and amylase was determined by residual washing performance in liquid detergent after storage at 37°C for up to 28 days.

[0331] To test the storage stability of proteases and amylases, liquid laundry test formulations F16, free of builders, were prepared using 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 in the application test to determine the effect of builders on enzyme stability by testing primary cleaning performance. All formulations were stored at 37°C for 7, 14, or 28 days. After the storage period, the formulations were washed using two different methods.

[0332] Table 4: Liquid laundry test formulation according to the present invention:

[0333]

[0334] 1 NIS1: Nonionic surfactant; C 13C 15 Carbonyl synthesis of alcohol ethoxylates (7 EO): Dehydol LT 7

[0335] Protease product: Lavergy® PRO 114 LS (BASF)

[0336] Amylase product: Amplify® prime 100L (Novozymes)

[0337] A) Application testing in HTS (High Throughput Systems); small-scale

[0338] The washing performance of the preparation is determined as follows.

[0339] Measure the L*, a*, and b* values ​​of a single stain before washing with MACH 5 from CFT / Color Consultant. The fabric is then washed in the detergent formulation at 30°C. After washing, the fabric is rinsed and dried.

[0340] After drying, washing performance for a single stain was determined by measuring L*, a*, and b* values ​​using a MACH 5 from CFT / Color Consultant. The dE value was calculated from the individual values ​​before and after washing. The value is the average of three replicates. Higher values ​​indicate better performance.

[0341] Washing conditions:

[0342]

[0343] Manufacturers: Center for Testmaterials BV, NL-3130 AC Vlaardingen; Swissatest Testmaterialien AG, Mövenstraße 12, CH-9015 St. Gallen

[0344] Test Results

[0345] Amylase (HTS-F16-EMPA 161) ΔE value

[0346]

[0347] ΔE value of protease (HTS-F16-CFT-PC 05)

[0348]

[0349] ΔE value of protease (HTS-F16-CFT-CS 38)

[0350]

[0351] The measurement error is + / - 0.5 ΔE units. Therefore, any value > 0.5 (ΔΔE) means that the EDDS (in the context of the test composition) exhibits a directional and significant contribution to the overall stability of the corresponding detergent formulation.

[0352] B) Application test in a Launder-O-meter for color fastness to washing; larger scale

[0353] The washing performance of the preparation is determined as follows.

[0354] Prior to washing with MACH 5 from CFT / Color Consult, the L*, a*, and b* values ​​of individual stains on a multi-stain monitor (eight different protease-associated stains) were measured. The fabric was then washed in a detergent formulation at 30°C with a cotton ballast fabric and 20 steel balls. After washing, the fabric was rinsed, tumble-dried, and air-dried.

[0355] After drying, washing performance for a single stain was determined by measuring L*, a*, and b* values ​​using a MACH 5 from CFT / Color Consultant. The dE value was calculated from the individual values ​​before and after washing. All eight stains from the monitored object were summed. Higher values ​​indicate better performance.

[0356] Washing conditions:

[0357]

[0358] Manufacturers: Test Materials Center BV, NL-3130 AC Fraltoningen; Test Materials GmbH, Switzerland, 12 Seagull Street, 9015 St. Gallen

[0359] Test Results

[0360] Protease (LOM - F16 - Multi-fouling Monitor) ΔE value

[0361]

[0362] The measurement error is + / - 2 ΔE units. Therefore, any value > 2 (total ΔE) indicates that the EDDS (in the context of the test composition) exhibits a directional and significant contribution to the overall stability of the corresponding detergent formulation. Any value > 4 (total ΔE) indicates that the EDDS (in the context of the test composition) exhibits even a significant contribution to the overall stability of the enzyme used.

Claims

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 in an amount ranging from 0.000001% to 5% by weight of the composition, wherein the at least one enzyme is selected from the group consisting of amylases and proteases; (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, wherein the cleaning composition has a viscosity ranging from 20 to 10000 mPa*s and a pH value ranging between 4 and 14, measured according to the description with the relevant methods.

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

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

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

5. The liquid cleansing composition according to claim 4(b), wherein, The cleaning composition further comprises a protease stabilizing system comprising a peptide aldehyde.

6. The liquid cleansing composition according to any one of claims 1 to 5, wherein, The at least one anionic surfactant (a) is present in an amount ranging from 2% to 40%, preferably 3% to 30%, most preferably 4% to 25% by weight of the composition; and / or (b) is selected from the group consisting of linear alkyl benzene sulfonates (LAS), alkyl sulfates (AS), alkyl alkoxy sulfates (AES), alkyl alkoxy carboxylates, modified alkyl benzene sulfonates (MLAS), methyl ester sulfonates (MES), alkyl sulfosuccinates and alpha-olefin sulfonates (AOS).

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

8. The liquid cleansing composition according to any one of claims 1 to 7, wherein, The viscosity ranges from 30 to 3000 mPa*s, preferably 40 to 2500 mPa*s and most preferably 50 to 2000 mPa*s.

9. The liquid cleansing composition according to any one of claims 1 to 8, wherein, The pH value ranges from 5 to 12, preferably 6 to 10 and most preferably 7 to 9.

10. The liquid cleansing composition according to any one of claims 1 to 9, wherein, The cleaning composition is a detergent composition.

11. The liquid cleansing composition according to any one of claims 1 to 10, wherein, The cleaning composition further comprises at least one element of the group consisting of non-anionic surfactants, amphoteric surfactants, co-builders, alcohols, biocides, thickeners, water soluble polymers, clay soil removal / anti-redeposition agents, polymeric soil release agents, bleaching agents, bleach activators, whitening agents, malodor control agents, pigments, dyes, opacifiers, hueing agents, dye transfer inhibitors, foam inhibitors (antifoams), anti-corrosion agents, softening agents and perfumes.

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

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

14. A method of manufacturing a liquid cleaning composition, the method comprising contacting and mixing components (i) to (v) according to claim 1.

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