Patent Grant
11001787
This application is a 35 U.S.C. 371 national application of international application no. PCT/EP2017/064673 filed Jun. 15, 2017, which claims priority or the benefit under 35 U.S.C. 119 of European application no. 16175968.3, filed Jun. 23, 2016, the contents of which are fully incorporated herein by reference.
The present invention concerns the use of enzymes for removing soil from a surface during the rising of the surface, wherein the rinsing is following a washing cycle. The invention further concerns a rinse aid composition for rinsing the surface and a method for removing soil from the surface during a rinsing step.
This application contains a Sequence Listing in computer readable form. The computer readable form is incorporated herein by reference.
Use of enzymes in dishwashing detergents is well known in the field of both automatic dishwashing (ADW) formulas, and in hand dishwashing formulas. Typically proteases and amylases are used in commercial dishwashing detergents. These enzymes are useful for degrading protein and starch/amylose, respectively.
The present invention concerns the use of at least one enzyme and water for removing soil from a surface during rinsing of the surface, wherein the rinsing is following a washing cycle. Further is claimed a rinse aid composition comprising at least one enzyme, a non-ionic surfactant and an acid.
The invention also concerns a method for removing soil from a surface, wherein the method comprises the steps of:
(i) Exposing the surface to a wash liquor, and
(ii) Rinsing the surface with water comprising at least one enzyme;
wherein the surface is a dishware or a hard surface.
Dishware: The term dish ware is intended to mean any form of kitchen utensil, dinner set or tableware such as but not limited to pans, plates, cops, knives, forks, spoons, porcelain etc.
Dish wash: The term “dish wash” refers to all forms of washing dishes, e.g. by hand (MDW) or automatic dish wash (ADW). Washing dishes includes, but is not limited to, the cleaning of all forms of crockery such as plates, cups, glasses, bowls, all forms of cutlery such as spoons, knives, forks and serving utensils as well as ceramics, plastics, metals, china, glass and acrylics.
Dish washing composition: The term “dish washing composition” refers to compositions intended for cleaning dishware such as plates, cups, glasses, bowls, cutlery such as spoons, knives, forks, serving utensils, ceramics, plastics, metals, china, glass and acrylics in a dishwashing machine. The terms encompass any materials/compounds selected for household or industrial washing applications and the form of the product can be liquid, powder or granulate. In addition enzymes, the automatic dishwashing composition contains detergent components such as polymers, bleaching systems, bleach activators, bleach catalysts, silicates, dyestuff and metal care agents. The dishwashing composition can be use in manual dishwashing (MDW) or automatic dishwashing (ADW).
Hard surface cleaning: The term “Hard surface cleaning” is defined herein as cleaning of hard surfaces wherein hard surfaces may include floors, tables, walls, roofs etc. as well as surfaces of hard objects such as cars (car wash) and dishes (dish wash). Dish washing includes but are not limited to cleaning of plates, cups, glasses, bowls, cutlery such as spoons, knives, forks, serving utensils, ceramics, plastics, metals, china, glass and acrylics.
Sequence identity: The relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter “sequence identity”.
For purposes of the present invention, the sequence identity between two amino acid sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277), preferably version 5.0.0 or later. The parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. The output of Needle labeled “longest identity” (obtained using the −nobrief option) is used as the percent identity and is calculated as follows:
(Identical Residues×100)/(Length of Alignment−Total Number of Gaps in Alignment)
For purposes of the present invention, the sequence identity between two deoxyribonucleotide sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, supra) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, supra), preferably version 5.0.0 or later. The parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EDNAFULL (EMBOSS version of NCBI NUC4.4) substitution matrix. The output of Needle labeled “longest identity” (obtained using the −nobrief option) is used as the percent identity and is calculated as follows:
(Identical Deoxyribonucleotides×100)/(Length of Alignment−Total Number of Gaps in Alignment)
Variant: The term “variant” means a polypeptide having enzyme activity comprising an alteration, i.e., a substitution, insertion, and/or deletion, at one or more (e.g., several) positions. A substitution means replacement of the amino acid occupying a position with a different amino acid; a deletion means removal of the amino acid occupying a position; and an insertion means adding an amino acid adjacent to and immediately following the amino acid occupying a position.
Wash cycle: The term “wash cycle” is defined herein as a washing operation wherein dishware are exposed to the wash liquor for a period of time by circulating the wash liquor and spraying the wash liquor onto the dishware in order to clean the dishware and finally the superfluous wash liquor is removed. A wash cycle may be repeated one, two, three, four, five or even six times at the same or at different temperatures. Hereafter the dishware is generally rinsed and dried. One of the wash cycles can be a soaking step, where the dishware is left soaking in the wash liquor for a period.
Rinse cycle: The term “rinse cycle” is defined herein a step carried out after the wash cycle, and where the dishware is rinsed with water or water comprising a rinse aid for a period of time. A rinse cycle may be repeated one or two times at the same or at different temperatures.
Rinse aid:
Wash liquor: The term “wash liquor” is intended to mean the solution or mixture of water and detergents optionally including enzymes used for dishwashing.
The invention concerns use of at least one enzyme and water for removing soil from a surface during rinsing of the surface, wherein the rinsing is following a washing cycle. The invention further concerns a rinse aid composition comprising at least one enzyme, a non-ionic surfactant and an acid. The composition can be granular or liquid. The liquid rinse aid composition can have a pH in the range of 1-7 such as in the in the range of 2-6 or in the range of 2-4 or in the range of 2.5-3.5. The rinse aid can be used for facilitating the rinsing the surface. Also is claimed a method for removing soil from a surface, wherein the method comprises the steps of:
(i) Exposing the surface to a wash liquor, and
(ii) Rinsing the hard surface with water comprising at least one enzyme;
wherein the surface is a dishware or a hard surface.
In one embodiment the wash liquor is removed before step (ii). The rinsing step (ii) can comprise more than one rinsing step such as two or three rinsing steps. If there is more than one rinsing step the at least one enzyme is comprised in the water of at least one of the rinsing steps. The rinse aid composition of the invention can be used in the method.
In one embodiment the invention the surface is a dish ware or a hard surface present in a dishwashing machine. The hard surface is present in the interior of a dishwashing machine such as walls, baskets, nozzles, pumps, sump, filters, pipelines, drains, and outlets.
The enzymes can be used in a process for automatic dish washing.
Use of enzymes for washing surfaces are commonly know. For example in dishwashing applications, enzymes can be used in the washing cycle in order to facilitate the removal of soil from the surface of the dishware and the interior of the dishwashing machine. The inventors have surpassingly found that by using enzymes during the rinsing step of a washing process the removal of soil is improved and for some enzymes even better than when the enzymes are used during the washing cycle.
Removal of soil from dishware is off course of importance as the consumer would like clean dishware. However cleaning of the interior of the dishwashing machine is also important because soil left in the dishwashing machine may cause malodor. Especially soil remained and accumulated in the filter, drain and sump can give rise to malodor. The use of enzymes in the rinsing step can reduce this problem as the enzymes are more likely to be present in the drain and sump after wash than the enzymes used during the wash cycle.
One way of measuring the removal of soil is by Assay I or Assay II as described herein. The inventors have found that the present invention reduces the soil by at least 70% when measured with Assay I or has a score above 7 when measured with Assay II. In one embodiment of the invention the soil is reduced by at least 75%, at least 80%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% when measured with Assay I. In one embodiment of the invention the score is above 7.5, above 8.0, above 8.5, above 9.0 or even above 9.5 when measured with Assay II.
According to the invention at least one enzymes is used during the rinsing of the surface. The enzyme can be selected from the group consisting of hemicellulases, peroxidases, proteases, cellulases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, mannanases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, R-glucanases, arabinosidases, hyaluronidase, chondroitinase, laccase, DNase chlorophyllases, amylases, perhydrolases, peroxidases, xanthanase and mixtures thereof.
The invention also concerns a rinse aid composition comprising at least one enzyme, a non-ionic surfactant and an acid. The rinse aid composition can be, wherein the composition has a pH in the range of 1-7. The composition can be a rinse aid. Rinse aids are commonly known to be used in automatic dishwashing (ADW) processes. The rinse aids are automatically dosed by the dishwashing machine and it helps remove water from the dishware and makes the dishware bright and shining.
In one embodiment of the invention the rinse aid composition comprises a non-ionic surfactant in an amount below 15% (w/w). In one embodiment the composition comprises a non-ionic surfactant in the range of 5-15%, in the range of 8-15%, in the range of 10-15%, in the range of 5-10% or in the range of 5-8% (all percentages are w/w %).
The non-ionic surfactant can be alcohol alkoxylates and/or biobased surfactants.
The alcohol alkoxylates are selected from the group consisting of epoxy-capped poly(oxyalkylated) alcohols and alcohol ethoxylates with linear radicals formed from alcohols of native origin having 12 to 18 carbon atoms. the alcohol alkoxylates can be alkoxylated primary alcohols having preferably 8 to 18 carbon atoms and an average of 1 to 20, preferably 1 to 12, mol of ethylene oxide (E0) per mole of alcohol, in which the alcohol radical may be linear or preferably 2-methyl-branched, or may comprise linear and methyl-branched radicals in a mixture. The alcohol alkoxylates are described in further details below.
The composition may further comprise a preservative and/or biocide. The preservative and/or biocide is selected from metholisothiazolinone or methylchlorisothiazolinone or a combination of metholisothiazolinone and methylchlorisothiazolinone. Metholisothiazolinone and methylchlorisothiazolinone have preserving effect and biocidal effect.
The compositions herein may additionally include an acid. Any suitable organic and/or inorganic acid in any suitable amount may be used in the rinse aid compositions and/or products. Some suitable acids include, but are not limited to acids selected from the group consisting of acetic acid, aspartic acid, benzoic acid, boric acid, bromic acid, citric acid, formic acid, gluconic acid, glutamic acid, lactic acid, malic acid, nitric acid, sulfamic acid, sulfuric acid, tartaric acid, and mixtures thereof.
In the case of a liquid rinse aid composition, adding an acid to the rinse aid composition enables water-soluble metal salts to at least partially dissolve in the composition. The acid also helps to at least partially reduce the precipitation on hard surfaces during the rinse cycle. The acid may also stabilize the liquid rinse aid composition against precipitation in the product prior to use. In the case of a solid rinse aid composition, adding an acid to the rinse aid composition enables water-soluble metal salts, once released, to at least partially dissolve quickly in the wash and/or rinse liquor of an automatic dishwashing appliance so as to prevent insoluble material from forming and/or from depositing onto hard surfaces, such as on flatware, glasses, dishes and/or components inside the automatic dishwashing appliance itself. In one embodiment of the invention the composition can further comprise a glass care ingredient such as zinc acetate, zinc chloride and bismuth.
In one embodiment the composition can comprise 75-80% water, 5-15% non-ionic surfactant, sodium- or potassium cumentesulfonate, citric acid, zinc acetate, metholisothiazolinone and methylchlorisothiazolinone and an amylase.
In one embodiment the composition can comprise 75-80% water, 5-15% non-ionic surfactant, sodium- or potassium cumentesulfonate, citric acid, zinc acetate, metholisothiazolinone and methylchlorisothiazolinone and an amylase and a protease.
The composition of the invention does not comprise bleaching agents.
In one embodiment of the invention the enzyme is an amylase, which amylase is an alpha-amylase or a glucoamylase.
In one embodiment the amylase has at least 80% sequence identity to SEQ ID NO: 1, such as at least 85% sequence identity to SEQ ID NO: 1, at least 90% sequence identity to SEQ ID NO: 1, at least 95% sequence identity to SEQ ID NO: 1, at least 96% sequence identity to SEQ ID NO: 1, at least 97% sequence identity to SEQ ID NO: 1, at least 98% sequence identity to SEQ ID NO: 1 or at least 99% sequence identity to SEQ ID NO: 1.
In one embodiment the amylase has at least 80% sequence identity to SEQ ID NO: 2, such as at least 85% sequence identity to SEQ ID NO: 2, at least 90% sequence identity to SEQ ID NO: 2, at least 95% sequence identity to SEQ ID NO: 2, at least 96% sequence identity to SEQ ID NO: 2, at least 97% sequence identity to SEQ ID NO: 2, at least 98% sequence identity to SEQ ID NO: 2 or at least 99% sequence identity to SEQ ID NO: 2.
In one embodiment of the invention the enzyme is a protease, which protease is a serine protease or a metalloprotease, preferably an alkaline microbial protease or a trypsin-like protease.
In one embodiment of the invention the protease has at least 80% sequence identity to SEQ ID NO: 3, such as at least 85% sequence identity to SEQ ID NO: 3, at least 90% sequence identity to SEQ ID NO: 3, at least 95% sequence identity to SEQ ID NO: 3, at least 96% sequence identity to SEQ ID NO: 3, at least 97% sequence identity to SEQ ID NO: 3, at least 98% sequence identity to SEQ ID NO: 3 or at least 99% sequence identity to SEQ ID NO: 3.
In one embodiment of the invention the protease has at least 80% sequence identity to SEQ ID NO: 4, such as at least 85% sequence identity to SEQ ID NO: 4, at least 90% sequence identity to SEQ ID NO: 4, at least 95% sequence identity to SEQ ID NO: 4, at least 96% sequence identity to SEQ ID NO: 4, at least 97% sequence identity to SEQ ID NO: 4, at least 98% sequence identity to SEQ ID NO: 4 or at least 99% sequence identity to SEQ ID NO: 4.
In one embodiment the amylase has at least 80% sequence identity to SEQ ID NO: 5, such as at least 85% sequence identity to SEQ ID NO: 5, at least 90% sequence identity to SEQ ID NO: 5, at least 95% sequence identity to SEQ ID NO: 5, at least 96% sequence identity to SEQ ID NO: 5, at least 97% sequence identity to SEQ ID NO: 5, at least 98% sequence identity to SEQ ID NO: 5 or at least 99% sequence identity to SEQ ID NO: 5.
In one embodiment of the invention one or more enzymes are used in addition to the at least one enzyme used in the rinsing of a surface. The one or more enzymes can be selected from the group consisting of hemicellulases, peroxidases, proteases, cellulases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, mannanases, pectate lyases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, R-glucanases, arabinosidases, hyaluronidase, chondroitinase, laccase, DNase chlorophyllases, amylases, perhydrolases, peroxidases, xanthanase and mixtures thereof. The enzymes are described in further details below.
In one embodiment of the invention amylase and protease are used when rinsing the surface e.g. by being comprised in the same rinse aid composition. In one embodiment the amylase amylase has at least 80% sequence identity to SEQ ID NO: 1 and is used together with a protease having at least 80% sequence identity to SEQ ID NO: 3. In one embodiment the amylase amylase has at least 80% sequence identity to SEQ ID NO: 1 and is used together with a protease having at least 80% sequence identity to SEQ ID NO: 4. In one embodiment the amylase amylase has at least 80% sequence identity to SEQ ID NO: 1 and is used together with a protease having at least 80% sequence identity to SEQ ID NO: 5. In one embodiment the amylase amylase has at least 80% sequence identity to SEQ ID NO: 2 and is used together with a protease having at least 80% sequence identity to SEQ ID NO: 3. In one embodiment the amylase amylase has at least 80% sequence identity to SEQ ID NO: 2 and is used together with a protease having at least 80% sequence identity to SEQ ID NO: 4. In one embodiment the amylase amylase has at least 80% sequence identity to SEQ ID NO: 2 and is used together with a protease having at least 80% sequence identity to SEQ ID NO: 5.
In one embodiment of the invention amylase and protease are used when rinsing the surface e.g. by being comprised in the same rinse aid composition. In one embodiment the amylase amylase has at least 85% sequence identity to SEQ ID NO: 1 and is used together with a protease having at least 85% sequence identity to SEQ ID NO: 3. In one embodiment the amylase amylase has at least 85% sequence identity to SEQ ID NO: 1 and is used together with a protease having at least 85% sequence identity to SEQ ID NO: 4. In one embodiment the amylase amylase has at least 85% sequence identity to SEQ ID NO: 1 and is used together with a protease having at least 85% sequence identity to SEQ ID NO: 5. In one embodiment the amylase amylase has at least 85% sequence identity to SEQ ID NO: 2 and is used together with a protease having at least 80% sequence identity to SEQ ID NO: 3. In one embodiment the amylase amylase has at least 85% sequence identity to SEQ ID NO: 2 and is used together with a protease having at least 85% sequence identity to SEQ ID NO: 4. In one embodiment the amylase amylase has at least 85% sequence identity to SEQ ID NO: 2 and is used together with a protease having at least 85% sequence identity to SEQ ID NO: 5.
In one embodiment of the invention amylase and protease are used when rinsing the surface e.g. by being comprised in the same rinse aid composition. In one embodiment the amylase amylase has at least 90% sequence identity to SEQ ID NO: 1 and is used together with a protease having at least 90% sequence identity to SEQ ID NO: 3. In one embodiment the amylase amylase has at least 90% sequence identity to SEQ ID NO: 1 and is used together with a protease having at least 90% sequence identity to SEQ ID NO: 4. In one embodiment the amylase amylase has at least 90% sequence identity to SEQ ID NO: 1 and is used together with a protease having at least 90% sequence identity to SEQ ID NO: 5. In one embodiment the amylase amylase has at least 90% sequence identity to SEQ ID NO: 2 and is used together with a protease having at least 90% sequence identity to SEQ ID NO: 3. In one embodiment the amylase amylase has at least 90% sequence identity to SEQ ID NO: 2 and is used together with a protease having at least 90% sequence identity to SEQ ID NO: 4. In one embodiment the amylase amylase has at least 90% sequence identity to SEQ ID NO: 2 and is used together with a protease having at least 90% sequence identity to SEQ ID NO: 5.
In one embodiment of the invention amylase and protease are used when rinsing the surface e.g. by being comprised in the same rinse aid composition. In one embodiment the amylase amylase has at least 95% sequence identity to SEQ ID NO: 1 and is used together with a protease having at least 95% sequence identity to SEQ ID NO: 3. In one embodiment the amylase amylase has at least 95% sequence identity to SEQ ID NO: 1 and is used together with a protease having at least 95% sequence identity to SEQ ID NO: 4. In one embodiment the amylase amylase has at least 95% sequence identity to SEQ ID NO: 1 and is used together with a protease having at least 95% sequence identity to SEQ ID NO: 5. In one embodiment the amylase amylase has at least 95% sequence identity to SEQ ID NO: 2 and is used together with a protease having at least 95% sequence identity to SEQ ID NO: 3. In one embodiment the amylase amylase has at least 95% sequence identity to SEQ ID NO: 2 and is used together with a protease having at least 95% sequence identity to SEQ ID NO: 4. In one embodiment the amylase amylase has at least 95% sequence identity to SEQ ID NO: 2 and is used together with a protease having at least 95% sequence identity to SEQ ID NO: 5.
In one embodiment of the invention amylase and protease are used when rinsing the surface e.g. by being comprised in the same rinse aid composition. In one embodiment the amylase amylase has at least 99% sequence identity to SEQ ID NO: 1 and is used together with a protease having at least 99% sequence identity to SEQ ID NO: 3. In one embodiment the amylase amylase has at least 99% sequence identity to SEQ ID NO: 1 and is used together with a protease having at least 99% sequence identity to SEQ ID NO: 4. In one embodiment the amylase amylase has at least 99% sequence identity to SEQ ID NO: 1 and is used together with a protease having at least 99% sequence identity to SEQ ID NO: 5. In one embodiment the amylase amylase has at least 99% sequence identity to SEQ ID NO: 2 and is used together with a protease having at least 99% sequence identity to SEQ ID NO: 3. In one embodiment the amylase amylase has at least 99% sequence identity to SEQ ID NO: 2 and is used together with a protease having at least 99% sequence identity to SEQ ID NO: 4. In one embodiment the amylase amylase has at least 99% sequence identity to SEQ ID NO: 2 and is used together with a protease having at least 99% sequence identity to SEQ ID NO: 5.
Suitable amylases which can be used in the rinse aid composition of the invention may be an alpha-amylase or a glucoamylase and may be of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, e.g., a special strain of Bacillus licheniformis, described in more detail in GB 1,296,839.
Suitable amylases include amylases having SEQ ID NO: 2 in WO 95/10603 or variants having 90% sequence identity to SEQ ID NO: 3 thereof. Preferred variants are described in WO 94/02597, WO 94/18314, WO 97/43424 and SEQ ID NO: 4 of WO 99/019467, such as variants with substitutions in one or more of 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.
Different suitable amylases include amylases having SEQ ID NO: 6 in WO 02/010355 or variants thereof having 90% sequence identity to SEQ ID NO: 6. Preferred variants of SEQ ID NO: 6 are those having a deletion in positions 181 and 182 and a substitution in position 193.
Other amylases which are suitable are hybrid alpha-amylase comprising residues 1-33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006/066594 and residues 36-483 of the B. licheniformis alpha-amylase shown in SEQ ID NO: 4 of WO 2006/066594 or variants having 90% sequence identity thereof. Preferred variants of this hybrid alpha-amylase are those having a substitution, a deletion or an insertion in one of more of the following positions: G48, T49, G107, H156, A181, N190, M197, I201, A209 and Q264. Most preferred variants of the hybrid alpha-amylase comprising residues 1-33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006/066594 and residues 36-483 of SEQ ID NO: 4 are those having the substitutions: M197T; H156Y+A181T+N190F+A209V+Q264S; or G48A+T49I+G107A+H156Y+A181T+N190F+1201F+A209V+Q264S.
Further amylases which are suitable are amylases having SEQ ID NO: 6 in WO 99/019467 or variants thereof having 90% sequence identity to SEQ ID NO: 6. Preferred variants of SEQ ID NO: 6 are those having a substitution, a deletion or an insertion in one or more of the following positions: R181, G182, H183, G184, N195, I206, E212, E216 and K269. Particularly preferred amylases are those having deletion in positions R181 and G182, or positions H183 and G184.
Additional amylases which can be used are those having SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 2 or SEQ ID NO: 7 of WO 96/023873 or variants thereof having 90% sequence identity to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7. Preferred variants of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or SEQ ID NO: 7 are those having a substitution, a deletion or an insertion in one or more of the following positions: 140, 181, 182, 183, 184, 195, 206, 212, 243, 260, 269, 304 and 476, using SEQ ID 2 of WO 96/023873 for numbering. More preferred variants are those having a deletion in two positions selected from 181, 182, 183 and 184, such as 181 and 182, 182 and 183, or positions 183 and 184. Most preferred amylase variants of SEQ ID NO: 1, SEQ ID NO: 2 or SEQ ID NO: 7 are those having a deletion in positions 183 and 184 and a substitution in one or more of positions 140, 195, 206, 243, 260, 304 and 476.
Other amylases which can be used are amylases having SEQ ID NO: 2 of WO 08/153815, SEQ ID NO: 10 in WO 01/66712 or variants thereof having 90% sequence identity to SEQ ID NO: 2 of WO 08/153815 or 90% sequence identity to SEQ ID NO: 10 in WO 01/66712. Preferred variants of SEQ ID NO: 10 in WO 01/66712 are those having a substitution, a deletion or an insertion in one of more of the following positions: 176, 177, 178, 179, 190, 201, 207, 211 and 264.
Further suitable amylases are amylases having SEQ ID NO: 2 of WO 09/061380 or variants having 90% sequence identity to SEQ ID NO: 2 thereof. Preferred variants of SEQ ID NO: 2 are those having a truncation of the C-terminus and/or a substitution, a deletion or an insertion in one of more of the following positions: Q87, Q98, S125, N128, T131, T165, K178, R180, S181, T182, G183, M201, F202, N225, S243, N272, N282, Y305, R309, D319, Q320, Q359, K444 and G475. More preferred variants of SEQ ID NO: 2 are those having the substitution in one of more of the following positions: Q87E,R, Q98R, S125A, N128C, T131I, T165I, K178L, T182G, M201L, F202Y, N225E,R, N272E,R, S243Q,A,E,D, Y305R, R309A, Q320R, Q359E, K444E and G475K and/or deletion in position R180 and/or S181 or of T182 and/or G183. Most preferred amylase variants of SEQ ID NO: 2 are those having the substitutions:
N128C+K178L+T182G+Y305R+G475K;
N128C+K178L+T182G+F202Y+Y305R+D319T+G475K;
S125A+N128C+K178L+T182G+Y305R+G475K; or
S125A+N128C+T131I+T165I+K178L+T182G+Y305R+G475K wherein the variants are C-terminally truncated and optionally further comprises a substitution at position 243 and/or a deletion at position 180 and/or position 181.
Further suitable amylases are amylases having SEQ ID NO: 1 of WO13184577 or variants having 90% sequence identity to SEQ ID NO: 1 thereof. Preferred variants of SEQ ID NO: 1 are those having a substitution, a deletion or an insertion in one of more of the following positions: K176, R178, G179, T180, G181, E187, N192, M199, I203, S241, R458, T459, D460, G476 and G477. More preferred variants of SEQ ID NO: 1 are those having the substitution in one of more of the following positions: K176L, E187P, N192FYH, M199L, 1203YF, S241QADN, R458N, T459S, D460T, G476K and G477K and/or deletion in position R178 and/or S179 or of T180 and/or G181. Most preferred amylase variants of SEQ ID NO: 1 are those having the substitutions:
E187P+1203Y+G476K
E187P+1203Y+R458N+T459S+D460T+G476K
wherein the variants optionally further comprises a substitution at position 241 and/or a deletion at position 178 and/or position 179.
Further suitable amylases are amylases having SEQ ID NO: 1 of WO10104675 or variants having 90% sequence identity to SEQ ID NO: 1 thereof. Preferred variants of SEQ ID NO: 1 are those having a substitution, a deletion or an insertion in one of more of the following positions: N21, D97, V128I K177, R179, S180, I181, G182, M200, L204, E242, G477 and G478. More preferred variants of SEQ ID NO: 1 are those having the substitution in one of more of the following positions: N21D, D97N, V128I K177L, M200L, L204YF, E242QA, G477K and G478K and/or deletion in position R179 and/or S180 or of I181 and/or G182. Most preferred amylase variants of SEQ ID NO: 1 are those having the substitutions:
N21D+D97N+V128I
wherein the variants optionally further comprises a substitution at position 200 and/or a deletion at position 180 and/or position 181.
Other suitable amylases are the alpha-amylase having SEQ ID NO: 12 in WO01/66712 or a variant having at least 90% sequence identity to SEQ ID NO: 12. Preferred amylase variants are those having a substitution, a deletion or an insertion in one of more of the following positions of SEQ ID NO: 12 in WO01/66712: R28, R118, N174; R181, G182, D183, G184, G186, W189, N195, M202, Y298, N299, K302, S303, N306, R310, N314; R320, H324, E345, Y396, R400, W439, R444, N445, K446, Q449, R458, N471, N484. Particular preferred amylases include variants having a deletion of D183 and G184 and having the substitutions R118K, N195F, R320K and R458K, and a variant additionally having substitutions in one or more position selected from the group: M9, G149, G182, G186, M202, T257, Y295, N299, M323, E345 and A339, most preferred a variant that additionally has substitutions in all these positions.
Other examples are amylase variants such as those described in WO2011/098531, WO2013/001078 and WO2013/001087.
Commercially available amylases are Duramyl™, Termamyl™, Fungamyl™, Stainzyme™, Stainzyme Plus™, Natalase™, Liquozyme X and BAN™ (from Novozymes NS), and Rapidase™, Purastar™/Effectenz™, Powerase, Preferenz S1000, Preferenz S100 and Preferenz S110 (from Genencor International Inc./DuPont).
Suitable proteases include those of bacterial, fungal, plant, viral or animal origin e.g. vegetable or microbial origin. Microbial origin is preferred. Chemically modified or protein engineered mutants are included. It may be an alkaline protease, such as a serine protease or a metalloprotease. A serine protease may for example be of the 51 family, such as trypsin, or the S8 family such as subtilisin. A metalloproteases protease may for example be a thermolysin from e.g. family M4 or other metalloprotease such as those from M5, M7 or M8 families.
The term “subtilases” refers to a sub-group of serine protease according to Siezen et al., Protein Engng. 4 (1991) 719-737 and Siezen et al. Protein Science 6 (1997) 501-523. Serine proteases are a subgroup of proteases characterized by having a serine in the active site, which forms a covalent adduct with the substrate. The subtilases may be divided into 6 sub-divisions, i.e. the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family and the Pyrolysin family.
Examples of subtilases are those derived from Bacillus such as Bacillus lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in; U.S. Pat. No. 7,262,042 and WO09/021867, and subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN′, subtilisin 309, subtilisin 147 and subtilisin 168 described in WO89/06279 and protease PD138 described in (WO93/18140). Other useful proteases may be those described in WO92/175177, WO01/016285, WO02/026024 and WO02/016547. Examples of trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO89/06270, WO94/25583 and WO05/040372, and the chymotrypsin proteases derived from Cellumonas described in WO05/052161 and WO05/052146.
A further preferred protease is the alkaline protease from Bacillus lentus DSM 5483, as described for example in WO95/23221, and variants thereof which are described in WO92/21760, WO95/23221, EP1921147 and EP1921148.
Examples of metalloproteases are the neutral metalloprotease as described in WO07/044993 (Genencor Int.) such as those derived from Bacillus amyloliquefaciens.
Examples of useful proteases are the variants described in: WO92/19729, WO96/034946, WO98/20115, WO98/20116, WO99/011768, WO01/44452, WO03/006602, WO04/03186, WO04/041979, WO07/006305, WO11/036263, WO11/036264, especially the variants with substitutions in one or more of the following positions: 3, 4, 9, 15, 24, 27, 42, 55, 59, 60, 66, 74, 85, 96, 97, 98, 99, 100, 101, 102, 104, 116, 118, 121, 126, 127, 128, 154, 156, 157, 158, 161, 164, 176, 179, 182, 185, 188, 189, 193, 198, 199, 200, 203, 206, 211, 212, 216, 218, 226, 229, 230, 239, 246, 255, 256, 268 and 269 wherein the positions correspond to the positions of the Bacillus Lentus protease shown in SEQ ID NO 1 of WO 2016/001449. More preferred the subtilase variants may comprise the mutations: S3T, V41, S9R, S9E, A15T, S24G, S24R, K27R, N42R, S55P, G59E, G59D, N60D, N60E, V66A, N74D, N85S, N85R, G96S, G96A, S97G, S97D, S97A, S97SD, S99E, S99D, S99G, S99M, S99N, S99R, S99H, S101A, V1021, V102Y, V102N, S104A, G116V, G116R, H118D, H118N, N120S, S126L, P127Q, S128A, S154D, A156E, G157D, G157P, S158E, Y161A, R164S, Q176E, N179E, S182E, Q185N, A188P, G189E, V193M, N198D, V199I, Y203W, S206G, L211Q, L211D, N212D, N212S, M216S, A226V, K229L, Q230H, Q239R, N246K, N255W, N255D, N255E, L256E, L256D T268A, R269H. The protease variants are preferably variants of the Bacillus Lentus protease (Savinase®) shown in SEQ ID NO 1 of WO 2016/001449, the Bacillus amylolichenifaciens protease (BPN′) shown in SEQ ID NO 2 of WO2016/001449. The protease variants preferably have at least 80% sequence identity to SEQ ID NO 1 or SEQ ID NO 2 of WO 2016/001449.
A protease variant comprising a substitution at one or more positions corresponding to positions 171, 173, 175, 179, or 180 of SEQ ID NO: 1 of WO2004/067737, wherein said protease variant has a sequence identity of at least 75% but less than 100% to SEQ ID NO: 1 of WO2004/067737.
Suitable commercially available protease enzymes include those sold under the trade names Alcalase®, Duralase™, Durazym™, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Primase®, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Coronase® Ultra, Blaze®, Blaze Evity® 100T, Blaze Evity® 125T, Blaze Evity® 150T, Neutrase®, Everlase® and Esperase® (Novozymes NS), those sold under the tradename Maxatase®, Maxacal®, Maxapem®, Purafect Ox®, Purafect OxP®, Puramax®, FN2®, FN3®, FN4®, Excellase®, Excellenz P1000™, Excellenz P1250™, Eraser®, Preferenz P100™, Purafect Prime®, Preferenz P110™, Effectenz P1000™, Purafect®™, Effectenz P1050™, Purafect Ox®™, Effectenz P2000™, Purafast®, Properase®, Opticlean® and Optimase® (Danisco/DuPont), Axapem™ (Gist-Brocases N.V.), BLAP (sequence shown in FIG. 29 of U.S. Pat. No. 5,352,604) and variants hereof (Henkel AG) and KAP (Bacillus alkalophilus subtilisin) from Kao.
Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, e.g., the fungal cellulases produced from Humicola insolens, Myceliophthora thermophila and Fusarium oxysporum disclosed in U.S. Pat. Nos. 4,435,307, 5,648,263, 5,691,178, 5,776,757 and WO 89/09259.
Especially suitable cellulases are the alkaline or neutral cellulases having colour care benefits. Examples of such cellulases are cellulases described in EP 0 495 257, EP 0 531 372, WO 96/11262, WO 96/29397, WO 98/08940. Other examples are cellulase variants such as those described in WO 94/07998, EP 0 531 315, U.S. Pat. Nos. 5,457,046, 5,686,593, 5,763,254, WO 95/24471, WO 98/12307 and WO99/001544.
Other cellulases are endo-beta-1,4-glucanase enzyme having a sequence of at least 97% identity to the amino acid sequence of position 1 to position 773 of SEQ ID NO:2 of WO 2002/099091 or a family 44 xyloglucanase, which a xyloglucanase enzyme having a sequence of at least 60% identity to positions 40-559 of SEQ ID NO: 2 of WO 2001/062903.
Commercially available cellulases include Celluzyme™, and Carezyme™ (Novozymes NS) Carezyme Premium™ (Novozymes NS), Celluclean™ (Novozymes NS), Celluclean Classic™ (Novozymes NS), Cellusoft™ (Novozymes NS), Whitezyme™ (Novozymes NS), Clazinase™, and Puradax HA™ (Genencor International Inc.), and KAC-500(B)™ (Kao Corporation).
Suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included. The mannanase may be an alkaline mannanase of Family 5 or 26. It may be a wild-type from Bacillus or Humicola, particularly B. agaradhaerens, B. licheniformis, B. halodurans, B. clausii, or H. insolens. Suitable mannanases are described in WO 1999/064619. A commercially available mannanase is Mannaway (Novozymes NS).
Suitable peroxidases/oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus, e.g., from C. cinereus, and variants thereof as those described in WO 93/24618, WO 95/10602, and WO 98/15257. Commercially available peroxidases include Guardzyme™ (Novozymes NS).
Suitable lipases and cutinases include those of bacterial or fungal origin. Chemically modified or protein engineered mutant enzymes are included. Examples include lipase from Thermomyces, e.g. from T. lanuginosus (previously named Humicola lanuginosa) as described in EP258068 and EP305216, cutinase from Humicola, e.g. H. insolens (WO96/13580), lipase from strains of Pseudomonas (some of these now renamed to Burkholderia), e.g. P. alcaligenes or P. pseudoalcaligenes (EP218272), P. cepacia (EP331376), P. sp. strain SD705 (WO95/06720 & WO96/27002), P. wisconsinensis (WO96/12012), GDSL-type Streptomyces lipases (WO10/065455), cutinase from Magnaporthe grisea (WO10/107560), cutinase from Pseudomonas mendocina (U.S. Pat. No. 5,389,536), lipase from Thermobifida fusca (WO11/084412), Geobacillus stearothermophilus lipase (WO11/084417), lipase from Bacillus subtilis (WO11/084599), and lipase from Streptomyces griseus (WO11/150157) and S. pristinaespiralis (WO12/137147).
Other examples are lipase variants such as those described in EP407225, WO92/05249, WO94/01541, WO94/25578, WO95/14783, WO95/30744, WO95/35381, WO95/22615, WO96/00292, WO97/04079, WO97/07202, WO00/34450, WO00/60063, WO01/92502, WO07/87508 and WO09/109500.
Preferred commercial lipase products include include Lipolase™, Lipex™; Lipolex™ and Lipoclean™ (Novozymes NS), Lumafast (originally from Genencor) and Lipomax (originally from Gist-Brocades).
Still other examples are lipases sometimes referred to as acyltransferases or perhydrolases, e.g. acyltransferases with homology to Candida antarctica lipase A (WO10/111143), acyltransferase from Mycobacterium smegmatis (WO05/56782), perhydrolases from the CE 7 family (WO09/67279), and variants of the M. smegmatis perhydrolase in particular the S54V variant used in the commercial product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd (WO10/100028).
A peroxidase according to the invention is a peroxidase enzyme comprised by the enzyme classification EC 1.11.1.7, as set out by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB), or any fragment derived therefrom, exhibiting peroxidase activity.
Suitable peroxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinopsis, e.g., from C. cinerea (EP 179,486), and variants thereof as those described in WO 93/24618, WO 95/10602, and WO 98/15257.
A peroxidase according to the invention also include a haloperoxidase enzyme, such as chloroperoxidase, bromoperoxidase and compounds exhibiting chloroperoxidase or bromoperoxidase activity. Haloperoxidases are classified according to their specificity for halide ions. Chloroperoxidases (E.C. 1.11.1.10) catalyze formation of hypochlorite from chloride ions.
In an embodiment, the haloperoxidase of the invention is a chloroperoxidase. Preferably, the haloperoxidase is a vanadium haloperoxidase, i.e., a vanadate-containing haloperoxidase. In a preferred method of the present invention the vanadate-containing haloperoxidase is combined with a source of chloride ion.
Haloperoxidases have been isolated from many different fungi, in particular from the fungus group dematiaceous hyphomycetes, such as Caldariomyces, e.g., C. fumago, Alternaria, Curvularia, e.g., C. verruculosa and C. inaequalis, Drechslera, Ulocladium and Botrytis.
Haloperoxidases have also been isolated from bacteria such as Pseudomonas, e.g., P. pyrrocinia and Streptomyces, e.g., S. aureofaciens.
In an preferred embodiment, the haloperoxidase is derivable from Curvularia sp., in particular Curvularia verruculosa or Curvularia inaequalis, such as C. inaequalis CBS 102.42 as described in WO 95/27046; or C. verruculosa CBS 147.63 or C. verruculosa CBS 444.70 as described in WO 97/04102; or from Drechslera hartlebii as described in WO 01/79459, Dendryphiella salina as described in WO 01/79458, Phaeotrichoconis crotalarie as described in WO 01/79461, or Geniculosporium sp. as described in WO 01/79460.
An oxidase according to the invention include, in particular, any laccase enzyme comprised by the enzyme classification EC 1.10.3.2, or any fragment derived therefrom exhibiting laccase activity, or a compound exhibiting a similar activity, such as a catechol oxidase (EC 1.10.3.1), an o-aminophenol oxidase (EC 1.10.3.4), or a bilirubin oxidase (EC 1.3.3.5).
Preferred laccase enzymes are enzymes of microbial origin. The enzymes may be derived from plants, bacteria or fungi (including filamentous fungi and yeasts).
Suitable examples from fungi include a laccase derivable from a strain of Aspergillus, Neurospora, e.g., N. crassa, Podospora, Botrytis, Collybia, Fomes, Lentinus, Pleurotus, Trametes, e.g., T. villosa and T. versicolor, Rhizoctonia, e.g., R. solani, Coprinopsis, e.g., C. cinerea, C. comatus, C. friesii, and C. plicatilis, Psathyrella, e.g., P. condelleana, Panaeolus, e.g., P. papilionaceus, Myceliophthora, e.g., M. thermophila, Schytalidium, e.g., S. thermophilum, Polyporus, e.g., P. pinsitus, Phlebia, e.g., P. radiata (WO 92/01046), or Coriolus, e.g., C. hirsutus (JP 2238885).
Suitable examples from bacteria include a laccase derivable from a strain of Bacillus.
A laccase derived from Coprinopsis or Myceliophthora is preferred; in particular a laccase derived from Coprinopsis cinerea, as disclosed in WO 97/08325; or from Myceliophthora thermophila, as disclosed in WO 95/33836.
Surfactants
The rinse aid composition of the invention can include at least one non-ionic surfactant. Suitable nonionic surfactants include, but are not limited to low-foaming nonionic (LFNI) surfactants. A LFNI surfactant is most typically used in an automatic dishwashing because of the improved water-sheeting action (especially from glassware) which they confer to the automatic dishwashing composition. They also may encompass non-silicone, phosphate or nonphosphate polymeric materials which are known to defoam food soils encountered in automatic dishwashing. The LFNI surfactant may have a relatively low cloud point and a high hydrophilic-lipophilic balance (HLB). Cloud points of 1% solutions in water are typically below about 32° C. and alternatively lower, e.g., 0° C., for optimum control of sudsing throughout a full range of water temperatures. If desired, a biodegradable LFNI surfactant having the above properties may be used.
A LFNI surfactant may include, but is not limited to: alkoxylated surfactants, especially ethoxylates derived from primary alcohols, and blends thereof with more sophisticated surfactants, such as the polyoxypropylene/polyoxyethylene/polyoxypropylene reverse block polymers. Suitable block polyoxyethylene-polyoxypropylene polymeric compounds that meet the requirements may include those based on ethylene glycol, propylene glycol, glycerol, trimethylolpropane and ethylenediamine, and mixtures thereof. Polymeric compounds made from a sequential ethoxylation and propoxylation of initiator compounds with a single reactive hydrogen atom, such as C12—is aliphatic alcohols, do not generally provide satisfactory suds control in Automatic dishwashing compositions. However, certain of the block polymer surfactant compounds designated as PLURONIC® and TETRONIC® by the BASF-Wyandotte Corp., Wyandotte, Mich., are suitable in Automatic dishwashing compositions.
The LFNI surfactant can optionally include a propylene oxide in an amount up to about 15% by weight. Other LFNI surfactants can be prepared by the processes described in U.S. Pat. No. 4,223,163. The LFNI surfactant may also be derived from a straight chain fatty alcohol containing from about 16 to about 20 carbon atoms (C16-C20 alcohol), alternatively a Ci8 alcohol, condensed with an average of from about 6 to about 15 moles, or from about 7 to about 12 moles, and alternatively, from about 7 to about 9 moles of ethylene oxide per mole of alcohol. The ethoxylated nonionic surfactant so derived may have a narrow ethoxylate distribution relative to the average.
In preferred embodiments, the surfactant is a non-ionic surfactant or a non-ionic surfactant system having a phase inversion temperature, as measured at a concentration of 1% in distilled water, between 40 and 70° C., preferably between 45 and 65° C. By a “non-ionic surfactant system” is meant herein a mixture of two or more non-ionic surfactants. Preferred for use herein are non-ionic surfactant systems. They seem to have improved cleaning and finishing properties and stability in product than single non-ionic surfactants. Suitable nonionic surfactants include: i) ethoxylated non-ionic surfactants prepared by the reaction of a monohydroxy alkanol or alkyphenol with 6 to 20 carbon atoms with preferably at least 12 moles particularly preferred at least 16 moles, and still more preferred at least 20 moles of ethylene oxide per mole of alcohol or alkylphenol; ii) alcohol alkoxylated surfactants having a from 6 to 20 carbon atoms and at least one ethoxy and propoxy group. Preferred for use herein are mixtures of surfactants i) and ii).
Another suitable non-ionic surfactants are epoxy-capped poly(oxyalkylated) alcohols represented by the formula:
R1O[CH2CH(CH3)O]x[CH2CH2O]y[CH2CH(OH)R2] (I)
wherein R1 is a linear or branched, aliphatic hydrocarbon radical having from 4 to 18 carbon atoms; R2 is a linear or branched aliphatic hydrocarbon radical having from 2 to 26 carbon atoms; x is an integer having an average value of from 0.5 to 1.5, more preferably about 1; and y is an integer having a value of at least 15, more preferably at least 20. Preferably, the surfactant of formula I has at least about 10 carbon atoms in the terminal epoxide unit [CH2CH(OH)R2]. Suitable surfactants of formula I are Olin Corporation's POLY-TERGENT® SLF-18B nonionic surfactants, as described, for example, in WO 94/22800, published Oct. 13, 1994 by Olin Corporation.
Preferably non-ionic surfactants and/or system herein have a Draves wetting time of less than 360 seconds, preferably less than 200 seconds, more preferably less than 100 seconds and especially less than 60 seconds as measured by the Draves wetting method (standard method ISO 8022 using the following conditions; 3-g hook, 5-g cotton skein, 0.1% by weight aqueous solution at a temperature of 25° C.). Amine oxides surfactants are also useful in the present invention as anti-redeposition surfactants include linear and branched compounds having the formula:
wherein R3 is selected from an alkyl, hydroxyalkyl, acylamidopropoyl and alkyl phenyl group, or mixtures thereof, containing from 8 to 26 carbon atoms, preferably 8 to 18 carbon atoms; R4 is an alkylene or hydroxyalkylene group containing from 2 to 3 carbon atoms, preferably 2 carbon atoms, or mixtures thereof; x is from 0 to 5, preferably from 0 to 3; and each R5 is an alkyl or hydroxyalkyl group containing from 1 to 3, preferably from 1 to 2 carbon atoms, or a polyethylene oxide group containing from 1 to 3, preferable 1, ethylene oxide groups. The R5 groups can be attached to each other, e.g., through an oxygen or nitrogen atom, to form a ring structure.
These amine oxide surfactants in particular include C10-C18 alkyl dimethyl amine oxides and C8-C18 alkoxy ethyl dihydroxyethyl amine oxides. Examples of such materials include dimethyloctylamine oxide, diethyldecylamine oxide, bis-(2-hydroxyethyl)dodecylamine oxide, dimethyldodecylamine oxide, dipropyltetradecylamine oxide, methylethylhexadecylamine oxide, dodecylamidopropyl dimethylamine oxide, cetyl dimethylamine oxide, stearyl dimethylamine oxide, tallow dimethylamine oxide and dimethyl-2-hydroxyoctadecylamine oxide. Preferred are C10-C18 alkyl dimethylamine oxide, and C10-C18 acylamido alkyl dimethylamine oxide. Surfactants and especially non-ionic surfactants may be present in amounts from 0 to 10% by weight, preferably from 0.1% to 10%, and most preferably from 0.25% to 6%.
Other suitable nonionic surfactants can be oxidized thioethers of alcohol alkoxylates e.g. the oxidized thioethers described in international patent application WO12095481 (BASF).
The rinse aid of the composition can be used in industrial dish washing (ware washing).
The invention is further summarized in the following paragraphs:
Wash assay I was used to test the effect of using an amylase in ADW rinse aid in combination with a commercial dishwash tab containing amylase and protease.
As detergent Finish all in 1 (from Germany) was used. Neophos rinse aid (from Denmark) was used in the rinsing phase. A total of 3 ml Neophos rinse aid (from Denmark) was used in the rinsing phase. Further, 0.09 gram of amylase SEQ ID NO: 2 was added to the rinse aid during the two rinse phases, as described in Wash Assay I.
The homemade soils used were mix starch and pasta which were prepared according to the Soil preparation procedure.
A first wash was conducted as described in Wash assay I.
The evaluation of the soil removal was done as described in Assay I. The performance on pasta soil is evaluated by visual scoring three trained test persons and according to Assay II.
Results:
Wash assay I was used to test the effect of using an amylase in ADW rinse aid in combination with a commercial dish wash tab containing amylase and protease.
As detergent Finish Quantum all in 1 (from Germany) was used. A total of 3 ml Neophos rinse aid (from Denmark) was used in the rinsing phase. Further, 0.09 gram of amylase SEQ ID NO: 2 was added during the rinse aid phase, as described in Wash Assay I.
The homemade soils used were mix starch and pasta which were prepared according to the Soil preparation procedure.
A first wash was then completed as described in Wash assay I.
The evaluation of the soil removal was done as described in Assay I. The performance on pasta soil is evaluated by visual scoring three trained test persons and according to Assay II.
Results:
Wash assay I was used to test the effect of using an amylase and a protease in ADW rinse aid in combination with a model detergent containing no enzymes.
As detergent 20 g of model detergent was used. A total of 3 ml Neophos rinse aid (from Denmark) was used in the rinsing phase. Further, 0.6 gram of amylase SEQ ID NO: 2 and 1.8 g of protease SEQ ID NO: 5 were added during the rinse aid phase, as described in Wash Assay I.
The homemade soils used were mix starch and egg yolk which were prepared according to the Soil preparation procedure.
A wash was conducted as described in Wash assay I.
The evaluation of the soil removal was done as described in Assay I
Results:
Wash assay I was used to test the effect of using an amylase and a protease in ADW rinse aid in combination with a model detergent containing amylase and protease.
As detergent 20 g of model detergent was used. 0.6 g of protease SEQ ID NO: 4 and 0.2 g of amylase SEQ ID NO: 1) were added to the detergent. A total of 3 ml Neophos rinse aid (from Denmark) was used in the rinsing phase. Further, 0.09 gram of amylase SEQ ID NO: 2 and 0.27 g of protease SEQ ID NO: 5 were added during the rinse aid phase, as described in Wash assay I. The homemade soils used were mix starch and egg yolk and were prepared according to the Soil preparation procedure.
A wash was conducted as described in Wash assay I.
The evaluation of the soil removal was done as described in Assay I
| Number | Date | Country | Kind |
|---|---|---|---|
| 16175968 | Jun 2016 | EP | regional |
| Filing Document | Filing Date | Country | Kind |
|---|---|---|---|
| PCT/EP2017/064673 | 6/15/2017 | WO | 00 |
| Publishing Document | Publishing Date | Country | Kind |
|---|---|---|---|
| WO2017/220422 | 12/28/2017 | WO | A |
| Number | Name | Date | Kind |
|---|---|---|---|
| 5551990 | Van Dijk | Sep 1996 | A |
| 20120172280 | Knotzel | Jul 2012 | A1 |
| 20120252106 | Knotzel | Oct 2012 | A1 |
| 20140251385 | Kelly-Murray | Sep 2014 | A1 |
| 20150107629 | Stott, II | Apr 2015 | A1 |
| 20150232827 | Raab | Aug 2015 | A1 |
| 20160083703 | Andersen | Mar 2016 | A1 |
| Number | Date | Country |
|---|---|---|
| 0070587 | Jan 1983 | EP |
| 0271155 | Jun 1988 | EP |
| 2071237 | Sep 1971 | FR |
| 2247025 | Feb 1992 | GB |
| 9407984 | Apr 1994 | WO |
| WO 9510603 | Apr 1995 | WO |
| 2015144780 | Oct 2015 | WO |
| 2015144782 | Oct 2015 | WO |
| 2015144932 | Oct 2015 | WO |
| 2015149641 | Oct 2015 | WO |
| WO 2015149641 | Oct 2015 | WO |
| WO 2016001449 | Jan 2016 | WO |
| Number | Date | Country | |
|---|---|---|---|
| 20190233766 A1 | Aug 2019 | US |
