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  Detergent compositionsUSPTO Application #: 20060189501Title: Detergent compositions Abstract: Detergent compositions containing high efficiency lipase enzymes and specific detergent formulations comprising less than 10 wt % zeolite and phosphate builder are described. Preferred formulations comprise surfactants selected from alkyl benzene sulphonates in combination with alky ethoxylated sulfates or MES or non-ionic surfactants. (end of abstract)
Agent: The Procter & Gamble Company Intellectual Property Division - Cincinnati, OH, US Inventors: Neil Joseph Lant, Steven George Patterson USPTO Applicaton #: 20060189501 - Class: 510392000 (USPTO) Related Patent Categories: Cleaning Compositions For Solid Surfaces, Auxiliary Compositions Therefor, Or Processes Of Preparing The Compositions, Cleaning Compositions Or Processes Of Preparing (e.g., Sodium Bisulfate Component, Etc.), Enzyme Component Of Specific Activity Or Source (e.g., Protease, Of Bacterial Origin, Etc.) The Patent Description & Claims data below is from USPTO Patent Application 20060189501. Brief Patent Description - Full Patent Description - Patent Application Claims
TECHNICAL FIELD [0001] The present invention relates to laundry detergent compositions and in particular to detergents comprising lipolytic or lipase enzymes. BACKGROUND OF THE INVENTION AND PRIOR ART [0002] Improved removal of greasy soils is a constant aim for laundry detergent manufacturers. In spite of the use of many effective surfactants and combinations of surfactants, especially when used at low water temperatures, many surfactant-based products still do not achieve complete removal of greasy/oily soils. Lipase enzymes have been used in detergents since the late 1980s for removal of fatty soils by breakdown of fatty soils into tri-glycerides. [0003] Until relatively recently, the main commercially available lipase enzymes, such as Lipolase (trade name, Novozymes) worked particularly effectively at the lower moisture levels of the drying phase of the wash process. These enzymes tended to produce significant cleaning only in the second wash step because the active site of the enzyme was occupied by water during the washing process, so that fat breakdown was significant only on soils remaining on laundered clothes during the drying stage, the broken down fats then being removed in the next washing step. However, more recently, higher efficiency lipases have been developed that also work effectively during the wash phase of the cleaning process, so that as well as cleaning in the second washing step, a significant improvement in cleaning effect due to lipase enzyme can be found in the first wash-cycle. Examples of such enzymes are as described in WO00/60063 and Research Disclsoure IP6553D. Such enzymes are referred to below as first wash lipases. Examples of such enzymes include certain variants of lipolase (wild-type Humicola lanuginosa) which should comprise one or more substitutions with positive amino acids near the N-terminal in the three-dimensional structure. The variants should further comprise a peptide addition at the C-terminal and/or should meet certain limitations on electrically charged amino acids at positions 90-101 and 210. [0004] The problem facing the present inventors was how to maximise performance from this new generation of enzymes. The present inventors found that whilst a small benefit could be achieved formulating such enzymes according to present day detergent formulations by simply replacing existing lipase enzymes with the new generation of enzymes, a considerable improvement in performance was found by formulating the detergent compositions in a different way and even reducing the levels of some conventional detergent ingredients. DEFINITION OF THE INVENTION [0005] In accordance with the present invention there is provided a detergent composition comprising a lipase which is a polypeptide having an amino acid sequence which: (a) has at least 90% identity with the wild-type lipase derived from Humicola lanuginosa strain DSM 4109; (b) compared to said wild-type lipase, comprises a substitution of an electrically neutral or negatively charged amino acid at the surface of the three-dimensional structure within 15 .ANG. of E1 or Q249 with a positively charged amino acid; and (c) comprises a peptide addition at the C-terminal; and/or (d) comprises a peptide addition at the N-terminal and/or (e) meets the following limitations: i) comprises a negative amino acid in position E210 of said wild-type lipase; ii) comprises a negatively charged amino acid in the region corresponding to positions 90-101 of said wild-type lipase; and iii) comprises a neutral or negative amino acid at a position corresponding to N94 of said wild-type lipase and/or has a negative or neutral net electric charge in the region corresponding to positions 90-101 of said wild-type lipase; the detergent composition comprising less than 10 wt % aluminosilicate (anhydrous basis) and less than 10 wt % phosphate builder, the composition having a reserve alkalinity of greater than 4. [0006] In accordance with the present invention there is provided a detergent composition comprising a lipase enzyme producing First Wash lard removal performance better than that produced by WT Lipolase (tradename from Novozymes) using the Lard First Wash Test described below, and the detergent composition comprising less than 10 wt % aluminosilicate builder and less than 10 wt % phosphate builder, the composition having a reserve alkalinity greater than 4. WT Lipolase from Novozymes is described in U.S. Pat. No. 5,869,438, seq#2. [0007] In a preferred aspect of the invention, the detergent compositions of the invention comprise less than 10 wt % builders selected from aluminosilicate (zeolite) builder and/or phosphate builder. In a further preferred aspect of the invention, the compositions comprise less than 8 wt % zeolite, or even less than 4 wt % and less than 8 wt % phosphate builder or even less than 4 wt %. [0008] The present inventors have found that when a first wash lipase is used in conjunction with a low level of phosphate and zeolite builder, dramatically improved grease removal benefits are obtained compared to formulating lipase with conventional builder levels. Without wishing to be bound by theory, it is believed that this is driven by the presence of divalent cations enhancing lipase activity by (i) increasing the deposition of enzyme onto the fabric surface and/or (ii) enhancing the precipitation of insoluble fatty acid salts arising from the lipolysis enzymatic process. [0009] While builder reduction or elimination might be expected to raise significant stain removal negatives on, for example, particulate and beverage stains, we have found that the compositions show unexpectedly good performance. Without wishing to be bound by theory it is believed that this is due to fatty acids released by the lipase during lipolysis of fatty soils acting to (i) destabilize these stains via a hardness sequestration effect and (ii) reduce the wash pH slightly resulting in lightening of pH-sensitive stains. DETAILED DESCRIPTION OF THE INVENTION Lipase Enzyme [0010] The reference lipase used in this invention is the wild type lipase derived from Humicola lanuginosa strain DSM 4109. It is described in EP258068 and EP305216 and has the amino acid sequence shown in positions 1-269 of SEQ ID NO: 2 of U.S. Pat. No. 5,869,438. In this specification, the reference lipase is also referred to as Lipolase. Substitution with Positive Amino Acid [0011] The lipase of the invention comprises one or more (e.g. 2-4, particularly two) substitutions of an electrically neutral or negatively charged amino acid near E1 or Q249 with a positively charged amino acid, preferably R. [0012] The substitution is at the surface of the three-dimensional structure within 15 .ANG. of E1 or Q249, e.g. at any of positions 1-11, 90, 95, 169, 171-175, 192-211, 213-226, 228-258, 260-262. [0013] The substitution may be within 10 .ANG. of E1 or Q249, e.g. at any of positions 1-7, 10, 175, 195, 197-202, 204-206, 209, 215, 219-224, 230-239, 242-254. [0014] The substitution may be within 15 .ANG. of E1, e.g. at any of positions 1-11, 169, 171, 192-199, 217-225, 228-240, 243-247, 249, 261-262. [0015] The substitution is most preferably within 10 .ANG. of E1, e.g. at any of positions 1-7, 10, 219-224 and 230-239. [0016] Thus, some preferred substitutions are S3R, S224R, P229R, T231R, N233R, D234R and T244R. Peptide Addition at C-Terminal [0017] The lipase may comprise a peptide addition attached to C-terminal L269. The peptide addition improves the first-wash performance in a variety of detergents. Continue reading... Full patent description for Detergent compositions Brief Patent Description - Full Patent Description - Patent Application Claims Click on the above for other options relating to this Detergent compositions patent application. ###  How KEYWORD MONITOR works... a FREE service from FreshPatents1. Sign up (takes 30 seconds). 2. Fill in the keywords to be monitored. 3. Each week you receive an email with patent applications related to your keywords. Start now! - Receive info on patent apps like Detergent compositions or other areas of interest. ### Previous Patent Application: Aqueous olanexidine solution, method of preparing the same, and disinfectant Next Patent Application: Cleaning compositions that provide grease removal and fragrance delivery Industry Class: Cleaning compositions for solid surfaces, auxiliary compositions therefor, or processes of preparing the compositions ### FreshPatents.com Support Thank you for viewing the Detergent compositions patent info. 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