EP0517761B1 - Lipase enthaltendes flüssiges einweichmittel und dessen verwendung - Google Patents
Lipase enthaltendes flüssiges einweichmittel und dessen verwendung Download PDFInfo
- Publication number
- EP0517761B1 EP0517761B1 EP19910905035 EP91905035A EP0517761B1 EP 0517761 B1 EP0517761 B1 EP 0517761B1 EP 19910905035 EP19910905035 EP 19910905035 EP 91905035 A EP91905035 A EP 91905035A EP 0517761 B1 EP0517761 B1 EP 0517761B1
- Authority
- EP
- European Patent Office
- Prior art keywords
- spotter
- lipase
- fat
- alcohol
- laundry
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
Links
- 239000004367 Lipase Substances 0.000 title claims abstract description 40
- 102000004882 Lipase Human genes 0.000 title claims abstract description 40
- 108090001060 Lipase Proteins 0.000 title claims abstract description 40
- 235000019421 lipase Nutrition 0.000 title claims abstract description 40
- 239000007788 liquid Substances 0.000 title claims abstract description 18
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims abstract description 21
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 13
- 239000004094 surface-active agent Substances 0.000 claims abstract description 11
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 claims description 30
- 239000000203 mixture Substances 0.000 claims description 21
- 238000005406 washing Methods 0.000 claims description 13
- 235000019626 lipase activity Nutrition 0.000 claims description 9
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 claims description 6
- 239000003381 stabilizer Substances 0.000 claims description 4
- 239000004599 antimicrobial Substances 0.000 claims description 2
- 230000000694 effects Effects 0.000 abstract description 18
- 235000019197 fats Nutrition 0.000 description 15
- 238000009472 formulation Methods 0.000 description 15
- 239000003921 oil Substances 0.000 description 13
- 235000019198 oils Nutrition 0.000 description 13
- 238000012360 testing method Methods 0.000 description 11
- 239000003599 detergent Substances 0.000 description 8
- 238000011156 evaluation Methods 0.000 description 8
- 239000000463 material Substances 0.000 description 8
- 150000002148 esters Chemical class 0.000 description 7
- 230000015572 biosynthetic process Effects 0.000 description 6
- 239000004744 fabric Substances 0.000 description 6
- 229920000742 Cotton Polymers 0.000 description 5
- 102000004190 Enzymes Human genes 0.000 description 5
- 108090000790 Enzymes Proteins 0.000 description 5
- 230000007062 hydrolysis Effects 0.000 description 5
- 238000006460 hydrolysis reaction Methods 0.000 description 5
- 235000008390 olive oil Nutrition 0.000 description 5
- 239000004006 olive oil Substances 0.000 description 5
- 238000003786 synthesis reaction Methods 0.000 description 5
- 150000001298 alcohols Chemical class 0.000 description 4
- 238000000034 method Methods 0.000 description 4
- 239000000843 powder Substances 0.000 description 4
- -1 NaCl) Chemical class 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- FERIUCNNQQJTOY-UHFFFAOYSA-N Butyric acid Chemical compound CCCC(O)=O FERIUCNNQQJTOY-UHFFFAOYSA-N 0.000 description 2
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 2
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- RAHZWNYVWXNFOC-UHFFFAOYSA-N Sulphur dioxide Chemical compound O=S=O RAHZWNYVWXNFOC-UHFFFAOYSA-N 0.000 description 2
- UYXTWWCETRIEDR-UHFFFAOYSA-N Tributyrin Chemical compound CCCC(=O)OCC(OC(=O)CCC)COC(=O)CCC UYXTWWCETRIEDR-UHFFFAOYSA-N 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- ZBJVLWIYKOAYQH-UHFFFAOYSA-N naphthalen-2-yl 2-hydroxybenzoate Chemical compound OC1=CC=CC=C1C(=O)OC1=CC=C(C=CC=C2)C2=C1 ZBJVLWIYKOAYQH-UHFFFAOYSA-N 0.000 description 2
- 244000215068 Acacia senegal Species 0.000 description 1
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- BDAGIHXWWSANSR-UHFFFAOYSA-M Formate Chemical compound [O-]C=O BDAGIHXWWSANSR-UHFFFAOYSA-M 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 229920000084 Gum arabic Polymers 0.000 description 1
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 239000004115 Sodium Silicate Substances 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- 239000000205 acacia gum Substances 0.000 description 1
- 235000010489 acacia gum Nutrition 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 235000010233 benzoic acid Nutrition 0.000 description 1
- WPYMKLBDIGXBTP-UHFFFAOYSA-N benzoic acid group Chemical group C(C1=CC=CC=C1)(=O)O WPYMKLBDIGXBTP-UHFFFAOYSA-N 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 235000014121 butter Nutrition 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 235000011148 calcium chloride Nutrition 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 125000004432 carbon atom Chemical group C* 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 235000019253 formic acid Nutrition 0.000 description 1
- 150000004674 formic acids Chemical class 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 235000014655 lactic acid Nutrition 0.000 description 1
- 235000013310 margarine Nutrition 0.000 description 1
- 239000003264 margarine Substances 0.000 description 1
- 239000000693 micelle Substances 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- 235000005985 organic acids Nutrition 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 230000035515 penetration Effects 0.000 description 1
- HWGNBUXHKFFFIH-UHFFFAOYSA-I pentasodium;[oxido(phosphonatooxy)phosphoryl] phosphate Chemical compound [Na+].[Na+].[Na+].[Na+].[Na+].[O-]P([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O HWGNBUXHKFFFIH-UHFFFAOYSA-I 0.000 description 1
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 0.000 description 1
- 235000019260 propionic acid Nutrition 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 235000019795 sodium metasilicate Nutrition 0.000 description 1
- NTHWMYGWWRZVTN-UHFFFAOYSA-N sodium silicate Chemical compound [Na+].[Na+].[O-][Si]([O-])=O NTHWMYGWWRZVTN-UHFFFAOYSA-N 0.000 description 1
- 229910052911 sodium silicate Inorganic materials 0.000 description 1
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- 235000019832 sodium triphosphate Nutrition 0.000 description 1
- 235000010199 sorbic acid Nutrition 0.000 description 1
- WSWCOQWTEOXDQX-MQQKCMAXSA-N sorbic acid group Chemical group C(\C=C\C=C\C)(=O)O WSWCOQWTEOXDQX-MQQKCMAXSA-N 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 235000010269 sulphur dioxide Nutrition 0.000 description 1
- 239000004291 sulphur dioxide Substances 0.000 description 1
- 238000011179 visual inspection Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
Definitions
- the invention relates to a lipase containing liquid pre-spotter and to a use of such pre-spotter.
- the purpose of the invention is the provision of a simple lipase containing liquid pre-spotter, which exhibits an improved fat and oil removing effect and an improved lipase stability.
- the lipase containing and surfactant free liquid pre-spotter according to the invention comprises a liquid mixture of an alcohol and water, with an alcohol content above 20% by weight, and an effective amount of lipase, whereby the balance is water. It should be noted that the pre-spotter according to the invention does not contain any surfactant, and thus exhibits a simple composition, in spite of the fact that the pre-spotter according to the invention is very effective, as demonstrated in the following examples.
- alcohol comprises both monovalent alcohols like ethanol and polyvalent alcohols (polyols) like propylene glycol. If the alcohol content is below 10% by weight, the effect and the stability of the lipase tend to be unsatisfactory.
- an effective amount of lipase means an amount, which is able to remove fat and oil stains effectively, when evaluated by swatch tests described later in this specification. It is intended that all lipases can be used in the pre-spotter according to the invention. Reference can be made to Research Disclosure June 1988, No. 290, 29056.
- DE-A-3 003 766 describes a lipase containing liquid pre-spotter which besides an alkanolamine contains at least 10% of a surfactant.
- This is a typical example of an aqueous, enzyme containing pre-spotter, as this kind of prior art pre-spotter all contain a surfactant.
- the pre-spotter according to the invention is surfactant free and does not need to contain alkalolamine.
- the effect of the pre-spotter according to the invention is as good as or better than the known surfactant containing pre-spotter and the pre-spotter according to the invention is cheaper than the prior art pre-spotters, because the pre-spotter according to the invention does not contain the relatively expensive surfactant.
- the pre-spotter further comprises a lipase stabilizer.
- a lipase stabilizer examples include CaCl2 (e.g. 0.1-0.5%) or a protease inhibitor (such as borate and formate).
- the alcohol is a mono- or polyvalent alcohol with 2-3 carbon atoms, preferably ethanol, propylene glycol, glycerol or a mixture of two or more of these. It has been found that the fat and oil removing effect is most satisfactory with these alcohols.
- the lipase activity is at least 10,000 LU/liter of liquid pre-spotter. It has been found that the time interval between application of pre-spotter and main wash is undue long in order to obtain an efficient fat and oil removal, if the lipase activity is less than 10,000 LU/liter of liquid pre-spotter. On the other hand, for economic reasons a suitable upper limit for the lipase activity is 5,000,000 LU/liter of liquid pre-spotter.
- the lipase is Lipolase®. It has been found that the fat and oil removal is very efficient in this embodiment.
- the pre-spotter contains an antimicrobial agent.
- antimicrobial agents are inorganic salts (such as NaCl), sugars (such as sucrose and glucose), organic acids (such as benzoic, sorbic, propionic, lactic and formic acids) which are generally effective in amounts of 0.01-2% at low pH (below 5).
- stabilizing agents are antioxidants (such as sulphur dioxide), 1,2-benz-iso-thioazolin-3-one (BIT) and parabens. Some of these may also serve to improve enzyme stability.
- the pH value is between 4 and 10, preferably between 5 and 9.
- the stability optimum and the activity optimum of the lipase should be taken into consideration.
- the invention comprises a use of the pre-spotter according to the invention, and this use is characterized by the fact that the pre-spotter is applied locally to the fat or oil spots on the laundry, that the laundry is left alone for a certain time period, and the the laundry subsequently is exposed to a low temperature washing process.
- the certain time period alluded to above is normally at least 5 minutes, but it can be shorter in case the lipase activity in the pre-spotter is extraordinarily high.
- the lipase activity is measured in LU lipase activity units.
- the LU activity determination method is based on hydrolysis of tributyrin in a pH-stat.
- 1 LU lipase Unit
- 1 LU lipase Unit is the amount of enzyme which liberates 1 ⁇ mole titratable butyric acid per minute at 30°C and pH 7.0 with gum arabic as an emulsifier. Further details are given in Novo Nordisk analytical Method AF 95/5, available on request from Novo Nordisk A/S, Novo Allé, DK-2880 Bagsvaerd, Denmark.
- Embodiments of liquid pre-spotter is applied to the fat stain on a test swatch by means of a pipette.
- the amount of pre-spotter used depends on the size of the stain and on the kind of fabric; typically 0.5-3 ml of pre-spotter is satisfactory.
- After 5-30 minutes of incubation the swatches are washed in a Laboratory washing machine (Launder-o-meter or Terg-o-tometer) at low temperature (20-40°C).
- the detergent used in the washing process is a standard powder or liquid detergent.
- the swatches are made from coloured (e.g. blue or green) cotton fabric.
- the fabric is cut into test pieces with the dimensions 12x12 cm, and 75-150 ⁇ l of fatty material (e.g. lard, margarine, butter, or olive oil) is applied to the center of each swatch.
- fatty material e.g. lard, margarine, butter, or olive oil
- the amount of fatty material applied depends on the type of fatty material used.
- the fatty material is heated to approx. 70°C before application in order to facilitate the penetration of fatty material into the fabric.
- the stained fabric was aged at room temperature for 1 day before treatment.
- the swatches After washing and drying the swatches are gently ironed. The swatches are visually inspected and compared to reference swatches which have been identically treated but without any lipase added to the pre-spotter formulation. In order to quantify the efficiency of the lipase, extraction of the residual fatty material can be carried out (Soxhlet, chloroform, 5 hours).
- Stain Lard on green cotton sheet. 75 ⁇ l of lard was applied on each swatch. After stain application, the swatches were heat treated in an oven for 30 minutes at 75°C in order to obtain a better distribution of the stain.
- Pre-spotting 1 ml of pre-spotter is applied with a pipette on the centre of the stains and subsequently the swatches are incubated for 15 minutes at room temperature.
- the pre-spotter formulations contained 1% Lipolase® 100L (100,000 LU/g) and 99% (w/w) of a mixture of water and propylene glycol. Accordingly the lipase activity in the pre-spotters was 1000 LU/g.
- Example 2 The same kind of test material and the same pre-spotting, washing, and evaluation method as described in Example 1 was used; the only difference being that the dosage of Lipolase® 100 L was varied between 0 and 5%.
- Example 2 The same experiments as described in Example 2 were carried out, the only difference being that four lipases of different origin (2 fungal, 1 bacterial and 1 from yeast) were investigated. The lipases were compared on an LU-activity basis.
- test material The same kind of test material and the same pre-spotting washing, and evaluation method as described in Example 1 was used.
- the lipase activity in the pre-spotter was 5000 LU/g.
- Washing Immediately after pre-spotting the swatches were washed in a Terg-o-tometer (30°C, 30 minutes, 18° dH, pH 9.5) with a commercial European powder detergent (5 g/l). Evaluation: The performance of the pre-spotter was evaluated by the same test panel method as described in Example 1. Results: The mean scores (12 persons) were as follows:
- Lipolase® The enzymatic stability of Lipolase® was investigated in 5 different pre-spotter formulations.
- the pre-spotter formulations were stored at 30°C in closed bottles and the activity was followed over a 2 months period.
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Wood Science & Technology (AREA)
- Organic Chemistry (AREA)
- Detergent Compositions (AREA)
- Chemical Or Physical Treatment Of Fibers (AREA)
Claims (8)
- Lipase enthaltendes und tensidfreies flüssiges Einweichmittel, das eine flüssige Mischung aus einem Alkohol und Wasser, mit einem Alkoholgehalt über 20 Gew.-%, und eine wirksame Menge an Lipase umfaßt, wobei der Rest Wasser ist.
- Einweichmittel nach Anspruch 1, das außerdem einen Lipasestabilisator umfaßt.
- Einweichmittel nach den Ansprüchen 1 bis 2, in dem der Alkohol Ethanol, Propylenglykol, Glycerin oder eine Mischung aus zwei oder mehreren derselben ist.
- Einweichmittel nach den Ansprüchen 1 bis 3, in dem die Lipaseaktivität wenigstens 10.000 LU/Liter flüssiges Einweichmittel beträgt.
- Einweichmittel nach den Ansprüchen 1 bis 4, wobei die Lipase Lipolase® ist.
- Einweichmittel nach den Ansprüchen 1 bis 5, wobei das Einweichmittel ein antimikrobielles Mittel enthält.
- Einweichmittel nach den Ansprüchen 1 bis 6, wobei der pH-Wert zwischen 4 und 10, vorzugsweise zwischen 5 und 9 liegt.
- Verwendung des Einweichmittels nach den Ansprüchen 1-7, gekennzeichnet durch die Tatsache, daß das Einweichmittel örtlich auf die Fett- oder Ölflecke auf der Wäsche aufgebracht wird, daß die Wäsche für einen bestimmten Zeitraum sich überlassen bleibt und daß die Wäsche anschließend einem Niedertemperatur-Waschverfahren ausgesetzt wird.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| AT91905035T ATE101642T1 (de) | 1990-03-01 | 1991-02-28 | Lipase enthaltendes fluessiges einweichmittel und dessen verwendung. |
Applications Claiming Priority (6)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DK53090A DK53090D0 (de) | 1990-03-01 | 1990-03-01 | |
| DK530/90 | 1990-03-01 | ||
| DK77290A DK77290D0 (da) | 1990-03-01 | 1990-03-26 | Lipaseholdig flydende pre-spotter og anvendelse af en saadan pre-spotter |
| DK772/90 | 1990-03-26 | ||
| DK118/91 | 1991-01-24 | ||
| DK11891A DK11891D0 (da) | 1991-01-24 | 1991-01-24 | Lipaseholdig flydende pre-spotter og anvendelse af en saadan pre-spotter. |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| EP0517761A1 EP0517761A1 (de) | 1992-12-16 |
| EP0517761B1 true EP0517761B1 (de) | 1994-02-16 |
Family
ID=27220418
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| EP19910905035 Expired - Lifetime EP0517761B1 (de) | 1990-03-01 | 1991-02-28 | Lipase enthaltendes flüssiges einweichmittel und dessen verwendung |
Country Status (6)
| Country | Link |
|---|---|
| EP (1) | EP0517761B1 (de) |
| JP (1) | JP2930719B2 (de) |
| DE (1) | DE69101219T2 (de) |
| DK (1) | DK0517761T3 (de) |
| ES (1) | ES2051122T3 (de) |
| WO (2) | WO1991013142A1 (de) |
Cited By (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2014200658A1 (en) | 2013-06-13 | 2014-12-18 | Danisco Us Inc. | Alpha-amylase from promicromonospora vindobonensis |
| WO2014200657A1 (en) | 2013-06-13 | 2014-12-18 | Danisco Us Inc. | Alpha-amylase from streptomyces xiamenensis |
| WO2014200656A1 (en) | 2013-06-13 | 2014-12-18 | Danisco Us Inc. | Alpha-amylase from streptomyces umbrinus |
| WO2014204596A1 (en) | 2013-06-17 | 2014-12-24 | Danisco Us Inc. | Alpha-amylase from bacillaceae family member |
| WO2015050724A1 (en) | 2013-10-03 | 2015-04-09 | Danisco Us Inc. | Alpha-amylases from a subset of exiguobacterium, and methods of use, thereof |
| WO2015050723A1 (en) | 2013-10-03 | 2015-04-09 | Danisco Us Inc. | Alpha-amylases from exiguobacterium, and methods of use, thereof |
| WO2015077126A1 (en) | 2013-11-20 | 2015-05-28 | Danisco Us Inc. | Variant alpha-amylases having reduced susceptibility to protease cleavage, and methods of use, thereof |
| WO2017173190A2 (en) | 2016-04-01 | 2017-10-05 | Danisco Us Inc. | Alpha-amylases, compositions & methods |
| WO2017173324A2 (en) | 2016-04-01 | 2017-10-05 | Danisco Us Inc. | Alpha-amylases, compositions & methods |
Families Citing this family (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ES2152246T3 (es) * | 1991-12-20 | 2001-02-01 | Novo Nordisk As | Eliminacion de esteres hidrofobicos de los tejidos. |
| US5605881A (en) * | 1993-09-03 | 1997-02-25 | Minolta Co., Ltd. | Cleaning liquid for recycling copy medium for electrophotography |
| CA2161975C (en) * | 1994-03-21 | 2000-02-01 | Jeanne A. O'brien | Stable enzyme-containing aqueous laundry prespotting composition |
| US5510052A (en) * | 1994-08-25 | 1996-04-23 | Colgate-Palmolive Co. | Enzymatic aqueous pretreatment composition for dishware |
| CN109844085A (zh) * | 2016-09-13 | 2019-06-04 | 诺维信公司 | 洗涤剂组合物、洗涤剂组合物的用途和洗涤纺织品的方法 |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| NL8000452A (nl) * | 1979-02-07 | 1980-08-11 | Unilever Nv | Voorbehandelingsmiddel voor wasgoed. |
| DE3223568A1 (de) * | 1982-06-24 | 1983-12-29 | Peter 5275 Bergneustadt Penz jun. | Detachiermittel und detachierverfahren |
| NL8900267A (nl) * | 1989-02-03 | 1990-09-03 | Douwe Egberts Tabaksfab | Vloeibaar reinigingsmiddel. |
-
1991
- 1991-02-28 WO PCT/DK1991/000059 patent/WO1991013142A1/en not_active Ceased
- 1991-02-28 WO PCT/DK1991/000058 patent/WO1991013141A1/en not_active Ceased
- 1991-02-28 EP EP19910905035 patent/EP0517761B1/de not_active Expired - Lifetime
- 1991-02-28 DE DE69101219T patent/DE69101219T2/de not_active Expired - Fee Related
- 1991-02-28 JP JP3504594A patent/JP2930719B2/ja not_active Expired - Lifetime
- 1991-02-28 DK DK91905035T patent/DK0517761T3/da active
- 1991-02-28 ES ES91905035T patent/ES2051122T3/es not_active Expired - Lifetime
Cited By (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2014200658A1 (en) | 2013-06-13 | 2014-12-18 | Danisco Us Inc. | Alpha-amylase from promicromonospora vindobonensis |
| WO2014200657A1 (en) | 2013-06-13 | 2014-12-18 | Danisco Us Inc. | Alpha-amylase from streptomyces xiamenensis |
| WO2014200656A1 (en) | 2013-06-13 | 2014-12-18 | Danisco Us Inc. | Alpha-amylase from streptomyces umbrinus |
| WO2014204596A1 (en) | 2013-06-17 | 2014-12-24 | Danisco Us Inc. | Alpha-amylase from bacillaceae family member |
| WO2015050724A1 (en) | 2013-10-03 | 2015-04-09 | Danisco Us Inc. | Alpha-amylases from a subset of exiguobacterium, and methods of use, thereof |
| WO2015050723A1 (en) | 2013-10-03 | 2015-04-09 | Danisco Us Inc. | Alpha-amylases from exiguobacterium, and methods of use, thereof |
| WO2015077126A1 (en) | 2013-11-20 | 2015-05-28 | Danisco Us Inc. | Variant alpha-amylases having reduced susceptibility to protease cleavage, and methods of use, thereof |
| WO2017173190A2 (en) | 2016-04-01 | 2017-10-05 | Danisco Us Inc. | Alpha-amylases, compositions & methods |
| WO2017173324A2 (en) | 2016-04-01 | 2017-10-05 | Danisco Us Inc. | Alpha-amylases, compositions & methods |
Also Published As
| Publication number | Publication date |
|---|---|
| DE69101219D1 (de) | 1994-03-24 |
| WO1991013141A1 (en) | 1991-09-05 |
| WO1991013142A1 (en) | 1991-09-05 |
| ES2051122T3 (es) | 1994-06-01 |
| DE69101219T2 (de) | 1994-06-01 |
| JP2930719B2 (ja) | 1999-08-03 |
| JPH05504368A (ja) | 1993-07-08 |
| EP0517761A1 (de) | 1992-12-16 |
| DK0517761T3 (da) | 1994-05-09 |
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