WO2003066792A1 - Detergent contenant une enzyme - Google Patents

Detergent contenant une enzyme Download PDF

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Publication number
WO2003066792A1
WO2003066792A1 PCT/JP2003/001209 JP0301209W WO03066792A1 WO 2003066792 A1 WO2003066792 A1 WO 2003066792A1 JP 0301209 W JP0301209 W JP 0301209W WO 03066792 A1 WO03066792 A1 WO 03066792A1
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WO
WIPO (PCT)
Prior art keywords
cholesterol
protein
detergent
solution
lipid
Prior art date
Application number
PCT/JP2003/001209
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English (en)
Japanese (ja)
Inventor
Yusuke Nagai
Masaki Imayasu
Sadanori Ohno
Original Assignee
Menicon Co., Ltd.
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Application filed by Menicon Co., Ltd. filed Critical Menicon Co., Ltd.
Priority to JP2003566144A priority Critical patent/JP4394955B2/ja
Publication of WO2003066792A1 publication Critical patent/WO2003066792A1/fr

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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 present invention relates to a cleaning agent for clothes, tableware, glasses, shave, brushes and the like to which lipids of biological origin adhere.
  • it relates to contact lens cleaning agents.
  • detergents that adhere to lipids of biological origin such as clothing, tableware, glasses, shave, and brushes, use detergents that use lipase as a surfactant and decompose components of lipid stains, such as wax esters and triglycerides. It has been known.
  • cholesterol ester is a substance that easily adheres to and is difficult to remove from lipid stains. Therefore, conventional products could not sufficiently decompose and remove lipid stains.
  • An object of the present invention is to provide a detergent capable of effectively decomposing and removing lipid stains caused by cholesterol esters in view of the above-mentioned conventional technology. Disclosure of the invention
  • the present invention relates to a detergent containing a protein having cholesterol esterase activity as an active ingredient.
  • the protein is preferably an enzyme derived from Pseudomonas sp., Particularly an enzyme derived from Pseudomonas aeruginosa. Preferably, there is.
  • the protein is preferably cholesterol esterase having the following physicochemical properties.
  • Substrate specificity High activity against cholesterol linoleate, cholesterol oleate, cholesterol stearate, cholesterol palmitate, n-force cholesterol prillate, cholesterol myristate, cholesterol laurate, cholesterol caprate
  • Optimum pH and pH stability Optimum pH for hydrolysis using cholesterol linoleate as a substrate: 5.5 to 9.5, 25 to 19 hours using Britton-Robinson broad buffer The remaining activity is about 100% at pH 5-10
  • Optimum temperature and temperature stability When cholesterol linoleate is used as a substrate, the optimum temperature for hydrolysis is about 53 ° C in 0.1 M phosphate buffer (pH 7.0). Residual activity after treatment at temperature for 30 minutes is almost 100% up to 50
  • the protein is preferably an enzyme derived from Trichoderma genus, in particular, Trichoderma sugihara strain (Trichoderma sugihara; deposited) Institution National Institute of Advanced Industrial Science and Technology (AIST) Patent Organism Depositary Center (I POD) 1-1, Higashi 1-chome, Tsukuba-shi, Ibaraki, Japan Deposit date: December 6, 2002, Deposit number: FERM BP-8273)
  • the enzyme is
  • FIG. 1 is a graph showing the amount and distribution of lipid remaining on a lens after a lipid removal test.
  • FIG. 2 is a graph showing the amount and distribution of lipid remaining on the lens after the lipid removal test.
  • FIG. 3 is a graph showing the amount and distribution of lipid remaining on the lens after the lipid removal test.
  • the protein having cholesterol esterase activity may be any protein that has cholesterol esterase activity and does not adversely affect the object to be washed, the human body, and the environment. It can be obtained by culturing microorganisms that produce proteins having the protein, or commercially available products include Wako Pure Chemical Industries, Ltd., Sigma-Aldrich (SI GMA-ALDR ICH), TOY ⁇ BO, Fuji Spinning Co., Ltd. Examples include those that can be obtained from Meito Sangyo Co., Ltd., Amano Enzym Co., Ltd., Novozims, etc.
  • отно ⁇ кактивное ка ⁇ ество a cholesterol esterase activity derived from commercially available products such as Amano 30 (hereinafter AY) (manufactured by Amano Enzym Co., Ltd.), or a strain of Pseudomonas aeruginoza Ml cultured and purified at Osaka Municipal Industrial Research Institute. Enzyme (hereinafter referred to as No.
  • CE cholesterol esterase
  • OF lipase OF
  • MY lipase MY
  • MY Meito Sangyo Co., Ltd.
  • Lipase AY Has a cholesterol esterase activity derived from commercially available products such as Amano 30 (hereinafter AY) (manufactured by Amano Enzym Co., Ltd.), or a strain of Pseudomonas aeruginoza Ml cultured and purified at Osaka Municipal Industrial Research Institute. Enzyme (hereinafter referred to as No.
  • cholesterol esterase No. 3 and S-CEII are enzymes having the following physicochemical properties, respectively.
  • Substrate specificity High activity against cholesterol linoleate, cholesterol oleate, cholesterol stearate, cholesterol palmitate, n-force cholesterol prillate, cholesterol myristate, cholesterol laurate, cholesterol caprate
  • Optimum temperature and temperature stability When cholesterol linoleate is used as a substrate, the optimum temperature for hydrolysis is about 53 ° C with 0.1 mM phosphate buffer (pH 7.0). Residual activity after treatment at temperature for 30 minutes is almost 100% up to 50 ° C
  • Substrate specificity cholesterol linoleate, cholesterol oleate, cholesterol stearate, cholesterol palmitate, cholesterol n-capillate, cholesterol myristate, cholesterol laurate, cholesterol pulpate, cholesterol puprilate
  • Optimum pH and pH stability The optimum pH for hydrolysis using cholesterol linoleate as a substrate is 4.5 to 6.5, and Britton-Robinson at 25 ° C using a wide-area buffer. The residual activity after 16 hours is pH4-8.
  • Optimum temperature and temperature stability When cholesterol linoleate is used as the substrate, the optimum temperature for hydrolysis is about 40 C in 0.1 M phosphate buffer (pH 7.0), and in each temperature in the same buffer. Almost 100% residual activity after 60 minutes treatment up to 60 ° C
  • Trichoderma sugihara strain Trichoderma sugihara; Depositary Agency, National Institute of Advanced Industrial Science and Technology
  • S-CEII derived from FERM BP-8273 is the most preferred.
  • Morphological properties (1) Morphology of vesicles: 1 x 2 m bacilli
  • Colony morphology Produces a water-soluble brown pigment by forming a wavy, convex, round colony on a normal agar medium at 30 ° C for 48 hours. The surface is shiny
  • the surface color of the hyphae was white or yellowish white in the form of a pillar or wool, and contaminants were observed from 5 days onward.
  • OA and MEA a change in colony color length to green is observed.
  • the colony surface becomes dry, no exudate is found, and no soluble pigment is produced.
  • the conidium becomes clumpy from the tip of the conidiophore, and the conidiophore also agglomerates to form a nodule.
  • conidia have many conidia-like fungi of Trichoderma spp., Which are regularly branched.
  • the conidia are unicellular, 2-3 m, and the surface is smooth.
  • the shape is spherical or subspherical.
  • the conidia sprouting germinating spermatozoa are divergent, with more than 90% of them diverging from two to four, smooth, short, and bulging on the midside.
  • Culturing of these strains can be carried out by a method known in the art.
  • an enzyme preparation (hereinafter, referred to as a crude enzyme solution) can be obtained from the clear solution by a known method such as ammonium sulfate salting out, solvent precipitation using alcohol, acetone, or the like, and concentration using an ultrafiltration membrane.
  • highly purified enzyme preparations (hereinafter referred to as purified enzyme solutions) can be obtained using conventional methods such as ion-exchange chromatography, adsorption chromatography, gel filtration chromatography, and hydrophobic chromatography. Purification may be performed by a conventional purification method. In the present invention, both the crude enzyme solution and the purified enzyme solution can be used.
  • the content of the protein having cholesterol esterase activity in the detergent of the present invention is preferably 0.01 to 20% by weight, more preferably 0.01 to 15% by weight. is there. If the content of the protein having cholesterol esterase activity is less than 0.001% by weight, a sufficient lipid removing effect may not be obtained. If the content is more than 20% by weight, the protein may be washed. It may remain and may harm the object to be cleaned or the human body.
  • the detergent of the present invention may further contain a pH adjuster for preventing inactivation of cholesterol esterase activity, a surfactant and the like.
  • the pH adjusting agent used in the present invention can provide a pH condition under which the enzyme agent and the protein having cholesterol esterase activity can be stably present in the enzyme preparation and Z or the final preparation liquid by its adjusting action, which adversely affects the object to be washed, the human body, and the environment. Anything can be used as long as it is not tolerated.
  • pH adjusters examples include AD A ⁇ N— (2-acetamido) iminoniacetic acid ⁇ , HEPES (N-2-hydroxyethylpiperazine-N, 12-ethanesulfonic acid), MES ⁇ 2- (N-morpholino) ethanesulfonic acid ⁇ , TES ⁇ N-tris (hydroxymethyl) methyl-12-aminoethanesulfonic acid ⁇ , tris (hydroxymethyl) aminomethane, bis-tris, bistrispropane, acetic acid , Verona, Shiridani Ammonium, ethanolamine, diethanolamine, triethanolamine, carbonic acid, fumaric acid, maleic acid, glycine, glycylglycine, citrate, phosphoric acid, histidine, pyrophosphate, EDTA (edetate) and its Buffer components such as salts thereof; and those known to have a pH adjusting function, such as hydrochloric acid, boric acid compounds, sodium hydroxide
  • the addition amount of the pH adjuster is preferably from 0.01 mM to 5 M, more preferably from 1 mM to 2 M. If the added amount of the pH adjuster is less than 0.0 ImM, the pH adjuster may not be able to exert sufficient buffering capacity, and if it is more than 5 M, the amount becomes excessive and the production cost of the detergent is unnecessarily increased. Tend to increase. Specifically, when tris (hydroxylmethyl) aminomethane is used, the amount is preferably from 0.01 to 30% by weight, more preferably from 0.01 to 20% by weight. Surfactants are used to further enhance the cleaning effect.
  • the surfactant used in the present invention may be any surfactant that does not inadvertently inhibit cholesterol esterase activity and does not adversely affect the object to be cleaned, the human body, and the environment.
  • any of a nonionic surfactant, an amphoteric surfactant and an anionic surfactant can be used.
  • Nonionic surfactants include polyoxyethylene alkyl ether, polyoxyethylene alkylphenyl ether, polyoxyethylene fatty acid ester, sorbitan monoalkylate, polyoxyethylene sorbitan monoalkylate, glycerol Monoalkylate, fatty acid genoleamide, polyoxyethylene alkylamine, polyoxyethylene fatty acid amide, di (polyoxyethylene) alkylamine, polyoxyethylene, polyoxyethylene polyoxypropylene block copolymer, etc. Is raised.
  • amphoteric surfactant examples include dimethyl alkyl betaine, alkyl glycine, alkyl alanine, alkyl amide betaine, 2-alkyl-1-N-hydroxypropyl-N-hydroxyethylimidazolinium betaine, and the like.
  • anionic surfactants include bile salts such as sodium cholate, conjugated bile salts such as sodium taurocholate, or alkyl sulfates, polyoxyethylene alkyl ether sulfates, and n-acyl amino acid salts. And polyoxyethylene alkyl ether acetates, alkyl sulfocarboxylates, polyolefin sulfonates, and polyxixylene alkyl ether phosphates.
  • bile salts and conjugated bile salts which do not affect enzyme activity and exhibit high detergency are preferred, and sodium cholate and sodium taurocholate are particularly preferred.
  • the addition amount of the surfactant is preferably 0.01 to 30% by weight, more preferably 0.01 to 25% by weight. If the amount of the surfactant is less than 0.001% by weight, a sufficient cleaning effect tends not to be obtained. If the amount is more than 30% by weight, there is a possibility that the cleaning target and the human body may be adversely affected. is there.
  • the cleaning agent of the present invention When the cleaning agent of the present invention is used as a liquid, water or the like is further added as necessary.
  • bactericides, preservatives, chelating agents, isotonic agents, thickeners, and bactericides and cleaning aids can be added according to the intended use.
  • the test solution can be prepared, for example, by adding 1 Omg of the protein to be tested to 5 ml of 0.5 mM EDTA-Na and 20 mM potassium phosphate buffer (PH7.5) containing 0.2% BSA. .
  • the crude enzyme solution is used in a 2 OmM potassium phosphate buffer solution (pH 7.5) containing 0.5 mM EDTA_Na and 0.2% BSA.
  • Diluents of various concentrations can be prepared by diluting with, and a test solution that can measure an appropriate absorbance can be selected and used.
  • the cholesterol esterase activity [UZm 1] of the test solution was determined by converting commercially available cholesterol esterase (for example, cholesterol esterase 16 U / mg, manufactured by Wako Pure Chemical Industries, Ltd.) to 0.5 mM EDTA_Na and 0.2% BSA ( ⁇ By dissolving in 2 OmM potassium phosphate buffer ( ⁇ 7.5) containing (serum albumin), a control solution with a known activity [UZml] can be prepared and calculated using the calibration curve method. .
  • commercially available cholesterol esterase for example, cholesterol esterase 16 U / mg, manufactured by Wako Pure Chemical Industries, Ltd.
  • BSA ⁇ By dissolving in 2 OmM potassium phosphate buffer ( ⁇ 7.5) containing (serum albumin
  • the change in absorbance at 500 nm was recorded for 1 minute, the change in absorbance per minute (AA t ) was determined from the initial gradient, and the value obtained by subtracting the change in absorbance (AA b ) from the blind value was calculated as (AA t — and AA b), cholesterol E cholinesterase activity of the test liquid can be determined by the following equation.
  • the cholesterol esterase activity was defined as one unit of the amount of the enzyme that produces 1 ⁇ mole of cholesterol per minute.
  • medium pH 7.0
  • One platinum loop of Pseudomonas aeruginosa Ml strain was inoculated into this medium, and this was cultured with shaking at 26 ° C for about 4 days.
  • the culture was centrifuged to remove the cells, and powdered sulfuric acid was added to the supernatant until the final concentration became 70% saturated, followed by standing at 15 ° C for 1 day.
  • the resulting precipitate was collected by centrifugation, dissolved in 15 ml of water, and dialyzed against a 2 mM phosphate buffer solution (PH 7.0) to obtain a crude enzyme solution.
  • This medium contains Trichoderma sugihara strain (Depositary Organization, National Institute of Advanced Industrial Science and Technology, Patent Organism Depositary Center (I POD) 1-1-1, Higashi, Tsukuba, Ibaraki, Japan Deposit date 2002, Date of deposit 2002 On December 25, FERM BP-8273)
  • I POD Patent Organism Depositary Center
  • One platinum loop was inoculated, and this was cultured with shaking at 26 ° C for about 4 days. After completion of the culture, the culture was centrifuged to remove the cells, and ammonium sulfate powder was added to the supernatant until the final concentration was 70% saturated, followed by standing at 15 ° C for 1 day. The resulting precipitate was collected by centrifugation, dissolved in 15 ml of water, and dialyzed against 2 mM phosphate buffer (pH 7.0) to obtain a crude enzyme solution.
  • Lipase F manufactured by Meito Sangyo Co., Ltd. (hereinafter referred to as OF), Lipase M Y Meito Sangyo Co., Ltd. (hereinafter referred to as MY), Lipase A "Amano” 6 Amano Enzym Co., Ltd. (hereinafter A), Lipase A "Amano” 10 Amano Enzym Co., Ltd. (M Lipase F-API5 Amano Enzym Co., Ltd. (hereinafter, F-API5), lipase AY "Amano" 30 Amano Enzym Co., Ltd.
  • AY lipase 100% Nagase Cholesterol esterase activity was measured by the following method for cholesterol esterase No. 3 (manufactured by Chemical Industry Co., Ltd. (hereinafter referred to as “Sigen”) and Pseudomonas aeruginosa Ml strain (Osaka Municipal Industrial Research Institute).
  • Cholesterol linoleate (manufactured by Sigma-Aldrich (SI GMA-ALDR ICH)) was used as a substrate, and an isopropanol solution (0.03 mM) of the same substrate was heated to 72-74 ° C at 1.0 vZ v%. After mixing with an aqueous solution of Triton X-100 and stirring for 30 minutes in a water bath at 72 to 74 ° C, the mixture was cooled to room temperature in running water. Then, 60 Omg of sodium cholate was added and dissolved, and the final liquid volume was adjusted to 10 Oml with the 1. Ov / v% Triton X-100 aqueous solution.
  • 0.2M potassium phosphate buffer 15 Om1 1.76 wZv% of 4-aminoantipyrine aqueous solution 5 m1, 6 wZv% of phenol aqueous solution 1 Om1, and 150 PU / m1 of horseradish-derived pel
  • the mixture was mixed with 10 ml of an aqueous oxidase solution (7500 priprogalin units dissolved in 50 ml of 0.1 M potassium phosphate buffer (pH 7.0)).
  • test solution 0.05 ml was added and mixed.
  • the cholesterol esterase activity [U / ml] of the test solution was determined by adding commercially available cholesterol esterase (for example, cholesterol esterase 16U / mg, manufactured by Wako Pure Chemical Industries, Ltd.) to 0.5 mM EDTA-Na and 0.2% BSA.
  • a control solution with a known activity [UZml] was prepared by dissolving in 2 OmM potassium phosphate buffer (pH 7.5) containing (pserum serum albumin), and calculated using the calibration curve method.
  • Cholesterol esterase S The cholesterol esterase activity of CEII was measured by the following method.
  • the crude enzyme solution obtained in Production Example 2 was appropriately diluted with a 2 OmM potassium phosphate buffer solution containing 0.5 mM EDTA-Na and 0.2% BSA (PH7.5). One used.
  • Cholesterol esterase activity was determined by using cholesterol linoleate (manufactured by ICN Pharmaceuticals Co., Ltd.) as a substrate and 0.03 M of the same substrate solution (dissolved in isopropanol) 21111 at 72-74 ° 1% Triton X— The mixture was mixed with 100 ml of 100 aqueous solution, kept at this temperature for 30 minutes, and then cooled to room temperature.
  • Tris buffer solution a tris (hydroxymethyl) aminomethane buffer solution (hereinafter referred to as a Tris buffer solution) containing 16 mg of each of the enzymes CE, ⁇ F, MY or AY, each containing 8 ml of 0.5 wZv% sodium taurocholate was used. (pH 7.4).
  • the No. manufactured in Production Example 1 was used.
  • 2.5 ml of the crude enzyme solution (3) was dissolved in 7.5 ml of Tris buffer (PH7.4) containing 1.0% w / v sodium taurocholate.
  • Example 6 4.4 ml of the crude enzyme solution of S-CEII produced in Production Example 2 was dissolved in 7.6 ml of Tris buffer (pH 7.4) containing 1.
  • Ow / v% sodium taurocholate was prepared.
  • 6 mg of the enzyme Ml was dissolved in 8 ml of Tris buffer (pH 7.4) containing 0.5 wZv% of sodium taurocholate, and in Comparative Example 2, 0.5 wZv% of taurochol containing no enzyme was dissolved.
  • a sodium acid-containing Tris buffer (PH7.4) was prepared.
  • 6 mg of the enzyme Ml was dissolved in 8 ml of a 1.0 wZv% sodium taurocholate-containing tris buffer (PH7.4).
  • the enzyme was not contained. 1.
  • OwZv A Tris buffer solution (pH 7.4) containing 5% sodium taurocholate was prepared.
  • a silicone-based contact lens (lipid-stained lens) to which lipid stains are artificially attached is treated according to Examples 1-4 and Comparative Examples 1-2, and the lipid stains remaining on the treated lenses are subjected to gas chromatography. The lipid removal ability of a protein having cholesterol esterase activity was evaluated.
  • Tripalmitin (manufactured by Nakarai Tesque Co., Ltd.), cholesterol oleate (manufactured by Tokyo Kasei Kogyo Co., Ltd.), and stearyl stearate (manufactured by Funakoshi Co., Ltd.) were weighed at 25 mg each, and the mixture was added to a 0.5 ml cloth form. After dissolving, 24.5 ml of physiological saline was added, and the mixture was vigorously stirred to prepare a suspension. The suspension (10 Om1) was dropped on the concave side of the silicone-based contact lens, and dried at room temperature for 3 days to prepare a lipid-stained lens to which lipid stains were artificially attached.
  • One lipid-stained lens was immersed in 2 ml of each test solution, and left standing at 30 for 2 hours to treat the lipid-stained lens. After the treatment, the lens was removed from the test solution, rinsed with a physiological saline solution, dried, and the amount of lipid stain remaining on the lens was determined by gas chromatography. The results are shown in Table 2 and FIG. Table 2
  • lipid-stained lens was immersed in 2 mL of the solution of Example 5 and Comparative Examples 3 and 4, and left at 30 ° C. for 2 hours to treat the lipid-stained lens. After the treatment, the lens was removed from the test solution or control solution, rinsed with a physiological saline solution, dried, and the amount of lipid stain remaining on the lens was determined by gas chromatography. Lipid stain was quantified as a control for an untreated lens with artificial stain.
  • Example 5 having cholesterol esterase activity had a smaller amount of residual lipid, indicating that lipids could be removed more.
  • lipid-stained lens was immersed in 2 mL of the solution of Example 6 and Comparative Examples 3 and 4, and allowed to stand at 30 ° C. for 2 hours to treat the lipid-stained lens. After the treatment, the lens was removed from the test solution or control solution, rinsed with a physiological saline solution, dried, and the amount of lipid stain remaining on the lens was determined by gas chromatography. Lipid stain was quantified as a control for an untreated lens with artificial stain.
  • Example 6 having cholesterol esterase activity had a smaller amount of residual lipid, indicating that lipids could be removed more.
  • Test Examples 1 to 3 are the results of a protein having cholesterol esterase activity effectively decomposing and removing lipids, especially cholesterol esters, and prove the effectiveness of the present invention.
  • lipid dirt components (especially cholesterol ester) can be effectively decomposed and removed, so that the fixed fat can be more effectively used than when lipase or the like having no such activity is used. Can be removed.
  • Lipid stain easily adheres to silicon-based low water content soft contact lenses among contact lenses.
  • surfactants alone Cholesterol esters, which are considered difficult to remove, contain proteins with cholesterol esterase activity, which can be efficiently decomposed and removed, prolonging the life of contact lenses and providing a better wearing feeling. And furthermore, it is possible to reduce eye damage caused by lipid contamination of the contact lens.

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  • 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)
  • Enzymes And Modification Thereof (AREA)

Abstract

La présente invention concerne un détergent qui contient comme principe actif une protéine ayant une activité de cholestérol estérase. Ce détergent permet de décomposer et d'éliminer efficacement les tâches de graisse dues à des esters de cholestérol.
PCT/JP2003/001209 2002-02-08 2003-02-06 Detergent contenant une enzyme WO2003066792A1 (fr)

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JP2003566144A JP4394955B2 (ja) 2002-02-08 2003-02-06 酵素含有洗浄剤

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JP2002-33162 2002-02-08
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Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2009520219A (ja) 2005-12-14 2009-05-21 ボーシュ アンド ローム インコーポレイティド レンズを包装する方法
WO2013122219A1 (fr) * 2012-02-15 2013-08-22 公益財団法人北九州産業学術推進機構 Composition tensioactive à base d'acide carboxylique, et détergent et agent d'extinction d'incendie contenant celle- ci

Citations (10)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS527483A (en) * 1975-07-03 1977-01-20 Nagase Sangyo Kk Prparation of cholesterol esterase
US4011138A (en) * 1974-06-17 1977-03-08 Kyowa Hakko Kogyo Co., Ltd. Process for the preparation of cholesterol esterase
JPH0598294A (ja) * 1991-10-08 1993-04-20 Nippon Petrochem Co Ltd 洗浄剤組成物
WO1994023052A1 (fr) * 1993-04-02 1994-10-13 Novo Nordisk A/S PROCEDE D'HYDROLYSE D'ESTERS DE CHOLESTEROL AU MOYEN D'ESTERASE DE CHOLESTEROL DE $i(PSEUDOMONAS FRAGI)
JPH07203959A (ja) * 1994-01-19 1995-08-08 Kyowa Hakko Kogyo Co Ltd 安定型コレステロール・エステラーゼおよびその製造法
JPH08109397A (ja) * 1994-10-13 1996-04-30 Hitachi Chem Co Ltd 洗浄剤及び洗浄方法
WO2000047708A1 (fr) * 1999-02-10 2000-08-17 The Procter & Gamble Company Solides particulaires faible densite utilises dans les detergents pour lessive
JP2000239696A (ja) * 1999-02-22 2000-09-05 Nof Corp コンタクトレンズ用処理溶液
JP2000241773A (ja) * 1999-02-22 2000-09-08 Nof Corp コンタクトレンズ用処理溶液
US6136778A (en) * 1998-07-22 2000-10-24 Kamiya; Akira Environment safeguarding aqueous detergent composition comprising essential oils

Patent Citations (10)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4011138A (en) * 1974-06-17 1977-03-08 Kyowa Hakko Kogyo Co., Ltd. Process for the preparation of cholesterol esterase
JPS527483A (en) * 1975-07-03 1977-01-20 Nagase Sangyo Kk Prparation of cholesterol esterase
JPH0598294A (ja) * 1991-10-08 1993-04-20 Nippon Petrochem Co Ltd 洗浄剤組成物
WO1994023052A1 (fr) * 1993-04-02 1994-10-13 Novo Nordisk A/S PROCEDE D'HYDROLYSE D'ESTERS DE CHOLESTEROL AU MOYEN D'ESTERASE DE CHOLESTEROL DE $i(PSEUDOMONAS FRAGI)
JPH07203959A (ja) * 1994-01-19 1995-08-08 Kyowa Hakko Kogyo Co Ltd 安定型コレステロール・エステラーゼおよびその製造法
JPH08109397A (ja) * 1994-10-13 1996-04-30 Hitachi Chem Co Ltd 洗浄剤及び洗浄方法
US6136778A (en) * 1998-07-22 2000-10-24 Kamiya; Akira Environment safeguarding aqueous detergent composition comprising essential oils
WO2000047708A1 (fr) * 1999-02-10 2000-08-17 The Procter & Gamble Company Solides particulaires faible densite utilises dans les detergents pour lessive
JP2000239696A (ja) * 1999-02-22 2000-09-05 Nof Corp コンタクトレンズ用処理溶液
JP2000241773A (ja) * 1999-02-22 2000-09-08 Nof Corp コンタクトレンズ用処理溶液

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2009520219A (ja) 2005-12-14 2009-05-21 ボーシュ アンド ローム インコーポレイティド レンズを包装する方法
WO2013122219A1 (fr) * 2012-02-15 2013-08-22 公益財団法人北九州産業学術推進機構 Composition tensioactive à base d'acide carboxylique, et détergent et agent d'extinction d'incendie contenant celle- ci

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