JPS6480282A - Nonaqueous highly active enzyme - Google Patents

Nonaqueous highly active enzyme

Info

Publication number
JPS6480282A
JPS6480282A JP62236261A JP23626187A JPS6480282A JP S6480282 A JPS6480282 A JP S6480282A JP 62236261 A JP62236261 A JP 62236261A JP 23626187 A JP23626187 A JP 23626187A JP S6480282 A JPS6480282 A JP S6480282A
Authority
JP
Japan
Prior art keywords
enzyme
lipid
buffer solution
nonaqueous
dissolved
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.)
Pending
Application number
JP62236261A
Other languages
Japanese (ja)
Inventor
Shigeo Okahata
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
NOF Corp
Original Assignee
Nippon Oil and Fats 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 Nippon Oil and Fats Co Ltd filed Critical Nippon Oil and Fats Co Ltd
Priority to JP62236261A priority Critical patent/JPS6480282A/en
Publication of JPS6480282A publication Critical patent/JPS6480282A/en
Pending legal-status Critical Current

Links

Classifications

    • YGENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y02TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
    • Y02PCLIMATE CHANGE MITIGATION TECHNOLOGIES IN THE PRODUCTION OR PROCESSING OF GOODS
    • Y02P20/00Technologies relating to chemical industry
    • Y02P20/50Improvements relating to the production of bulk chemicals
    • Y02P20/52Improvements relating to the production of bulk chemicals using catalysts, e.g. selective catalysts

Landscapes

  • Enzymes And Modification Thereof (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)

Abstract

PURPOSE:To obtain an enzyme capable of carrying out reaction, such as ester or peptide synthesis, in high yield in a nonaqueous system, by dispersing a lipid in a buffer solution containing the enzyme dissolved therein and cooling the resultant dispersion. CONSTITUTION:A hydrolase, such as lipase, is dissolved in a buffer solution at pH 5.0-7.0 and a lipid, such as monogalactosyldiglyceride, alone or a solution thereof dissolved in a hydrophilic organic solvent, buffer solution, etc., is dripped thereon while cooling and dispersed by a stirrer, ultrasonic waves, etc. After sufficient dispersion, cooling is carried out to deposit and precipitate the resultant enzyme-lipid complex. The obtained precipitates are subsequently separated by centrifugation, etc., and washed with a buffer solution and then distilled water, directly subjected to treatment, such as freeze-drying, to afford the aimed powdery nonaqueous highly active enzyme. The lipid is preferably mixed with the enzyme at a solid weight ratio (lipid weight/enzyme weight) within the range of 0.2-100.
JP62236261A 1987-09-22 1987-09-22 Nonaqueous highly active enzyme Pending JPS6480282A (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
JP62236261A JPS6480282A (en) 1987-09-22 1987-09-22 Nonaqueous highly active enzyme

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
JP62236261A JPS6480282A (en) 1987-09-22 1987-09-22 Nonaqueous highly active enzyme

Publications (1)

Publication Number Publication Date
JPS6480282A true JPS6480282A (en) 1989-03-27

Family

ID=16998160

Family Applications (1)

Application Number Title Priority Date Filing Date
JP62236261A Pending JPS6480282A (en) 1987-09-22 1987-09-22 Nonaqueous highly active enzyme

Country Status (1)

Country Link
JP (1) JPS6480282A (en)

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH09118842A (en) * 1995-10-26 1997-05-06 Nippon Paint Co Ltd Self-renewal type stainproof coating composition
WO2002103003A1 (en) * 2001-06-15 2002-12-27 Matsushita Electric Industrial Co., Ltd. Lipid-modified enzymes, process for producing the same and biosensor
JP2009029790A (en) * 1995-11-14 2009-02-12 Aventis Pharma Sa Lipopolyamine as transfection agent and pharmaceutical use thereof

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH09118842A (en) * 1995-10-26 1997-05-06 Nippon Paint Co Ltd Self-renewal type stainproof coating composition
JP2009029790A (en) * 1995-11-14 2009-02-12 Aventis Pharma Sa Lipopolyamine as transfection agent and pharmaceutical use thereof
WO2002103003A1 (en) * 2001-06-15 2002-12-27 Matsushita Electric Industrial Co., Ltd. Lipid-modified enzymes, process for producing the same and biosensor

Similar Documents

Publication Publication Date Title
Weetall Alkaline phosphatase insolubilized by covalent linkage to porous glass
Ståhl et al. The synthesis of a D-amino acid ester in an organic media with α-chymotrypsin modified by a bio-imprinting procedure
GB2297907B (en) Liposomes containing particulate materials
Morton Alkaline phosphatase of milk. 2. Purification of the enzyme
SUZUKI et al. Purification of bovine bradykininogen
Yoshimoto et al. Synthesis of eicosapentaenoyl phosphatidylcholines by polyethylene glycol-modified lipase in benzene
Nickerson et al. Keratinase: II. Properties of the crystalline enzyme
Hashimoto et al. Studies on Xylanase from Trichoderma viride Part I. Isolation and Some Properties of Crystalline Xylanase
JPS6480282A (en) Nonaqueous highly active enzyme
Kise et al. Enzymatic reactions in aqueous-organic media. IV. Chitin-alpha-chymotrypsin complex as a catalyst for amino acid esterification and peptide synthesis in organic solvents
Ohnishi Induction of the site I phosphorylation in vivo in Saccharomyces carlsbergensis
YOSHINAGA et al. Purification and molecular properties of allosteric phosphoenolpyruvate carboxylase from Escherichia coli
Hradec et al. Effect of cholesteryl 14-methylhexadecanoate on the activity of some amino acid-transfer ribonucleic acid ligases from mammalian tissues
Willstätter Problems and methods in enzyme research
RU2148636C1 (en) Method of preparing yeast low-molecular extract and substance prepared by this method
EP0211223A3 (en) Spherical grains of polyamino acid and production method thereof
Hoffman et al. ATP‐stimulated transmitter release and cyclic amp synthesis in isolated chromaffin granules
Pennington et al. Silastic entrapment of glucose oxidase–peroxidase and acetylcholine esterase
JPS6331538A (en) Immobilizing carrier
Johnson et al. Penicillin production by a superior strain of mold
JPS60145095A (en) Preparation of xylitol by immobilized microorganism
SU717129A2 (en) Method of producing mixture of aminoacids and lowest peptides
RU1814900C (en) Method for producing extract of saga horns
Skorkowski Chromatophorotropic neurohormones of the shrimp Crangon crangon. Partial purification of the red-pigment-concentrating hormone
JPS6474987A (en) Novel proline acylase and its production