JPS6474986A - Protease and a novel microorganism producing the same - Google Patents

Protease and a novel microorganism producing the same

Info

Publication number
JPS6474986A
JPS6474986A JP23288587A JP23288587A JPS6474986A JP S6474986 A JPS6474986 A JP S6474986A JP 23288587 A JP23288587 A JP 23288587A JP 23288587 A JP23288587 A JP 23288587A JP S6474986 A JPS6474986 A JP S6474986A
Authority
JP
Japan
Prior art keywords
optimal
active
protease
temperature
same
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.)
Granted
Application number
JP23288587A
Other languages
Japanese (ja)
Other versions
JPH0763366B2 (en
Inventor
Toru Kobayashi
Jun Hitomi
Hiroshi Sonohara
Susumu Ito
Kikuhiko Okamoto
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.)
Kao Corp
Original Assignee
Kao Corp
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 Kao Corp filed Critical Kao Corp
Priority to JP23288587A priority Critical patent/JPH0763366B2/en
Publication of JPS6474986A publication Critical patent/JPS6474986A/en
Publication of JPH0763366B2 publication Critical patent/JPH0763366B2/en
Anticipated expiration legal-status Critical
Expired - Lifetime legal-status Critical Current

Links

Landscapes

  • Enzymes And Modification Thereof (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)

Abstract

NEW MATERIAL:A protease of about 25,000mol.wt. (according to the gel filtration), having the following physical and chemical properties: Action: acts on urea-modified hemoglobin, keratin and a little acts on casein, too; active and optimal pH: the optimal pH ranges from 6.5-10.5, and the active pH is 4.5-12.0; pH stability: it is very stable in 5-12 pH; optimal temperature: the active temperature is 10-70 deg.C, and the optimal temperature is 40 deg.C; inhibitor: it is not inhibited by metal ions and surface active agents. USE:It is used as a heavy or light detergent component. PREPARATION:Bacillus sp. KSM2004 (FERM P-9452) is cultured in an enriched medium and the enzyme is isolated and purified from the filtrates of cell-crushed mixture and the culture mixture.
JP23288587A 1987-09-17 1987-09-17 Novel protease Expired - Lifetime JPH0763366B2 (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
JP23288587A JPH0763366B2 (en) 1987-09-17 1987-09-17 Novel protease

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
JP23288587A JPH0763366B2 (en) 1987-09-17 1987-09-17 Novel protease

Related Child Applications (1)

Application Number Title Priority Date Filing Date
JP26848194A Division JP2509540B2 (en) 1994-11-01 1994-11-01 Novel microorganism that produces new protease

Publications (2)

Publication Number Publication Date
JPS6474986A true JPS6474986A (en) 1989-03-20
JPH0763366B2 JPH0763366B2 (en) 1995-07-12

Family

ID=16946367

Family Applications (1)

Application Number Title Priority Date Filing Date
JP23288587A Expired - Lifetime JPH0763366B2 (en) 1987-09-17 1987-09-17 Novel protease

Country Status (1)

Country Link
JP (1) JPH0763366B2 (en)

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5312561A (en) * 1991-01-22 1994-05-17 Kao Corporation Detergent composition
US5888797A (en) * 1995-02-10 1999-03-30 Novo Nordisk A/S Alkaline protease from Bacillus sp. ZI315

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5312561A (en) * 1991-01-22 1994-05-17 Kao Corporation Detergent composition
US5888797A (en) * 1995-02-10 1999-03-30 Novo Nordisk A/S Alkaline protease from Bacillus sp. ZI315

Also Published As

Publication number Publication date
JPH0763366B2 (en) 1995-07-12

Similar Documents

Publication Publication Date Title
EP1160327A3 (en) Novel proteolytic enzymes and their use in detergents
ES2162132T3 (en) THERMO-STABLE DNA POLYMERASE FROM THERMOANAEROBACTER THERMOHYDROSULFURICUS AND MUTANT ENZYMES, OF SUPPLIED EXONUCLEASE ACTIVITY SO OBTAINED.
KR970009949B1 (en) Novel serine proteolytic enzyme and its process
DK284985A (en) BIOLOGICALLY PURE ASPERGILLUS CULTURE AND A RECOVERED LIPOLYTIC ENZYM
MY103943A (en) Orthorhombic ciclosporin crystal form, process for its production and pharmaceutical compositions containing it
EP0232169A3 (en) Alkaline protease produced by a bacillus
ATE63338T1 (en) PROCESS FOR THE PREPARATION OF 6HYDROXYNICOTINE|URE.
ATE76660T1 (en) ENZYMES FOR THE DEGRADATION OF LIGNIN.
AU7339596A (en) Alkaline protease, process for the production thereof, use thereof, and microorganism producing the same
AU1778988A (en) Novel fibrinolytic enzymes
JPS6474986A (en) Protease and a novel microorganism producing the same
MX9706272A (en) Psychrophilic protease and psychrophilic bacteria.
CA2018562A1 (en) Process for the enzymatic cleavage of vinyl 2-aryl-propionates
DK0667872T3 (en) Mutant interleukin 6 with improved biological activity over wild-type interleukin 6
ATE22702T1 (en) PRODUCTION OF GLUCOSE DEHYDROGENASE.
JP2985018B2 (en) New microorganism
Britsyna et al. Stability of proteinases immobilized on siliceous supports by the glutaraldehyde and benzoquinone methods.
AU548094B2 (en) Unsaturated halogenated diamines
JP3026111B2 (en) Novel alkaline protease and method for producing the same
EP0386240A4 (en) Novel polypeptide compounds
JPS6427498A (en) Production of optically active mercapto compound
WO1990010006A3 (en) NOVEL β-METHOXYACRYLATES, THEIR PRODUCTION AND USE
EP0403172A3 (en) Purified enzyme and process therefor
中川孝之 et al. Properties of the extracellular lytic proteinase of Pseudomonas sp..
Papaioannou et al. Purification and Properties of a Neutral Protease from Soil Bacterium WM 122