1992 Fiscal Year Final Research Report Summary
Improvement of Screening Method for a New Protease-Producing Microorganism and Studies on a Novel Type of Protease
| Project/Area Number |
03660120
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
応用微生物学・発酵学
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| Research Institution | The Kumamoto Institute of Technology |
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Principal Investigator |
MURAO Sawao The Kumamoto Institute of Technology Department of Applied Microbial Technology Professor, 工学部, 教授 (00081472)
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| Co-Investigator(Kenkyū-buntansha) |
OYAMA Hiroshi The Kumamoto Institute of Technology Department of Applied Microbial Technology, 工学部, 助手 (50221700)
SHIN Takashi The Kumamoto Institute of Technology Department of Applied Microbial Technology, 工学部, 助教授 (50179066)
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| Project Period (FY) |
1991 – 1992
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| Keywords | Protease / Screening / Substrate specificity |
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| Research Abstract |
Murao et al. improved the screening method for a new protease-producing Microorganism. The unique points of this screening method were, 1 ; the use of various specific protease inhibitors (SSI, MAPI, etc.), 2 ; the use of fluorescence substrate, 3 ; the use of HPLC. We isolated to semi-alkaline protease, two prolyl endopeptidases, and elastase-like protease for a short term. [1] The molecular weights and isoelectric point(pI) of semi-alkaline protease from Penicillium sp. FG-1 were estimated to be 32,000 and 9.4, respectively. The enzyme specifically hydrolyzed the-Leu(15)-Tyr(16) bond in iinsulin B chain. [2] The molecular weights and isoelectric point(pI) of prolyl endopeptidase from Alcaligenes sp. KU-22 were estimated to be 76,000 and 4.9, respectively. The enzyme specifically hydrolyzed the -Pro-X- bond in Z-Gly-Pro-pNA. [3] The molecular weights and isoelectric point(pI) of prolyl endopeptidase from Streptomyces xanthophaeus HA-36 were estimated to be 47,000 and 4.8, respectively. The enzyme specigically hydrolyzed the -Pro-X- bond in Z-Ala-Ala-Pro-pNA. [4] The molecular weights and isoelectric point(pI) of elastase-like protrease from Streptomyces sp. SH-22 were estimated to be 26,000 and 6.4, respectively. The enzyme specifically hydrolyzed the-Ala-X- bond in Z-Ala-Ala-Ala-pNA. Detailed investigation of characterization of these enzymes have been undertaken now in our laboratory.
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