| Budget Amount *help |
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1992: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1991: ¥1,500,000 (Direct Cost: ¥1,500,000)
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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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