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Improvement of Screening Method for a New Protease-Producing Microorganism and Studies on a Novel Type of Protease

新型产蛋白酶微生物筛选方法的改进及新型蛋白酶的研究

基本信息

批准号：
03660120
负责人：
MURAO Sawao
金额：
$ 1.41万
依托单位：
The Kumamoto Institute of Technology
依托单位国家：
日本
项目类别：
Grant-in-Aid for General Scientific Research (C)
财政年份：
1991
资助国家：
日本
起止时间：
1991 至 1992
项目状态：
已结题

项目摘要

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.

Murao等人。对一株新型产酶微生物的筛选方法进行了改进。该筛选方法的独到之处是，1；使用各种特异性的蛋白酶抑制剂(SSI、MAPI等)；2；使用荧光底物；3；使用高效液相色谱法。我们在短期内分离到了半碱性蛋白酶、两个脯氨基内肽酶和弹性蛋白酶样酶。[1]青霉半碱性蛋白酶的相对分子质量和等电点。FG-1估计分别为3.2万和9.4。该酶能特异性地降解胰岛素B链上的-Leu(15)-Tyr(16)键。[2]产碱菌Prolyl内肽酶的相对分子质量和等电点。KU-22估计分别为7.6万人和4.9人。该酶能特异性地降解Z-Gly-Pro-PNA中的-Pro-X键。[3]测定了黄色链霉菌HA-36的Pro内切酶的相对分子质量为47,000，等电点为4.8。该酶能特异性地降解Z-Ala-Ala-Pro-PNA中的-Pro-X键。[4]链霉菌类弹性蛋白酶的相对分子质量和等电点。SH-22估计分别为2.6万人和6.4人。该酶能特异性地降解Z-Ala-PNA中的-Ala-X-键。我们实验室现在已经对这些酶的特性进行了详细的研究。