A thermostable collagenolytic protease with a very large molecular mass produced by thermophilic Bacillus sp. strain MO-1

被引：77

作者：

Okamoto M. ^{[1
]}

Yonejima Y. ^{[1
]}

Tsujimoto Y. ^{[1
]}

Suzuki Y. ^{[1
]}

Watanabe K. ^{[1
]}

机构：

[1] Department of Applied Biochemistry, Kyoto Prefectural University, Kyoto 606-8522, Shimogamo, Sakyo

来源：

Applied Microbiology and Biotechnology | 2001年 / 57卷 / 1期

关键词：

Molecular Mass; Gelatin; Collagenase; Serine Protease; Clostridium;

D O I：

10.1007/s002530100731

中图分类号：

学科分类号：

摘要：

A collagenolytic protease was purified to homogeneity from thermophilic Bacillus sp. strain MO-1. The protease from strain MO-1 showed high activity toward type I and IV collagens and gelatin. However, peptide substrates (4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-Arg and 2-furylacryloyl-Leu-Gly-Pro-Ala) for collagenases were inert as substrates. The collagenolytic protease cleaved oxidized insulin B-chain at 11 sites and degraded type I and IV collagens into anonymous small pieces, suggesting that the protease digests collagens at multiple sites. The collagenolytic protease was far more thermostable than a mesophilic Clostridium histolyticum collagenase. The collagenolytic protease possesses two salient features: (1) it has a very large molecular mass, 210 kDa, and consists of two, identical 105-kDa subunits; (2) it belongs to a serine protease group. The high molecular mass is unique among serine proteases but common for collagenases. The features of the enzyme from strain MO-1 suggest that it is a new collagenolytic protease which is distinct from previously reported collagenases and serine proteases.

引用

页码：103 / 108

页数：5

共 29 条

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