Expression in Escherichia coli of a Gene Encoding a Thermostable Chitinase from Streptomyces thermoviolaceus OPC-520
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概要
- 論文の詳細を見る
An expression plasmid for a thermostable chitinase gene from S. thermoviolaceus OPC-520 in E. coli was constructed. A cloned chitinase (Chi40) was purified from the periplasmic space of E. coli harboring the expression plasmid. The N-terminal sequence of Chi40 was 11 amino acids longer than that of chitinase from S. thermovilaceus OPC-520 (ST chitinase), however, a loss or addition of the amino acid residues did not affect the enzymatic properties. The mutations of Asp-145 and Glu-147 drastically decreased the specific activity of chitinase from the wild type, indicating that both amino acid residues are the best candidates for the essential catalytic residues of Chi40.
- 社団法人日本農芸化学会の論文
- 1995-01-23
著者
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TSUJIBO Hiroshi
Osaka University of Pharmaceutical Sciences
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MIYAMOTO Katsushiro
Osaka University of Pharmaceutical Sciences
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INAMORI Yoshihiko
Osaka University of Pharmaceutical Sciences
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ENDO Hiroshi
Osaka University of Pharmaceutical Sciences
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Endo H
Endo Microalgal Res. Lab. Tokyo Jpn
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Miyamoto K
Central Research Laboratories Osaka University Of Pharmaceutical Sciences
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Inamori Yoshihiko
Osaka College Of Pharmacy
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Miyamoto Katsushiro
Osaka Univ. Of Pharmaceutical Sciences
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