Purification and Characterization of a Thermostable Chitinase from Streptomyces thermoviolaceus OPC-520 and Cloning of the Encoding Gene
スポンサーリンク
概要
- 論文の詳細を見る
When Streptomyces thermoviolaceus OPC-520 was grown in a minimal medium with 1% chitin, three activity bands corresponding to proteins of 40kDa (Chi40), 30kDa (Chi30), and 25kDa (Chi25) were detected. Among them, Chi30 was purified from the culture filtrate of the strain. The molecular mass was estimated to be 30kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and its isoelectric point was 3.8 The optimum pH and temperature of Chi30 were 4.0 and 60℃, respectively. Chi30 was stable at pH 6-8 up to 60℃. The gene encoding Chi30 (chi30) was cloned and its nucleotides sequenced. The open reading frame of chi30 encoded a protein consisting of 347 amino acids with a calculated molecular weight of 35,621. The mature Chi30 consisted of only a catalytic domain and showed a significant similarity with ChiA from S. coelicolor and ChiA from S. lividans. The existence of a 12-bp direct repeat sequence in the promoter region of chi30 was detected, which have been suggested to be involved in both chitin induction and glucose repression.
- 社団法人日本農芸化学会の論文
- 2000-01-23
著者
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Inamori Yoshihiko
Department Of Microbiology Osaka University Of Pharmaceutical Sciences
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Hatano Naoya
Osaka University Of Pharmaceutical Sciences
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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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TSUJIBO Hiroshi
Department of Microbiology, Osaka University of Pharmaceutical Sciences
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ENDO Hiroshi
Osaka University of Pharmaceutical Sciences
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Tsujibo H
Department Of Microbiology 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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