Highly Thermostable Neutral Protease from Bacillus stearothemophilus
スポンサーリンク
概要
- 論文の詳細を見る
Bacillus stearothermophilus MK232,which produced a highly thermostable neutral protease, was isolated from a natural environment. By several steps of mutagenesis, a hyper-producing mutant strain, YG185,was obtained. The enzyme productivity was twice as much as that of the original strain. This extracellular neutral protease was purified and crystallized. The molecular weight of the enzyme was 34,000 by SDS-polyacrylamide gel electrophoresis and gel filtration. The optimum pH and temperature for the enzyme activity were 7.5 and 70℃, respectively, and the enzyme was stable at pH 5-10 and below 70℃. The thermostability and specific activity of the new protease are around 10% and 40% higher than those of thermolysin (the neutral protease from Bacillus thermoproteolytics), respectively. The enzyme was inactivated by EDTA, but not by phenylmethylusulfonyl fluoride. These results indicata that the enzyme is a highly thermostable neutral-(metallo) protease.
- 社団法人日本生物工学会の論文
- 1988-02-25
著者
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IMANAKA Tadayuki
Department of Synthetic and Biological Chemistry, Graduate School of Engineering, Kyoto University
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Seto Koji
Biotechnology Research Laboratory Tosoh Co. Ltd.
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Seto Koji
Biotechnology Research Laboratory Tosoh Corporation
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Kubo Motoki
Department Of Bioscience And Technology Faculty Of Science And Engineering Ritsumeikan University
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Kubo Motoki
Department Of Fermentation Technology Faculty Of Engineering Osaka University
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Imanaka Tadayuki
Department Of Applied Biotechnology Faculty Of Engineering Osaka University
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Imanaka Tadayuki
Department Of Fermentation Technology Faculty Of Engineering Osaka University
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Kubo Motoki
Department Of Bioscience & Technology Faculty Of Science & Engineering Ritsumeikan Universit
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MURAYAMA Keiichi
Biotechnology Research Laboratory, Tosoh Co., Ltd.
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Murayama K
Matsushita Electric Ind. Co. Ltd. Bizen‐shi Jpn
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IMANAKA TADAYUKI
Department of Fermentation Technology, Faculty of Engineering, Osaka University
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