Isolation and Characterization of Membrane-bound L-Sorbose Dehydrogenase from Gluconobacter melanogenus UV10(Microbiology & Fermentation Industry)
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概要
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Membrane-bound L-sorbose dehydrogenase was purified from the membrane fraction of Gluconobacter melanogenus UV10. The reaction with 2,6-dichlorophenolindophenol or phenazine methosulfate as acceptor was formulated as; L-sorbose+acceptor→L-sorbosone+reduced acceptor. The enzyme was purified by DEAE-Cellulose, DEAE-Sepharose, and Sephadex G-200 column chromatographies after differential solubilization with Triton X-100 and Tween 80, and appeared as a single band in a SDS-PAGE gel at the molecular weight of about 58,000. It was most active at pH7.0 and 48℃, and rather stable at around 7.0 in a buffer containing 200 mM L-sorbose, below 30℃. It showed high substrate specificity for L-sorbose, and its activity was stimulated by Fe^<3+> and Co^<2+> , and inhibited by Cu^<2+> , quinine, mono-iodoacetate, and sodium fluoroacetate.
- 1991-02-23
著者
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Fujiwara Akiko
Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima Uni
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Fujiwara A
Department Of Applied Microbiology Nippon Roche Research Center
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Hoshino Tatsuo
Departments of Medicine, Keio University and The Lankenau Hospital
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Fujiwara Akiko
Department Of Applied Microbiology Nippon Roche Research Center
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Hoshino T
Department Of Applied Microbiology Nippon Roche Research Center
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Sugisawa Teruhide
Department of Applied Microbiology, Nippon Roche Research Center
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NOMURA Setsuko
Department of Applied Microbiology, Nippon Roche Research Center
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Nomura Setsuko
Department Of Applied Microbiology Nippon Roche Research Center
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Hoshino Tatsuo
Department Of Applied Microbiology Nippon Roche Research Center
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Fujiwara Masahiro
Department Of Applied Microbiology Nippon Roche Research Center
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Sugisawa T
Nippon Roche Res. Center Kanagawa Jpn
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Sugisawa Teruhide
Department Of Applied Microbiology Nippon Roche Research Center
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