Isolation and Characterization of NAD(P)-Dependent L-Sorbosone Dehydrogenase from Gluconobacter melanogenus UV10(Microbiology & Fermentation Industry)
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概要
- 論文の詳細を見る
NAD(P)-Dependent L-sorbosone dehydrogenase has been purified from the cytosol fraction of Gluconobacter melanogenus UV10. The enzyme was purified about 30-fold with an overall yield of 19% by column chromatographies on DEAE-Sepharose CL-6B, DEAE-Sephadex A-50, and Blue Sepharose CL-6B. The enzyme required NAD or NADP as a cofactor, and showed broad substrate specificity on various aldehyde compounds. Among them, L-sorbosone was the best substrate for the enzyme. In this respect, the enzyme is a kind of aldehyde dehydrogenase.
- 1991-03-23
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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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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