Purification and Characterization of the Alcohol Dehydrogenase with a Broad Substrate Specificity Originated from 2-Phenylethanol-Assimilating Brevibacterium sp. KU 1309(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

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概要

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• A novel 2-phenylethanol dehydrogenase has been purified from a soil bacterium Brevibacterium sp. KU 1309. The enzyme was purified about 1400-fold to homogeneity, and found to be a monomeric enzyme of apparent 39kDa. The enzyme had broad substrate specificity and catalyzes a reversible oxidation of various primary alcohols to aldehydes. The enzyme required NAD^+, but not NADP^+ as a cofactor. Thus, the enzyme was classified into a group of NAD^+-dependent primary alcohol dehydrogenase. The activity was inhibited by Cu^<2+>, Ni^<2+>, Ba^<2+>, Hg^<2+> and p-chloromer-curibenzoate. The enzyme is expected to be applicable as an effective biocatalyst in the oxidation of various alcohols.

• 公益社団法人日本生物工学会の論文
• 2005-09-25

著者

• Ohta Hiromichi

  Department Of Applied Chemistry School Of Engineering Nagoya University

• Ohta Hiromichi

  Department Of Biosciences And Informatics Center For Biosciences And Informatics Keio University

• Miyamoto Kenji

  Department Of Biosciences And Informatics Center For Biosciences And Informatics Keio University

• Hirano Junichiro

  Department of Biosciences and Informatics, Center for Biosciences and Informatics, Keio University

• Hirano Junichiro

  Department Of Biosciences And Informatics Center For Biosciences And Informatics Keio University

• Hirano Jun-ichiro

  Department of Biosciences and Informatics, Center for Biosciences and Informatics, Keio University

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