Journal
BIOTECHNOLOGY LETTERS
Volume 32, Issue 4, Pages 533-537Publisher
SPRINGER
DOI: 10.1007/s10529-009-0194-z
Keywords
Alcohol dehydrogenase; Anti-Prelog; Oenococcus oeni; (R)-2-Octanol; 2-Octanone reduction
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Funding
- National Natural Science Foundation of China (NSFC) [20376031]
- National Key Basic Research and Development Program of China (973 Program) [2003CB716008]
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An anti-Prelog alcohol dehydrogenase from Oenococcus oeni that reduces 2-octanone to (R)-2-octanol was purified by 26-fold to homogeneity. The enzyme had a homodimeric structure consisting of 49 kDa subunits, required NADPH, but not NADH, as a cofactor and was a Zn-independent short-chain dehydrogenase. Aliphatic methyl ketones (chain length a parts per thousand yen6 carbon atoms) and aromatic methyl ketones were the preferred substrates for the enzyme, the best being 2-octanone. Maximum enzyme activity with 2-octanone was at 45A degrees C and at pH 8.0.
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