Journal
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
Volume 100, Issue 3, Pages 318-322Publisher
SOC BIOSCIENCE BIOENGINEERING JAPAN
DOI: 10.1263/jbb.100.318
Keywords
Brevibacterium; 2-phenylethanol; alcohol dehydrogenase
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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 39 kDa. 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 Cu2+, Ni2+, Ba2+, Hg2+ and p-chloromercuribenzoate. The enzyme is expected to be applicable as an effective biocatalyst in the oxidation of various alcohols.
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