Purification and characterization of the alcohol dehydrogenase with a broad substrate specificity originated from 2-phenylethanol-assimilating Brevibacterium sp. KU 1309

• Published in: Journal of bioscience and bioengineering Vol. 100; no. 3; pp. 318 - 322
• Main Authors: Hirano, Jun-ichiro, Miyamoto, Kenji, Ohta, Hiromichi
• Format: Journal Article
• Language: English
• Published: Amsterdarm Elsevier B.V 01.09.2005; Elsevier Science; Elsevier Limited
• Subjects: 2-phenylethanol; ACTIVIDAD ENZIMATICA; ACTIVITE ENZYMATIQUE; ALCOHOL DEHYDROGENASE; Alcohol Dehydrogenase - antagonists & inhibitors; Alcohol Dehydrogenase - chemistry; Alcohol Dehydrogenase - isolation & purification; ALCOHOL DESHIDROGENASA; ALCOOL DESHYDROGENASE; Amino Acid Sequence; Bacterial Proteins - antagonists & inhibitors; Bacterial Proteins - chemistry; Bacterial Proteins - isolation & purification; Biological and medical sciences; Biotechnology; BREVIBACTERIUM; Brevibacterium - enzymology; DURABILITE; ENZYME ACTIVITY; Enzyme Inhibitors - pharmacology; Fundamental and applied biological sciences. Psychology; Hydrogen-Ion Concentration; Ions - pharmacology; Metals - pharmacology; Molecular Sequence Data; Phenylethyl Alcohol - metabolism; PURIFICACION; PURIFICATION; SOSTENIBILIDAD; Substrate Specificity; SUSTAINABILITY; Temperature; 2-phenylethanol; alcohol dehydrogenase; Brevibacterium; Characterization; Purification; Enzyme; Substrate specificity; Brevibacteriaceae; Bacteria; Actinomycetes; Oxidoreductases; Alcohol dehydrogenase
• ISSN: 1389-1723; 1347-4421
• DOI: 10.1263/jbb.100.318

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 Cu 2+, Ni 2+, Ba 2+, Hg 2+ and p-chloromercuribenzoate. The enzyme is expected to be applicable as an effective biocatalyst in the oxidation of various alcohols.