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

Jun Ichiro Hirano, Kenji Miyamoto, Hiromichi Ohta

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)318-322
Number of pages5
JournalJournal of Bioscience and Bioengineering
Volume100
Issue number3
DOIs
Publication statusPublished - 2005 Dec 15

Keywords

  • 2-phenylethanol
  • Alcohol dehydrogenase
  • Brevibacterium

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

Fingerprint Dive into the research topics of 'Purification and characterization of the alcohol dehydrogenase with a broad substrate specificity originated from 2-phenylethanol-assimilating Brevibacterium sp. KU 1309'. Together they form a unique fingerprint.

  • Cite this