Purification and characterization of aldehyde dehydrogenase with a broad substrate specificity originated from 2-phenylethanol-assimilating Brevibacterium sp. KU1309

Jun Ichiro Hirano, Kenji Miyamoto, Hiromichi Ohta

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Phenylacetaldehyde dehydrogenase (PADH) was purified and characterized from Brevibacterium sp. KU1309, which can grow on the medium containing 2-phenylethanol as the sole carbon source. This enzyme was a homotetrameric protein with a subunit of 61 kDa. The enzyme catalyzed the oxidation of aryl (benzaldehyde, phenylacetaldehyde, 3-phenylpropionaldehyde) and aliphatic (hexanal, octanal, decanal) aldehydes to the corresponding carboxylic acids using NAD+ as the electron acceptor. The PADH activity was enhanced by several divalent cationic ions such as Mg2+, Ca2+, and Mn2+. On the other hand, it was inhibited by SH reagents (Hg 2+, p-chloromercuribenzoate, iodoacetamide, and N-ethylmaleinimide). The substrate specificity of the enzyme is compared with those of various aldehyde dehydrogenases.

Original languageEnglish
Pages (from-to)357-363
Number of pages7
JournalApplied Microbiology and Biotechnology
Volume76
Issue number2
DOIs
Publication statusPublished - 2007 Aug 1

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

Fingerprint Dive into the research topics of 'Purification and characterization of aldehyde dehydrogenase with a broad substrate specificity originated from 2-phenylethanol-assimilating Brevibacterium sp. KU1309'. Together they form a unique fingerprint.

  • Cite this