Halophile aldehyde dehydrogenase from Halobacterium salinarum

Hyo Jeong Kim, Won A. Joo, Chang Won Cho, Chan Wha Kim

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Halobacterium salinarum is a member of the halophilic archaea. In the present study, H. salinarum was cultured at various NaCl concentrations (3.5, 4.3, and 6.0 M NaCl), and its proteome was determined and identificated via proteomics technique. We detected 14 proteins which were significantly down-regulated in 3.5 M and/or 6 M NaCl. Among the identified protein spots, aldehyde dehydrogenase (ALDH) was selected for evaluation with regard to its potential applications in industry. The most effective metabolism function exhibited by ALDH is the oxidation of aldehydes to carboxylic acids. The ALDH gene from H. salinarum (1.5 kb fragment) was amplified by PCR and cloned into the E. coli strain, BL21 (DE3), with the pGEX-KG vector. We subsequently analyzed the enzyme activity of the recombinant ALDH (54 kDa) at a variety of salt concentrations. The purified recombinant ALDH from H. salinarum exhibited the most pronounced activity at 1 M NaCl. Therefore, the ALDH from H. salinarum is a halophilic enzyme, and may prove useful for applications in hypersaline environments.

Original languageEnglish
Pages (from-to)192-195
Number of pages4
JournalJournal of Proteome Research
Volume5
Issue number1
DOIs
Publication statusPublished - 2006 Jan

Keywords

  • 2-DE
  • ALDH
  • ESI-Q TOF mass spectrometry
  • H. salinarum
  • MALDI-TOF

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry(all)

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