Halophile aldehyde dehydrogenase from Halobacterium salinarum

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

Research output: Contribution to journalArticle

3 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 1

Fingerprint

Halobacterium salinarum
Aldehyde Dehydrogenase
Archaea
Enzyme activity
Enzymes
Proteome
Carboxylic Acids
Metabolism
Aldehydes
Proteomics
Escherichia coli
Industry
Proteins
Salts
Genes
Polymerase Chain Reaction
Oxidation

Keywords

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

ASJC Scopus subject areas

  • Genetics
  • Biotechnology
  • Biochemistry

Cite this

Halophile aldehyde dehydrogenase from Halobacterium salinarum. / Kim, Hyo Jeong; Joo, Won A.; Cho, Chang Won; Kim, Chan Wha.

In: Journal of Proteome Research, Vol. 5, No. 1, 01.01.2006, p. 192-195.

Research output: Contribution to journalArticle

Kim, Hyo Jeong ; Joo, Won A. ; Cho, Chang Won ; Kim, Chan Wha. / Halophile aldehyde dehydrogenase from Halobacterium salinarum. In: Journal of Proteome Research. 2006 ; Vol. 5, No. 1. pp. 192-195.
@article{f66a06f2ff804c6fbf4469bf5716e5a3,
title = "Halophile aldehyde dehydrogenase from Halobacterium salinarum",
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.",
keywords = "2-DE, ALDH, ESI-Q TOF mass spectrometry, H. salinarum, MALDI-TOF",
author = "Kim, {Hyo Jeong} and Joo, {Won A.} and Cho, {Chang Won} and Kim, {Chan Wha}",
year = "2006",
month = "1",
day = "1",
doi = "10.1021/pr050258u",
language = "English",
volume = "5",
pages = "192--195",
journal = "Journal of Proteome Research",
issn = "1535-3893",
publisher = "American Chemical Society",
number = "1",

}

TY - JOUR

T1 - Halophile aldehyde dehydrogenase from Halobacterium salinarum

AU - Kim, Hyo Jeong

AU - Joo, Won A.

AU - Cho, Chang Won

AU - Kim, Chan Wha

PY - 2006/1/1

Y1 - 2006/1/1

N2 - 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.

AB - 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.

KW - 2-DE

KW - ALDH

KW - ESI-Q TOF mass spectrometry

KW - H. salinarum

KW - MALDI-TOF

UR - http://www.scopus.com/inward/record.url?scp=30744449010&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=30744449010&partnerID=8YFLogxK

U2 - 10.1021/pr050258u

DO - 10.1021/pr050258u

M3 - Article

C2 - 16396511

AN - SCOPUS:30744449010

VL - 5

SP - 192

EP - 195

JO - Journal of Proteome Research

JF - Journal of Proteome Research

SN - 1535-3893

IS - 1

ER -