Characterization of alcohol dehydrogenase from the haloalkaliphilic archaeon Natronomonas pharaonis

Yi Cao, Li Liao, Xue Wei Xu, Aharon Oren, Ce Wang, Xu Feng Zhu, Min Wu*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

23 Scopus citations


Alcohol dehydrogenase (ADH; EC: is a key enzyme in production and utilization of ethanol. In this study, the gene encoding for ADH of the haloalkaliphilic archaeon Natronomonas pharaonis (NpADH), which has a 1,068-bp open reading frame that encodes a protein of 355 amino acids, was cloned into the pET28b vector and was expressed in Escherichia coli. Then, NpADH was purified by Ni-NTA affinity chromatography. The recombinant enzyme showed a molecular mass of 41.3 kDa by SDS-PAGE. The enzyme was haloalkaliphilic and thermophilic, being most active at 5 M NaCl or 4 M KCl and 70°C, respectively. The optimal pH was 9.0. Zn2+ significantly inhibited activity. The Km value for acetaldehyde was higher than that for ethanol. It was concluded that the physiological role of this enzyme is likely the catalysis of the oxidation of ethanol to acetaldehyde.

Original languageAmerican English
Pages (from-to)471-476
Number of pages6
Issue number3
StatePublished - May 2008

Bibliographical note

Funding Information:
Acknowledgments This work was supported by the grants from the Major State Basic Research Development Program of China (973 Program) (Grant No. 2004CB719604-3) and the National Natural Science Foundation of China (Grant No. 30670048).


  • Alcohol dehydrogenase
  • Haloalkaliphilic
  • Molecular cloning
  • Natronomonas pharaonis


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