4.7 Article

Characterization of a broad-range aldehyde dehydrogenase involved in alkane degradation in Geobacillus thermodenitrificans NG80-2

Journal

MICROBIOLOGICAL RESEARCH
Volume 165, Issue 8, Pages 706-712

Publisher

ELSEVIER GMBH, URBAN & FISCHER VERLAG
DOI: 10.1016/j.micres.2010.01.006

Keywords

Geobacillus thermodenitrificans NG80-2; Aldehyde dehydrogenase; Aliphatic aldehydes; Aromatic aldehydes

Categories

Funding

  1. Chinese National Science Fund for Distinguished Young Scholars [30788001]
  2. National 863 program of China [2007AA02Z106, 2007AA021303]
  3. Tianjin Municipal Science and Technology Committee [06YFJZJC02200]

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An aldehyde dehydrogenase (ALDH) involved in alkane degradation in crude oil-degrading Geobacillus thermodenitrificans NG80-2 was characterized in vitro. The ALDH was expressed heterologously in Escherichia coli and purified as a His-tagged homotetrameric protein with a subunit of 57 kDa based on SDS-PAGE and Native-PAGE analysis. The purified ALDH-oxidized alkyl aldehydes ranging from formaldehyde (C-1) to eicosanoic aldehyde (C-20) with the highest activity on C-1. It also oxidized several aromatic aldehydes including benzaldehyde, phenylacetaldehyde, o-chloro-benzaldehyde and o-phthalaldehyde. The ALDH uses only NAD(+) as the cofactor, and has no reductive activity on acetate or hexadecanoic acid. Therefore, it is an irreversible NAD(+)-dependent aldehyde dehydrogenase. Kinetic parameters, temperature and pH optimum of the enzyme, and effects of metal ions, EDTA and Triton X-100 on the enzyme activity were investigated. Physiological roles of the ALDH for the survival of NG80-2 in oil reservoirs are discussed. (C) 2010 Elsevier GmbH. All rights reserved.

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