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Published online ahead of print on 21 April 2009 as doi:10.1099/mic.0.027201-0
Microbiology 2009;155:2078.

Microbiology (2009), DOI 10.1099/mic.0.027201-0
© 2009 Society for General Microbiology
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Microbiology 0 (2009), mic.0.027201; DOI  10.1099/mic.0.027201-0
© 2009 Society for General Microbiology

Two novel metal-independent long-chain alkyl-alcohol dehydrogenases from Geobacillus thermodenitrificans NG80-2

X. Liu, Y. Dong, J. Zhang, A. Zhang, L. Wang and L. Feng1

TEDA School of Biological Sciences and Biotechnology, Nankai University, Tianjin 300457, P. R. China

ABSTRACT

Two alkylalcohol dehydrogenase (ADH) genes from long-chain alkane-degrading Geobacillus thermodenitrificans NG80-2 were characterized in vitro. ADH1 and ADH2 were prepared heterologously in Escherichia coli as homooctameric and homodimeric protein respectively. Both ADHs can oxidize a broad range of alkylalcohols up to at least C30, as well as 1,3-propanediol and acetaldehyde. ADH1 also oxidizes glycerol, and ADH2 oxidizes isopropylalcohol, isoamylol, acetone, octanal and decanal. The most suitable substrate is ethanol for ADH1 and 1-octanol for ADH2. For either ADH, the optimum assay condition is at 60 °C and pH 8.0, and both NAD and NADP can be used as the cofactor. Sequence analysis reveals that ADH1 and ADH2 belong to Fe-containing/activated long-chain ADHs. However, the two enzymes contain neither Fe nor other metals, and Fe is not required for the activity, suggesting a new type of ADHs. The ADHs characterized are potentially useful in crude oil bioremediation and other bioconversion processes.

1 E-mail: fenglu63{at}nankai.edu.cn






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