Two novel metal-independent long-chain alkyl alcohol dehydrogenases from Geobacillus thermodenitrificans NG80-2-Reference-Cited by-同舟云学术

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

Published:2009-06-01 Issue:6 Volume:155 Page:2078-2085
ISSN:1350-0872
Container-title:Microbiology
language:en
Short-container-title:

Author:

Liu Xueqian¹²³,Dong Yanpeng¹²³,Zhang Jing¹²³,Zhang Aixiang¹²³,Wang Lei³⁴⁵¹²,Feng Lu⁴⁵¹²³

Affiliation:

1. Tianjin Research Center for Functional Genomics and Biochip, Tianjin 300457, PR China

2. Tianjin Key Laboratory of Microbial Functional Genomics, Tianjin 300457, PR China

3. TEDA School of Biological Sciences and Biotechnology, Nankai University, Tianjin 300457, PR China

4. The Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, PR China

5. The Engineering and Research Center for Microbial Functional Genomics and Detection Technology, Ministry of Education, PR China

Abstract

Two alkyl alcohol dehydrogenase (ADH) genes from the long-chain alkane-degrading strainGeobacillus thermodenitrificansNG80-2 were characterizedin vitro. ADH1 and ADH2 were prepared heterologously inEscherichia colias a homooctameric and a homodimeric protein, respectively. Both ADHs can oxidize a broad range of alkyl alcohols up to at least C30, as well as 1,3-propanediol and acetaldehyde. ADH1 also oxidizes glycerol, and ADH2 oxidizes isopropyl alcohol, isoamylol, acetone, octanal and decanal. The best substrate is ethanol for ADH1 and 1-octanol for ADH2. For both ADHs, 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 the 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 ADH. The ADHs characterized here are potentially useful in crude oil bioremediation and other bioconversion processes.

Publisher

Microbiology Society

Subject

Microbiology

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