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Background  The strictly anaerobic, sulfate-reducing bacterium  Desulfococcus biacutus  can utilize acetone as sole carbon and energy source for growth. Whereas in aerobic and nitrate-reducing bacteria acetone is activated by carboxylation with CO 2  to acetoacetate,  D. biacutus  involves CO as a cosubstrate for acetone activation through a different, so far unknown pathway. Proteomic studies indicated that, among others, a predicted medium-chain dehydrogenase/reductase (MDR) superfamily, zinc-dependent alcohol dehydrogenase (locus tag DebiaDRAFT_04514) is specifically and highly produced during growth with acetone.    Results  The MDR gene DebiaDRAFT_04514 was cloned and overexpressed in  E. coli . The purified recombinant protein required zinc as cofactor, and accepted NADH/NAD +  but not NADPH/NADP +  as electron donor/acceptor. The pH optimum was at pH 8, and the temperature optimum at 45 °C. Highest specific activities were observed for reduction of C 3  - C 5 -aldehydes with NADH, such as propanal to propanol (380 ± 15 mU mg −1  protein), butanal to butanol (300 ± 24 mU mg −1 ), and 3-hydroxybutanal to 1,3-butanediol (248 ± 60 mU mg −1 ), however, the enzyme also oxidized 3-hydroxybutanal with NAD +  to acetoacetaldehyde (83 ± 18 mU mg −1 ).    Conclusion  The enzyme might play a key role in acetone degradation by  D. biacutus , for example as a bifunctional 3-hydroxybutanal dehydrogenase/reductase. Its recombinant production may represent an important step in the elucidation of the complete degradation pathway.    Electronic supplementary material  The online version of this article (doi:10.1186/s12866-016-0899-9) contains supplementary material, which is available to authorized users.

bmc microbiology

Cloning, functional expression and characterization of a bifunctional 3-hydroxybutanal dehydrogenase /reductase involved in acetone metabolism by Desulfococcus biacutus