Protein Information

ID 1648
Name alcohol dehydrogenase 6
Synonyms ADH 6; ADH6; ADH6 protein; Alcohol dehydrogenase 6; alcohol dehydrogenase 6 (class V); ADH6 proteins; Alcohol dehydrogenase 6s; alcohol dehydrogenase 6 (class V)s

Compound Information

ID 724
Name furfural
CAS 2-furancarboxaldehyde

Reference

PubMed Abstract RScore(About this table)
18330568 Almeida JR, Roder A, Modig T, Laadan B, Liden G, Gorwa-Grauslund MF: NADH- vs NADPH-coupled reduction of 5-hydroxymethyl furfural (HMF) and its implications on product distribution in Saccharomyces cerevisiae. Appl Microbiol Biotechnol. 2008 Apr;78(6):939-45. Epub 2008 Mar 11.
Saccharomyces cerevisiae alcohol dehydrogenases responsible for NADH-, and NADPH-specific reduction of the furaldehydes 5-hydroxymethyl-furfural (HMF) and furfural have previously been identified. In the present study, strains overexpressing the corresponding genes (mut-ADH1 and ADH6), together with a control strain, were compared in defined medium for anaerobic fermentation of glucose in the presence and absence of HMF. All strains showed a similar fermentation pattern in the absence of HMF. In the presence of HMF, the strain overexpressing ADH6 showed the highest HMF reduction rate and the highest specific ethanol productivity, followed by the strain overexpressing mut-ADH1. This correlated with in vitro HMF reduction capacity observed in the ADH6 overexpressing strain. Acetate and glycerol yields per biomass increased considerably in the ADH6 strain. In the other two strains, only the overall acetate yield per biomass was affected. When compared in batch fermentation of spruce hydrolysate, strains overexpressing ADH6 and mut-ADH1 had five times higher HMF uptake rate than the control strain and improved specific ethanol productivity. Overall, our results demonstrate that (1) the cofactor usage in the HMF reduction affects the product distribution, and (2) increased HMF reduction activity results in increased specific ethanol productivity in defined mineral medium and in spruce hydrolysate.
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