Journal
YEAST
Volume 25, Issue 3, Pages 191-198Publisher
JOHN WILEY & SONS LTD
DOI: 10.1002/yea.1578
Keywords
alcohol dehydrogenase; 5-hydroxymethylfurfural; detoxification; lignocellulosic hydrolysates
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We report on the identification and characterization of a mutated alcohol dehydrogenase I from the industrial Saccharomyces cerevisiae strain TMB3000 that mediates the NADII-dependent reduction of 5-hydroxymethyllfurfural (HMF) to 2,5-bis-hydroxymethylfuran. The co-factor preference distinguished this alcohol dehydrogenase from the previously reported NADPH-dependent S. cerevisiae HMF alcohol dehydrogenase Adh6. The amino acid sequence revealed three novel mutations (S109P, L116S and Y294C) that were all predicted at the vicinity of the substrate binding site, which could explain the unusual substrate specificity. Increased biomass production and HMF conversion rate were achieved in a CEN.PK S. cerevisiae strain overexpressing the mutated ADHI gene. Copyright (c) 2008 John Wiley & Sons, Ltd.
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