Characterization of alcohol dehydrogenase 1 of the thermotolerant methylotrophic yeast Hansenula polymorpha

Applied Microbiology and Biotechnology
Surisa SuwannarangseeOhsuk Kwon

Abstract

The thermotolerant methylotrophic yeast Hansenula polymorpha has recently been gaining interest as a promising host for bioethanol production due to its ability to ferment xylose, glucose, and cellobiose at elevated temperatures up to 48 degrees C. In this study, we identified and characterized alcohol dehydrogenase 1 of H. polymorpha (HpADH1). HpADH1 seems to be a cytoplasmic protein since no N-terminal mitochondrial targeting extension was detected. Compared to the ADHs of other yeasts, recombinant HpADH1 overexpressed in Escherichia coli exhibited much higher catalytic efficiency for ethanol oxidation along with similar levels of acetaldehyde reduction. HpADH1 showed broad substrate specificity for alcohol oxidation but had an apparent preference for medium chain length alcohols. Both ADH isozyme pattern analysis and ADH activity assay indicated that ADH1 is the major ADH in H. polymorpha DL-1. Moreover, an HpADH1-deleted mutant strain produced less ethanol in glucose or glycerol media compared to wild-type. Interestingly, when the ADH1 mutant was complemented with an HpADH1 expression cassette, the resulting strain produced significantly increased amounts of ethanol compared to wild-type, up to 36.7 g l(-1). Taken together,...Continue Reading

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Citations

Jan 18, 2012·Applied Microbiology and Biotechnology·Surisa SuwannarangseeOhsuk Kwon
Feb 6, 2013·Bioprocess and Biosystems Engineering·Oh Cheol KimOhsuk Kwon
Nov 3, 2010·Journal of Biotechnology·Jessica SchneiderAlexander Goesmann
Dec 25, 2015·Fungal Genetics and Biology : FG & B·James M Wagner, Hal S Alper
Apr 28, 2017·Journal of Experimental Botany·Tessa MosesAlain Goossens

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