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

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dc.contributor.authorS Suwannarangsee-
dc.contributor.authorDoo-Byoung Oh-
dc.contributor.authorJeong Woo Seo-
dc.contributor.authorChul Ho Kim-
dc.contributor.authorS K Rhee-
dc.contributor.authorH A Kang-
dc.contributor.authorW Chulalaksananukul-
dc.contributor.authorOh Suk Kwon-
dc.date.accessioned2017-04-19T09:19:35Z-
dc.date.available2017-04-19T09:19:35Z-
dc.date.issued2010-
dc.identifier.issn0175-7598-
dc.identifier.uri10.1007/s00253-010-2752-7ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/9717-
dc.description.abstractThe 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 °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 gl-1. Taken together, our results suggest that optimization of ADH1 expression would be an ideal method for developing H. polymorpha into an efficient bioethanol production strain.-
dc.publisherSpringer-
dc.titleCharacterization of alcohol dehydrogenase 1 of the thermotolerant methylotrophic yeast Hansenula polymorpha-
dc.title.alternativeCharacterization of alcohol dehydrogenase 1 of the thermotolerant methylotrophic yeast Hansenula polymorpha-
dc.typeArticle-
dc.citation.titleApplied Microbiology and Biotechnology-
dc.citation.number2-
dc.citation.endPage507-
dc.citation.startPage497-
dc.citation.volume88-
dc.contributor.affiliatedAuthorDoo-Byoung Oh-
dc.contributor.affiliatedAuthorJeong Woo Seo-
dc.contributor.affiliatedAuthorChul Ho Kim-
dc.contributor.affiliatedAuthorOh Suk Kwon-
dc.contributor.alternativeNameSuwannarangsee-
dc.contributor.alternativeName오두병-
dc.contributor.alternativeName서정우-
dc.contributor.alternativeName김철호-
dc.contributor.alternativeName이상기-
dc.contributor.alternativeName강현아-
dc.contributor.alternativeNameChulalaksananuk-
dc.contributor.alternativeName권오석-
dc.identifier.bibliographicCitationApplied Microbiology and Biotechnology, vol. 88, no. 2, pp. 497-507-
dc.identifier.doi10.1007/s00253-010-2752-7-
dc.subject.keywordAlcohol dehydrogenaseADH1-
dc.subject.keywordEthanol production-
dc.subject.keywordGlycerol fermentation-
dc.subject.keywordHansenula polymorpha-
dc.subject.localAlcohol dehydrogenaseADH1-
dc.subject.localEthanol production-
dc.subject.localethanol production-
dc.subject.localGlycerol fermentation-
dc.subject.localHansenulapolymorpha-
dc.subject.localhansenula polymorpha-
dc.subject.localHansenula polymorpha-
dc.subject.localHansenula polymorpha (Pichia angusta)-
dc.description.journalClassY-
Appears in Collections:
Aging Convergence Research Center > 1. Journal Articles
Jeonbuk Branch Institute > Microbial Biotechnology Research Center > 1. Journal Articles
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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