Detailed Information

Cited 17 time in webofscience Cited 0 time in scopus
Metadata Downloads

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

Authors
Suwannarangsee, SurisaOh, Doo-ByoungSeo, Jeong-WooKim, Chul HoRhee, Sang KiKang, Hyun AhChulalaksananukul, WarawutKwon, Ohsuk
Issue Date
Sep-2010
Publisher
SPRINGER
Keywords
Alcohol dehydrogenase; ADH1; Hansenula polymorpha; Ethanol production; Glycerol fermentation
Citation
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, v.88, no.2, pp 497 - 507
Pages
11
Journal Title
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume
88
Number
2
Start Page
497
End Page
507
URI
https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/22248
DOI
10.1007/s00253-010-2752-7
ISSN
0175-7598
1432-0614
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 A 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, our results suggest that optimization of ADH1 expression would be an ideal method for developing H. polymorpha into an efficient bioethanol production strain.
Files in This Item
There are no files associated with this item.
Appears in
Collections
College of Natural Sciences > Department of Life Science > 1. Journal Articles

qrcode

Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.

Related Researcher

Researcher Kang, Hyun Ah photo

Kang, Hyun Ah
자연과학대학 (생명과학과)
Read more

Altmetrics

Total Views & Downloads

BROWSE