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KMID : 1094720120170061156
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Biotechnology and Bioprocess Engineering
2012 Volume.17 No. 6 p.1156 ~ p.1164
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Functions of membrane-bound alcohol dehydrogenase and aldehyde dehydrogenase in the bio-oxidation of alcohols in Gluconobacter oxydans DSM 2003
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Wei Liu-Jing
Zhou Ji-Lai
Zhu Dan-Ni
Cai Bai-Yi
Lin Jin-Ping
Hua Qiang
Wei Dong-Zhi
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Abstract
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In this study a new insight was provided to understand the functions of membrane-bound alcohol dehydrogenase (mADH) and aldehyde dehydrogenase (mALDH) in the bio-oxidation of primary alcohols, diols and poly alcohols using the resting cells of Gluconobacter oxydans DSM 2003 and its mutant strains as catalyst. The results demonstrated that though both mADH and mALDH participated in most of the oxidation of alcohols to their corresponding acid, the exact roles of these enzymes in each reaction might be different. For example, mADH played a key role in the oxidation of diols to its corresponding organic acid in G. oxydans, but it was dispensable when the primary alcohols were used as substrates. In contrast to mADH, mALDH appears to play a relatively minor role in organic acid-producing reactions because of the possible presence of other isoenzymes. Aldehydes were, however, found to be accumulated in the mALDH-deficient strain during the oxidation of alcohols.
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KEYWORD
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Gluconobacter oxydans, membrane-bound alcohol dehydrogenase, membrane-bound aldehyde dehydrogenase, oxidative alcohols
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