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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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Abstract

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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Authors and Affiliations

  1. State Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, Shanghai, 200-237, China

    Liu-Jing Wei, Jin-Ping Lin & Dong-Zhi Wei

  2. State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, 200-237, China

    Ji-lai Zhou, Dan-ni Zhu, Bai-yi Cai & Qiang Hua

Authors
  1. Liu-Jing Wei
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  2. Ji-lai Zhou
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  3. Dan-ni Zhu
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  4. Bai-yi Cai
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  5. Jin-Ping Lin
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  6. Qiang Hua
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  7. Dong-Zhi Wei
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Correspondence to Qiang Hua or Dong-Zhi Wei.

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Wei, LJ., Zhou, Jl., Zhu, Dn. et al. Functions of membrane-bound alcohol dehydrogenase and aldehyde dehydrogenase in the bio-oxidation of alcohols in Gluconobacter oxydans DSM 2003. Biotechnol Bioproc E 17, 1156–1164 (2012). https://doi.org/10.1007/s12257-012-0339-0

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  • DOI: https://doi.org/10.1007/s12257-012-0339-0

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