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Construction and characterization of fermentative lactate dehydrogenase Escherichia coli mutant and its potential for bacterial hydrogen production

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Abstract

In Escherichia coli, classified as a mixed-acid producer in fermentation, D-lactate is one of the final metabolites from pyruvate. In order to achieve a high efficiency of bacterial hydrogen production from glucose, we have constructed an E. coli strain deficient in fermentative lactate dehydrogenase (LDH-A) by P1 transduction. The mutant, designated as MC13-4, entirely lost LDH-A activity while retaining whole formate hydrogenlyase activity. This mutation resulted in an increase in hydrogen production based on glucose consumed. The effect of uptake hydrogenases on the hydrogen production was also discussed.

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Authors and Affiliations

  1. Department of Biotechnology, Tokyo University of Agriculture and Technology, 2-24-16 Nakamachi, Koganei, 184-8588, Tokyo, Japan

    Koji Sode, Mika Watanabe & Hiroshi Makimoto

  2. National Institute of Agrobiological Resources, Kannondai, Tsukuba-city, Ibaraki, Japan

    Masamitsu Tomiyama

Authors
  1. Koji Sode
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  2. Mika Watanabe
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  3. Hiroshi Makimoto
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  4. Masamitsu Tomiyama
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Correspondence to Koji Sode.

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Sode, K., Watanabe, M., Makimoto, H. et al. Construction and characterization of fermentative lactate dehydrogenase Escherichia coli mutant and its potential for bacterial hydrogen production. Appl Biochem Biotechnol 77, 317–323 (1999). https://doi.org/10.1385/ABAB:77:1-3:317

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  • DOI: https://doi.org/10.1385/ABAB:77:1-3:317

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