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Purification and kinetic characteristics of pyruvate decarboxylase and ethanol dehydrogenase from Zymomonas mobilis in relation to ethanol production

  • Biotechnology
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Summary

Alcohol dehydrogenase (EC 1.1.1.1) and pyruvate decarboxylase (EC 4.1.1.1) from Zymomonas mobilis were partially purified and characterized. Alcohol dehydrogenase exhibits a pH optimum at 6.5 and pyruvate decarboxylase a major peak at pH 6.0 and a minor one at pH 4.3. The molecular weights were estimated to be 147,300±14,700 and 219,700±20,400 daltons, respectively. Both enzymes exhibit hyperbolic saturation curves with their respective substrates. Whereas alcohol dehydrogenase was inhibited by ethanol (Ki=6.86×10−4 M) and NAD+ (Ki=1.44×10−4 M), no inhibition was observed with pyruvate decarboxylase at similar concentrations of ethanol. Neither of the enzymes responded to sulphydryl-binding reagents, but differed in their response to a number of divalent metals. The results are compared with those of the respective enzymes from yeast and discussed with a view towards ethanol production limitations by Zymomonas mobilis.

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  1. Department of Microbiology, University of Queensland, 4067, St. Lucia, Qld., Australia

    Toni C. Hoppner & Horst W. Doelle

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  1. Toni C. Hoppner
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  2. Horst W. Doelle
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Hoppner, T.C., Doelle, H.W. Purification and kinetic characteristics of pyruvate decarboxylase and ethanol dehydrogenase from Zymomonas mobilis in relation to ethanol production. European J. Appl. Microbiol. Biotechnol. 17, 152–157 (1983). https://doi.org/10.1007/BF00505880

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