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Substrate specificity and stereoselectivity of fatty alcohol oxidase from the yeast Candida maltosa

  • Biochemical Engineering
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Summary

In Candida maltosa and other alkene-utilizing yeasts a membrane-bound fatty alcohol oxidase (FAOD) is induced by growth on n-alkenes. The oxidation of 1-alkanols to the corresponding aldehydes is accompanied by the stoichiometric consumption of 1 mol O2 and formation of 1 mol hydrogen peroxide (H2O2). The FAOD of C. maltosa shows a broad substrate specificity. It catalyses the oxidation of 1-alkanols (C4 to C22), with a maximal activity of 1.85 gmmol H2O2/ min × mg protein for 1-octanol, as well as the transformation of 2-alkanols (C8 to C16) to ketones. Other compounds as α,ω-alkenediols, ω-hydroxypalmitic acid, phenylalkanols and terpene alcohols are substrates for the enzyme, although mostly with decreased activities. The oxidation of the racemic 2-alkanols by the FAOD proceeds with very high stereoselectivity for the R(−)-enatiomers only, leaving the S(+)-2-alkanol untouched.

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Author notes

  1. Stephan Mauersberger, Hannelore Drechsler, Günther Oehme & Hans-Georg Müller

    Present address: Max Delbrück Centre, for Molecular Medicine, Robert-Rössle-Straβe 10, O-1115, Berlin-Buch, FRG

Authors and Affiliations

  1. Department of Enzymology, Central Institute of Molecular Biology, Robert-Rössle-Strasse 10, O-1115, Berlin-Buch, Federal Republic of Germany

    Stephan Mauersberger, Hannelore Drechsler & Hans-Georg Müller

  2. Division of Complex Catalysis, Central Institute of Organic Chemistry, Buchbinder-Strasse 5-6, O-2500, Rostock, Federal Republic of Germany

    Günther Oehme

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  1. Stephan Mauersberger
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  2. Hannelore Drechsler
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  3. Günther Oehme
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  4. Hans-Georg Müller
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Mauersberger, S., Drechsler, H., Oehme, G. et al. Substrate specificity and stereoselectivity of fatty alcohol oxidase from the yeast Candida maltosa . Appl Microbiol Biotechnol 37, 66–73 (1992). https://doi.org/10.1007/BF00174205

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  • DOI: https://doi.org/10.1007/BF00174205

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