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Purification and some properties of a novel microbial lactate oxidase

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Abstract

 Geotrichum candidum was found to produce a lactate oxidase. The enzyme was purified by gel filtration and ion-exchange chromatography. The purified lactate oxidase showed a molecular mass of 50 kDa under denaturing and about 400 kDa under non-denaturing conditions. Transmission electron micro-scopy analysis confirmed an octameric structure. FMN was found to be a cofactor for this enzyme. Polarographic studies confirmed an oxygen uptake by the lactate oxidase. The enzyme showed specificity towards the L isomer of lactate and did not oxidise pyruvate, fumarate, succinate, maleate and ascorbate. It was stable at alkaline pH and also for 15 min at 45°C. The addition of glycerol and dextran 500 000 to the enzyme sample enhanced storage stability.

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Authors and Affiliations

  1. Gesellschaft für Biotechnologische Forschung, Mascheroder Weg 1, D-38124 Braunschweig, Germany. Fax: (0531) 6181 302 e-mail: HSZ@gbf-braunschweig.de , , , , , , DE

    H. Sztajer, W. Wang, H. Lünsdorf, A. Stocker & R. D. Schmid

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  1. H. Sztajer
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  2. W. Wang
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  3. H. Lünsdorf
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  4. A. Stocker
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  5. R. D. Schmid
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Received: 28 September 1995/Received revision: 10 January 1996/Accepted: 15 January 1996

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Sztajer, H., Wang, W., Lünsdorf, H. et al. Purification and some properties of a novel microbial lactate oxidase. Appl Microbiol Biotechnol 45, 600–606 (1996). https://doi.org/10.1007/s002530050736

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  • DOI: https://doi.org/10.1007/s002530050736

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