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Cloning and characterization of an epoxide hydrolase-encoding gene from Rhodotorula glutinis

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Abstract

We cloned and characterized the epoxide hydrolase gene, EPH1, from Rhodotorula glutinis. The EPH1 open reading frame of 1230 bp was interrupted by nine introns and encoded a polypeptide of 409 amino acids with a calculated molecular mass of 46.3 kDa. The amino acid sequence was similar to that of microsomal epoxide hydrolase, which suggests that the epoxide hydrolase of R. glutinis also belongs to the α/β hydrolase fold family. EPH1 cDNA was expressed in Escherichia coli and resting cells showed a specific activity of 200 nmol min−1 (mg protein)−1 towards 1,2-epoxyhexane.

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Authors and Affiliations

  1. Division of Industrial Microbiology, Department of Food Technology and Nutritional Sciences, Wageningen University, P. O. Box 8129, 6700 EV Wageningen, The Netherlands e-mail: hans.visser@imb.ftns.wau.nl Tel.: +31-317-483393 Fax: +31-317-484978, , , , , , NL

    H. Visser, S. Vreugdenhil, J. A. M. de Bont & J. C. Verdoes

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  1. H. Visser
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  2. S. Vreugdenhil
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  3. J. A. M. de Bont
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  4. J. C. Verdoes
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Received: 2 August 1999 / Received revision: 4 October 1999 / Accepted: 10 October 1999

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Visser, H., Vreugdenhil, S., de Bont, J. et al. Cloning and characterization of an epoxide hydrolase-encoding gene from Rhodotorula glutinis . Appl Microbiol Biotechnol 53, 415–419 (2000). https://doi.org/10.1007/s002530051635

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  • DOI: https://doi.org/10.1007/s002530051635

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