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Applied and Environmental Microbiology, June 1999, p. 2388-2395, Vol. 65, No. 6
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Multiple Epoxide Hydrolases in Alternaria alternata f. sp. lycopersici and Their Relationship to Medium Composition and Host-Specific Toxin Production

Christophe Morisseau,1 Barney L. Ward,2 David G. Gilchrist,2 and Bruce D. Hammock1,*

Department of Entomology1 and Department of Plant Pathology,2 University of California, Davis, California 95616

Received 7 December 1998/Accepted 23 March 1999

The production of Alternaria alternata f. sp. lycopersici host-specific toxins (AAL toxins) and epoxide hydrolase (EH) activity were studied during the growth of this plant-pathogenic fungus in stationary liquid cultures. Media containing pectin as the primary carbon source displayed peaks of EH activity at day 4 and at day 12. When pectin was replaced by glucose, there was a single peak of EH activity at day 6. Partial characterization of the EH activities suggests the presence of three biochemically distinguishable EH activities. Two of them have a molecular mass of 25 kDa and a pI of 4.9, while the other has a molecular mass of 20 kDa and a pI of 4.7. Each of the EH activities can be distinguished by substrate preference and sensitivity to inhibitors. The EH activities present at day 6 (glucose) or day 12 (pectin) are concomitant with AAL toxin production.

* Corresponding author. Mailing address: Departments of Entomology and Environmental Toxicology, University of California, One Shields Ave., Davis, CA 95616. Phone: (530) 752-7519. Fax: (530) 752-1537. E-mail: bdhammock{at}ucdavis.edu.

Applied and Environmental Microbiology, June 1999, p. 2388-2395, Vol. 65, No. 6
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.




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