Multiple epoxide hydrolases in Alternaria alternata f. sp. lycopersici and their relationship to medium composition and host-specific toxin production

Christophe Morisseau, Barney L. Ward, David G. Gilchrist, Bruce D. Hammock

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)2388-2395
Number of pages8
JournalApplied and Environmental Microbiology
Volume65
Issue number6
StatePublished - Jun 1999

ASJC Scopus subject areas

  • Environmental Science(all)
  • Biotechnology
  • Microbiology

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