Degradation of the minor Fusarium mycotoxin beauvericin by intracellular enzymes of Saccharomyces cerevisiae

Beauvericin (BEA) is a cyclic depsipeptide with antibiotic and insecticidal effects. It was discovered for the first time from the fungus Beauveria bassiana, but more significantly, is produced by several Fusarium strains, and considered a contaminant of several cereals like corn, wheat and barley. tudy investigated the degradation of BEA by intracellular raw enzymes of four strains of Saccharomyces cerevisiae, named LO9, YE5, A34, and A17. The BEA at 25 mg/kg in a model solution and in corn flour was co-incubated with the raw enzymes from the four yeast strains, respectively. The reduction of BEA was evaluated using liquid chromatography coupled to a diode array detector (LC–DAD); the products formed during the co-incubation were determined by liquid chromatography coupled to mass spectrometry-linear ion trap (LC–MS-LIT). In model solution BEA reduction ranged from 83 to 100%. In corn flour treated with the intracellular raw enzymes, the BEA degradation was from 66 to 91%. A product resulted from the BEA degradation was identified.