4.7 Article

Characterization of Two Dehydrogenases from Gluconobacter oxydans Involved in the Transformation of Patulin to Ascladiol

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TOXINS
卷 14, 期 7, 页码 -

出版社

MDPI
DOI: 10.3390/toxins14070423

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mycotoxin; patulin; ascladiol; Gluconobacter oxydans; detoxification; enzyme; dehydrogenase

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  1. Agriculture and Agri-Food Canada (AAFC) [AAFC J-002250]

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Patulin is a mycotoxin that contaminates apples and apple products, but can be transformed into E-ascladiol by extracts from Gluconobacter oxydans ATCC 621. The identification and characterization of enzymes involved in the transformation provide insights into their potential application for patulin detoxification.
Patulin is a mycotoxin that primarily contaminate apples and apple products. Whole cell or cell-free extracts of Gluconobacter oxydans ATCC 621 were able to transform patulin to E-ascladiol. Proteins from cell-free extracts were separated by anion exchange chromatography and fractions with patulin transformation activity were subjected to peptide mass fingerprinting, enabling the identification of two NADPH dependent short chain dehydrogenases, GOX0525 and GOX1899, with the requisite activity. The genes encoding these enzymes were expressed in E. coli and purified. Kinetic parameters for patulin reduction, as well as pH profiles and thermostability were established to provide further insight on the potential application of these enzymes for patulin detoxification.

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