4.7 Article

Purification and characterization of the enzymes from Brevundimonas naejangsanensis that degrade ochratoxin A and B

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FOOD CHEMISTRY
卷 419, 期 -, 页码 -

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ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2023.135926

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Ochratoxin A; Ochratoxin B; Brevundimonas naejangsanensis; Peptidase; Amidase; Biodegradation

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In this study, four novel OTA and OTB degrading enzymes, BnOTase1, BnOTase2, BnOTase3, and BnOTase4, were purified from the metabolites of Brevundimonas naejangsanensis ML17 strain. These enzymes hydrolyzed OTA into OT alpha and OTB into OT beta. They showed no significant cytotoxicity to HEK293 cells, suggesting their potential in mitigating the toxicity of OTA and OTB.
Ochratoxin A (OTA) and Ochratoxin B (OTB) co-contaminate many types of agricultural products. Screening enzymes that degrade both OTA and OTB has significance in food safety. In this study, four novel OTA and OTB degrading enzymes, namely BnOTase1, BnOTase2, BnOTase3, and BnOTase4, were purified from the metabolites of the Brevundimonas naejangsanensis ML17 strain. These four enzymes hydrolyzed OTA into OT alpha and hydrolyzed OTB into OT beta.BnOTase1,BnOTase2,BnOTase3, and BnOTase4 have the apparent Km values for hydrolyzing OTA of 19.38, 0.92, 12.11, 1.09 mu mol/L and for hydrolyzing OTB of 0.76, 2.43, 0.60, 0.64 mu mol/L respectively. OT alpha and OT beta showed no significant cytotoxicity to HEK293 cells, suggesting that these enzymes mitigate the toxicity of OTA and OTB. The discovery of the novel OTA and OTB degrading enzymes enriches the research on ochratoxin control and provides objects for protein rational design.

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