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Purification and characterization of the enzymes from Brevundimonas naejangsanensis that degrade ochratoxin A and B.
Peng, Mengxue; Zhang, Zhenzhen; Xu, Xinge; Zhang, Haoxiang; Zhao, Zitong; Liang, Zhihong.
Afiliación
  • Peng M; College of Food Science and Nutritional Engineering, China Agricultural University, Beijing, China.
  • Zhang Z; College of Food Science and Nutritional Engineering, China Agricultural University, Beijing, China.
  • Xu X; College of Food Science and Nutritional Engineering, China Agricultural University, Beijing, China.
  • Zhang H; College of Food Science and Nutritional Engineering, China Agricultural University, Beijing, China.
  • Zhao Z; College of Food Science and Nutritional Engineering, China Agricultural University, Beijing, China.
  • Liang Z; College of Food Science and Nutritional Engineering, China Agricultural University, Beijing, China; The Supervision, Inspection and Testing Center of Genetically Modified Organisms, Ministry of Agriculture, Beijing, China; Beijing Laboratory for Food Quality and Safety, College of Food Science and N
Food Chem ; 419: 135926, 2023 Sep 01.
Article en En | MEDLINE | ID: mdl-37011575
ABSTRACT
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 OTα and hydrolyzed OTB into OTß. BnOTase1, BnOTase2, BnOTase3, and BnOTase4 have the apparent Km values for hydrolyzing OTA of 19.38, 0.92, 12.11, 1.09 µmol/L and for hydrolyzing OTB of 0.76, 2.43, 0.60, 0.64 µmol/L respectively. OTα and OTß 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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Texto completo: 1 Base de datos: MEDLINE Asunto principal: Ocratoxinas Idioma: En Revista: Food Chem Año: 2023 Tipo del documento: Article

Texto completo: 1 Base de datos: MEDLINE Asunto principal: Ocratoxinas Idioma: En Revista: Food Chem Año: 2023 Tipo del documento: Article