{"title":"芳香密菇3J2MO降解黄曲霉毒素B1的研究","authors":"Xue Wang, Yao-Yao Gao, Dun Wang, Qi Zhang, Hao-Ran Wang, Ting-Ting Zhang, Meng-Jie Zhu, Jing Dong, Dong Ling, Peng Feng, Xue-Hui Tang, Pei-Wu Li","doi":"10.3390/biology14060724","DOIUrl":null,"url":null,"abstract":"<p><p>To address the issue of aflatoxin contamination, which poses a significant threat to food safety and human health, we have conducted extensive research. We have isolated a strain of <i>Myroides odoratimimus</i> (3J2MO) from the soil that exhibited remarkable efficiency in degrading various aflatoxin types, including AFB1, AFB2, AFG1, AFG2, and AFM1. SDS-PAGE analysis confirmed the purity of the enzymes to be over 95%. Through fluorescence assays, we quantified the enzymatic activity, with an AFB1 degradation rate of 95% achieved at 37 °C and a pH of 8.0. Further analysis using HPLC-MS/MS identified the degradation intermediates, revealing the mechanisms of lactone ring cleavage and epoxy group hydrolysis. GO/COG/KEGG annotations provided insights into the functions of these enzymes, with peroxidase linked to reactive oxygen species (ROS) generation and helicase associated with ATP-dependent conformational changes. Helicase, on the other hand, hydrolyzes ATP, driving conformational changes in AFB1 and facilitating its breakdown into non-toxic metabolites. The potential industrial-scale application of this discovery could significantly mitigate aflatoxin-related economic losses while minimizing chemical residues in the food chain.</p>","PeriodicalId":48624,"journal":{"name":"Biology-Basel","volume":"14 6","pages":""},"PeriodicalIF":3.6000,"publicationDate":"2025-06-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12189741/pdf/","citationCount":"0","resultStr":"{\"title\":\"Study on the Degradation of Aflatoxin B1 by <i>Myroides odoratimimus</i> 3J2MO.\",\"authors\":\"Xue Wang, Yao-Yao Gao, Dun Wang, Qi Zhang, Hao-Ran Wang, Ting-Ting Zhang, Meng-Jie Zhu, Jing Dong, Dong Ling, Peng Feng, Xue-Hui Tang, Pei-Wu Li\",\"doi\":\"10.3390/biology14060724\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>To address the issue of aflatoxin contamination, which poses a significant threat to food safety and human health, we have conducted extensive research. We have isolated a strain of <i>Myroides odoratimimus</i> (3J2MO) from the soil that exhibited remarkable efficiency in degrading various aflatoxin types, including AFB1, AFB2, AFG1, AFG2, and AFM1. SDS-PAGE analysis confirmed the purity of the enzymes to be over 95%. Through fluorescence assays, we quantified the enzymatic activity, with an AFB1 degradation rate of 95% achieved at 37 °C and a pH of 8.0. Further analysis using HPLC-MS/MS identified the degradation intermediates, revealing the mechanisms of lactone ring cleavage and epoxy group hydrolysis. GO/COG/KEGG annotations provided insights into the functions of these enzymes, with peroxidase linked to reactive oxygen species (ROS) generation and helicase associated with ATP-dependent conformational changes. Helicase, on the other hand, hydrolyzes ATP, driving conformational changes in AFB1 and facilitating its breakdown into non-toxic metabolites. The potential industrial-scale application of this discovery could significantly mitigate aflatoxin-related economic losses while minimizing chemical residues in the food chain.</p>\",\"PeriodicalId\":48624,\"journal\":{\"name\":\"Biology-Basel\",\"volume\":\"14 6\",\"pages\":\"\"},\"PeriodicalIF\":3.6000,\"publicationDate\":\"2025-06-19\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12189741/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biology-Basel\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.3390/biology14060724\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biology-Basel","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.3390/biology14060724","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOLOGY","Score":null,"Total":0}
Study on the Degradation of Aflatoxin B1 by Myroides odoratimimus 3J2MO.
To address the issue of aflatoxin contamination, which poses a significant threat to food safety and human health, we have conducted extensive research. We have isolated a strain of Myroides odoratimimus (3J2MO) from the soil that exhibited remarkable efficiency in degrading various aflatoxin types, including AFB1, AFB2, AFG1, AFG2, and AFM1. SDS-PAGE analysis confirmed the purity of the enzymes to be over 95%. Through fluorescence assays, we quantified the enzymatic activity, with an AFB1 degradation rate of 95% achieved at 37 °C and a pH of 8.0. Further analysis using HPLC-MS/MS identified the degradation intermediates, revealing the mechanisms of lactone ring cleavage and epoxy group hydrolysis. GO/COG/KEGG annotations provided insights into the functions of these enzymes, with peroxidase linked to reactive oxygen species (ROS) generation and helicase associated with ATP-dependent conformational changes. Helicase, on the other hand, hydrolyzes ATP, driving conformational changes in AFB1 and facilitating its breakdown into non-toxic metabolites. The potential industrial-scale application of this discovery could significantly mitigate aflatoxin-related economic losses while minimizing chemical residues in the food chain.
期刊介绍:
Biology (ISSN 2079-7737) is an international, peer-reviewed, quick-refereeing open access journal of Biological Science published by MDPI online. It publishes reviews, research papers and communications in all areas of biology and at the interface of related disciplines. Our aim is to encourage scientists to publish their experimental and theoretical results in as much detail as possible. There is no restriction on the length of the papers. The full experimental details must be provided so that the results can be reproduced. Electronic files regarding the full details of the experimental procedure, if unable to be published in a normal way, can be deposited as supplementary material.