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Cloning and Characterization of Three Novel Enzymes Responsible for the Detoxification of Zearalenone

Zearalenone is a common mycotoxin contaminant in cereals that causes severe economic losses and serious risks to health of human and animals. Many strategies have been devised to degrade ZEN and keep food safe. The hydrolase ZHD101 from Clonostachys rosea, which catalyzes the hydrolytic degradation...

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Autores principales: Zhang, Yi, Liu, Xiaomeng, Zhang, Yunpeng, Zhang, Xiaolin, Huang, He
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8879097/
https://www.ncbi.nlm.nih.gov/pubmed/35202110
http://dx.doi.org/10.3390/toxins14020082
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author Zhang, Yi
Liu, Xiaomeng
Zhang, Yunpeng
Zhang, Xiaolin
Huang, He
author_facet Zhang, Yi
Liu, Xiaomeng
Zhang, Yunpeng
Zhang, Xiaolin
Huang, He
author_sort Zhang, Yi
collection PubMed
description Zearalenone is a common mycotoxin contaminant in cereals that causes severe economic losses and serious risks to health of human and animals. Many strategies have been devised to degrade ZEN and keep food safe. The hydrolase ZHD101 from Clonostachys rosea, which catalyzes the hydrolytic degradation of ZEN, has been studied widely. In the current research, three new enzymes that have the capacity to detoxify ZEN were identified, namely CLA, EXO, and TRI, showing 61%, 63%, and 97% amino acids identities with ZHD101, respectively. Three coding genes was expressed as heterologous in Escherichia coli BL21. Through biochemical analysis, the purified recombinant CLA, EXO, TRI, and ZHD101 exhibited high activities of degrading ZEN with the specific activity of 114.8 U/mg, 459.0 U/mg, 239.8 U/mg, and 242.8 U/mg. The optimal temperatures of CLA, EXO, TRI, and ZHD101 were 40 °C, 40 °C, 40 °C, and 45 °C, and their optimum pH were 7.0, 9.0, 9.5, and 9.0, respectively. Our study demonstrated that the novel enzymes CLA, EXO, and TRI possessed high ability to degrade ZEN from the model solutions and could be the promising candidates for ZEN detoxification in practical application.
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spelling pubmed-88790972022-02-26 Cloning and Characterization of Three Novel Enzymes Responsible for the Detoxification of Zearalenone Zhang, Yi Liu, Xiaomeng Zhang, Yunpeng Zhang, Xiaolin Huang, He Toxins (Basel) Article Zearalenone is a common mycotoxin contaminant in cereals that causes severe economic losses and serious risks to health of human and animals. Many strategies have been devised to degrade ZEN and keep food safe. The hydrolase ZHD101 from Clonostachys rosea, which catalyzes the hydrolytic degradation of ZEN, has been studied widely. In the current research, three new enzymes that have the capacity to detoxify ZEN were identified, namely CLA, EXO, and TRI, showing 61%, 63%, and 97% amino acids identities with ZHD101, respectively. Three coding genes was expressed as heterologous in Escherichia coli BL21. Through biochemical analysis, the purified recombinant CLA, EXO, TRI, and ZHD101 exhibited high activities of degrading ZEN with the specific activity of 114.8 U/mg, 459.0 U/mg, 239.8 U/mg, and 242.8 U/mg. The optimal temperatures of CLA, EXO, TRI, and ZHD101 were 40 °C, 40 °C, 40 °C, and 45 °C, and their optimum pH were 7.0, 9.0, 9.5, and 9.0, respectively. Our study demonstrated that the novel enzymes CLA, EXO, and TRI possessed high ability to degrade ZEN from the model solutions and could be the promising candidates for ZEN detoxification in practical application. MDPI 2022-01-21 /pmc/articles/PMC8879097/ /pubmed/35202110 http://dx.doi.org/10.3390/toxins14020082 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Zhang, Yi
Liu, Xiaomeng
Zhang, Yunpeng
Zhang, Xiaolin
Huang, He
Cloning and Characterization of Three Novel Enzymes Responsible for the Detoxification of Zearalenone
title Cloning and Characterization of Three Novel Enzymes Responsible for the Detoxification of Zearalenone
title_full Cloning and Characterization of Three Novel Enzymes Responsible for the Detoxification of Zearalenone
title_fullStr Cloning and Characterization of Three Novel Enzymes Responsible for the Detoxification of Zearalenone
title_full_unstemmed Cloning and Characterization of Three Novel Enzymes Responsible for the Detoxification of Zearalenone
title_short Cloning and Characterization of Three Novel Enzymes Responsible for the Detoxification of Zearalenone
title_sort cloning and characterization of three novel enzymes responsible for the detoxification of zearalenone
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8879097/
https://www.ncbi.nlm.nih.gov/pubmed/35202110
http://dx.doi.org/10.3390/toxins14020082
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