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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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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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. |
format | Online Article Text |
id | pubmed-8879097 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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