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Isolation and Mechanistic Characterization of a Novel Zearalenone-Degrading Enzyme

Zearalenone (ZEN) and its derivatives pose a serious threat to global food quality and animal health. The use of enzymes to degrade mycotoxins has become a popular method to counter this threat. In this study, Aspergillus niger ZEN-S-FS10 extracellular enzyme solution with ZEN-degrading effect was s...

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Autores principales: Ji, Jian, Yu, Jian, Xu, Wei, Zheng, Yi, Zhang, Yinzhi, Sun, Xiulan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9498698/
https://www.ncbi.nlm.nih.gov/pubmed/36141036
http://dx.doi.org/10.3390/foods11182908
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author Ji, Jian
Yu, Jian
Xu, Wei
Zheng, Yi
Zhang, Yinzhi
Sun, Xiulan
author_facet Ji, Jian
Yu, Jian
Xu, Wei
Zheng, Yi
Zhang, Yinzhi
Sun, Xiulan
author_sort Ji, Jian
collection PubMed
description Zearalenone (ZEN) and its derivatives pose a serious threat to global food quality and animal health. The use of enzymes to degrade mycotoxins has become a popular method to counter this threat. In this study, Aspergillus niger ZEN-S-FS10 extracellular enzyme solution with ZEN-degrading effect was separated and purified to prepare the biological enzyme, FSZ, that can degrade ZEN. The degradation rate of FSZ to ZEN was 75–80% (pH = 7.0, 28 °C). FSZ can function in a temperature range of 28–38 °C and pH range of 2.0–7.0 and can also degrade ZEN derivatives (α-ZAL, β-ZOL, and ZAN). According to the enzyme kinetics fitting, ZEN has a high degradation rate. FSZ can degrade ZEN in real samples of corn flour. FSZ can be obtained stably and repeatedly from the original strain. One ZEN degradation product was isolated: FSZ−P(C(18)H26O(4)), with a relative molecular weight of 306.18 g/mol. Amino-acid-sequencing analysis revealed that FSZ is a novel enzyme (homology < 10%). According to the results of molecular docking, ZEN and ZAN can utilize their end-terminal carbonyl groups to bind FSZ residues PHE307, THR55, and GLU129 for a high-degradation rate. However, α-ZAL and β-ZOL instead contain hydroxyl groups that would prevent binding to GLU129; thus, the degradation rate is low for these derivatives.
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spelling pubmed-94986982022-09-23 Isolation and Mechanistic Characterization of a Novel Zearalenone-Degrading Enzyme Ji, Jian Yu, Jian Xu, Wei Zheng, Yi Zhang, Yinzhi Sun, Xiulan Foods Article Zearalenone (ZEN) and its derivatives pose a serious threat to global food quality and animal health. The use of enzymes to degrade mycotoxins has become a popular method to counter this threat. In this study, Aspergillus niger ZEN-S-FS10 extracellular enzyme solution with ZEN-degrading effect was separated and purified to prepare the biological enzyme, FSZ, that can degrade ZEN. The degradation rate of FSZ to ZEN was 75–80% (pH = 7.0, 28 °C). FSZ can function in a temperature range of 28–38 °C and pH range of 2.0–7.0 and can also degrade ZEN derivatives (α-ZAL, β-ZOL, and ZAN). According to the enzyme kinetics fitting, ZEN has a high degradation rate. FSZ can degrade ZEN in real samples of corn flour. FSZ can be obtained stably and repeatedly from the original strain. One ZEN degradation product was isolated: FSZ−P(C(18)H26O(4)), with a relative molecular weight of 306.18 g/mol. Amino-acid-sequencing analysis revealed that FSZ is a novel enzyme (homology < 10%). According to the results of molecular docking, ZEN and ZAN can utilize their end-terminal carbonyl groups to bind FSZ residues PHE307, THR55, and GLU129 for a high-degradation rate. However, α-ZAL and β-ZOL instead contain hydroxyl groups that would prevent binding to GLU129; thus, the degradation rate is low for these derivatives. MDPI 2022-09-19 /pmc/articles/PMC9498698/ /pubmed/36141036 http://dx.doi.org/10.3390/foods11182908 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
Ji, Jian
Yu, Jian
Xu, Wei
Zheng, Yi
Zhang, Yinzhi
Sun, Xiulan
Isolation and Mechanistic Characterization of a Novel Zearalenone-Degrading Enzyme
title Isolation and Mechanistic Characterization of a Novel Zearalenone-Degrading Enzyme
title_full Isolation and Mechanistic Characterization of a Novel Zearalenone-Degrading Enzyme
title_fullStr Isolation and Mechanistic Characterization of a Novel Zearalenone-Degrading Enzyme
title_full_unstemmed Isolation and Mechanistic Characterization of a Novel Zearalenone-Degrading Enzyme
title_short Isolation and Mechanistic Characterization of a Novel Zearalenone-Degrading Enzyme
title_sort isolation and mechanistic characterization of a novel zearalenone-degrading enzyme
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9498698/
https://www.ncbi.nlm.nih.gov/pubmed/36141036
http://dx.doi.org/10.3390/foods11182908
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