ArticleFoods (Basel, Switzerland)2022
Isolation and Mechanistic Characterization of a Novel Zearalenone-Degrading Enzyme.
Article in Foods (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- Peptidomics-based identification of endogenous free peptides fromFrontiers in pharmacology · 2026Article
- Advances in zearalenone-degrading enzymes research: characteristics, mining, improvement, and application.Journal of animal science and biotechnology · 2025Review
- Enzymatic detoxification of major mycotoxins: current status, challenges, and future prospective.Mycotoxin research · 2025Review
- Biodegradation of ZEN byFrontiers in microbiology · 2025Article
- Optimization of response surface methodology for the extraction of isoliquiritigenin fromFrontiers in pharmacology · 2025Article
- Bioenzymatic detoxification of mycotoxins.Frontiers in microbiology · 2024Review
- Mechanisms by which microbial enzymes degrade four mycotoxins and application in animal production: A review.Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2023Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
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(C18H26O4), 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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