首页    期刊浏览 2024年10月06日 星期日
登录注册

文章基本信息

  • 标题:Isolation and Mechanistic Characterization of a Novel Zearalenone-Degrading Enzyme
  • 本地全文:下载
  • 作者:Jian Ji ; Jian Yu ; Wei Xu
  • 期刊名称:Foods
  • 电子版ISSN:2304-8158
  • 出版年度:2022
  • 卷号:11
  • 期号:18
  • DOI:10.3390/foods11182908
  • 语种:English
  • 出版社:MDPI Publishing
  • 摘要: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 18H26O 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.
  • 关键词:zearalenone;enzyme;biodegradation;structural analysis
国家哲学社会科学文献中心版权所有