Metabolism and Toxicology of Mycotoxins and Their Masked Forms: 2nd Edition

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Mycotoxins".

Deadline for manuscript submissions: 31 August 2026 | Viewed by 1184

Special Issue Editors


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Guest Editor
State Key Laboratory of Animal Nutrition, College of Animal Science and Technology, China Agricultural University, Beijing 100193, China
Interests: mycotoxin bio-degradation; mycotoxin detoxification; feed-food safety; molecular toxicology of dietary mycotoxins
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Guest Editor
Beijing Laboratory for Food Quality and Safety, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China
Interests: mycotoxin; microbiology; food nutrition; food safety
Special Issues, Collections and Topics in MDPI journals

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Guest Editor
School of Life Science, Shanxi University, Taiyuan 030006, China
Interests: mycotoxins; degradation of mycotoxins; detection
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Following on from the first Special Issue, this Special Issue, “Metabolism and Toxicology of Mycotoxins and Their Masked Forms: 2nd Edition”, will continue to focus on the most recent research on the development of metabolic transformation mechanisms and toxicity of masked mycotoxins and to propose new strategies for evaluation and/or reducing mycotoxin contamination.

In this Special Issue, we welcome all submissions related to the following topics: (1) the metabolic transformation mechanism of mycotoxins, especially masked mycotoxins, and work implementing an omics approach to understanding the mechanism; (2) in vitro and in vivo toxicology and the metabolics of emerging or masked mycotoxins; and (3) the accurate evaluation of the interactive toxic effects of mycotoxins and/or their masked forms on humans or animals.

Prof. Dr. Qiugang Ma
Prof. Dr. Zhihong Liang
Prof. Dr. Ru Jia
Guest Editors

Manuscript Submission Information

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Keywords

  • masked mycotoxins
  • metabolic transformation mechanism
  • toxicology
  • interactive effects
  • oxidative stress
  • DNA damage
  • cell apoptosis

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Published Papers (1 paper)

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Research

17 pages, 1786 KB  
Article
Genome-Guided Identification of an OTA-Degrading Amidohydrolase AMH2102 from Acinetobacter kookii AK4 with Enhanced Soluble Expression in Escherichia coli
by Zehui Niu, Shengyue Bai, Yuyun Xiao, Jingran Lai, Yuxin Jin, Zitong Zhao, Yan Yang, Shujuan Cun and Zhihong Liang
Toxins 2026, 18(2), 101; https://doi.org/10.3390/toxins18020101 - 16 Feb 2026
Viewed by 685
Abstract
Ochratoxin A (OTA) is a globally distributed mycotoxin that poses serious threats to food safety and human health due to its nephrotoxic, hepatotoxic, and carcinogenic properties. Previous enzymatic detoxification strategies for OTA have been constrained by low degradation efficiency or poor soluble expression [...] Read more.
Ochratoxin A (OTA) is a globally distributed mycotoxin that poses serious threats to food safety and human health due to its nephrotoxic, hepatotoxic, and carcinogenic properties. Previous enzymatic detoxification strategies for OTA have been constrained by low degradation efficiency or poor soluble expression of highly active enzymes. In this study, a bacterial strain with strong OTA-degrading activity was isolated and identified as Acinetobacter kookii AK4, which degraded 95.44% of 1 μg/mL OTA within 6 h. The predominant OTA-degrading activity was derived from intracellular enzymes. Through genome mining and experimental validation, gene2102 was identified as encoding an amidohydrolase. The enzyme was designated AMH2102 and was heterologously expressed in Escherichia coli. Codon optimization combined with fusion of an N-terminal SUMO tag increased the soluble expression of AMH2102 by 14.81-fold, enabling complete (100%) OTA degradation within 3 min. Overall, this study achieved the identification of an efficient OTA-degrading strain and enzyme and explored strategies for improving enzyme expression, yielding effective outcomes that provide useful references for future studies on strain mining and enzyme engineering. Full article
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