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A Sustainable Approach for Degradation of Alternariol by Peroxidase Extracted from Soybean Hulls: Performance, Pathway, and Toxicity Evaluation.

Xingke ZhangHao ZhengHao LvJiyuan YinYi LiKexin ZhangLiangyu ZhangWei ZhangZhixiang WangLihong ZhaoYongpeng Guo
Published in: Foods (Basel, Switzerland) (2024)
Alternariol (AOH), an emerging mycotoxin, inevitably exists widely in various food and feed commodities with cereals and fruits being particularly susceptible, raising global concerns over its harm to human and livestock health. The development of eco-friendly and efficient strategies to decontaminate AOH has been an urgent task. This study provided insight into the utilization of crude soybean hull peroxidase as a powerful biocatalyst for degrading AOH. The results confirmed that crude soybean hull peroxidase (SHP) could catalyze the oxidation of AOH by use of H 2 O 2 as a co-substrate. The optimum reaction conditions for SHP-catalyzed AOH degradation were recorded at pH 4.0-8.0, at 42-57 °C, and at H 2 O 2 concentration of 100-500 μM. Mass analysis elucidated the degradation of AOH through hydroxylation and methylation by crude SHP. Moreover, toxicological analysis indicated that crude SHP-catalyzed AOH degradation detoxified the hepatotoxicity of this mycotoxin. The performance of crude SHP to degrade AOH in food matrices was further evaluated, and it was found that the enzyme agent could achieve AOH degradation by 77% in wheat flour, 84% in corn flour, 34% in grape juice, and 26% in apple juice. Collectively, these findings establish crude SHP as a promising candidate for effective AOH degradation, with potential applications in the food and feed industry.
Keyphrases
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  • oxidative stress
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  • dna methylation
  • amino acid
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