Enzymatic characterization and application of soybean hull peroxidase as an efficient and renewable biocatalyst for degradation of zearalenone.
Enzymatic characterization and application of soybean hull peroxidase as an efficient and renewable biocatalyst for degradation of zearalenone.
复制标题
大豆皮过氧化物酶作为玉米赤霉烯酮降解的高效可再生生物催化剂的酶学表征和应用。
DOI：
10.1016/j.ijbiomac.2024.129664
复制
发表时间：
2024
影响因子：
8.2
通讯作者：
Lihong Zhao
中科院分区：
文献类型：
--
作者：
Yongpeng Guo;Yu Tang;Liangyu Zhang;Yanrong Liu;Qiugang Ma;Lihong Zhao
Zearalenone (ZEN) is a notorious mycotoxin commonly found inFusarium-contaminated crops, which causes great loss in livestock farming and serious health problems to humans. In the present work, we found that crude peroxidase extraction from soybean hulls could use H2O2as a co-substate to oxidize ZEN. Molecular docking and dynamic simulation also supported that ZEN could bind to the active site of soybean hull peroxidase (SHP). Subsequently, SHP extracted from soybean hulls was purified using a combined purification protocol involving ammonium sulfate precipitation, ion exchange chromatography and size exclusion chromatography. The purified SHP showed wide pH resistance and high thermal stability. This peroxidase could degrade 95 % of ZEN in buffer with stepwise addition of 100 μM H2O2in 1 h. The two main ZEN degradation products were identified as 13-OH-ZEN and 13-OH-ZEN-quinone. Moreover, SHP-catalyzed ZEN degradation products displayed much less cytotoxicity to human liver cells than ZEN. The application of SHP in various food matrices obtained 54 % to 85 % ZEN degradation. The findings in this study will promote the utilization of SHP as a cheap and renewable biocatalyst for degrading ZEN in food.
