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Updated: Oct 25, 2026

Synthesis of an Intein-mediated Artificial Protein Hydrogel
Published on: January 27, 2014
A Novel Hydrolase Capable of Efficiently Degrading the Highly Toxic ZEN Derivative
Mingzhu Yan1,2, Jian Gao2, Qianli Zhang2,3
1School of Biological Engineering, Tianjin University of Science and Technology, No 9, 13th, Avenue, Tianjin Economic and Technological Development Area, Tianjin300457, China.
Abstract:
Zearalenone (ZEN) and its toxic derivatives (α-ZAL and α-ZEL) pose significant challenges to food and feed safety, while efficient degrading enzymes for these toxins remain limited. This study identified a novel XyZHD exhibiting higher catalytic activity toward α-ZAL and α-ZEL than ZEN under the assay conditions. Recombinant XyZHD showed optimal activity at pH 9.0 and 45 °C, and its activity was significantly affected by Zn2+ and Fe3+. Structural analysis combined with mutagenesis studies provided insights into residues associated with catalytic activity. The S153E mutant showed a 3.1-fold increase in activity compared with the wild type. XyZHD exhibited high specific activity toward ZEN derivatives, favorable thermal stability, and efficient degradation of α-ZAL in corn grits, suggesting its potential for further research and development in the field of ZEN biocontrol.
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