A Novel Hydrolase Capable of Efficiently Degrading the Highly Toxic ZEN Derivative

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.