Kinetic Characterization of Peroxidase and Laccase Degradation of Zearalenone and Their Application for Removal of Zearalenone from Beer

In this study, peroxidase (POD) and laccase (LC) were selected to enzymatically degrade zearalenone (ZEN). Reaction parameters, including enzyme concentration, pH, and temperature, were optimized, and kinetic models were established to evaluate their catalytic characteristics. Additionally, the degradation efficiencies of ZEN in beer as a food matrix by POD and LC were assessed. The results showed that under the optimal reaction conditions of 40 ℃, pH 7, and 48 U/mL, POD degraded more than 90% of ZEN. When activated by 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), methyl syringate (MSG), or acetosyringone (AS), LC could also degrade more than 90% of ZEN. Kinetic analysis indicated that both POD and LC exhibited interactions with ZEN. The KM and Vmax values for POD were 2.01 μg/mL and 0.015 μg/(mL·min), respectively. The KM and Vmax values for LC were 2.66 μg/mL and 0.017 μg/(mL·min), respectively. Compared with model solutions, the degradation efficiencies of ZEN in beer were reduced due to acidic pH, metal ions, and matrix complexity. This study provides a theoretical basis for enzymatic detoxification of mycotoxins in food systems and supports the development of functional enzyme preparations.