Zearalenone reduction by commercial peroxidase enzyme and peroxidases from soybean bran and rice bran.

The peroxidase (POD) enzyme, obtained from different sources, has been described in the literature regarding its good results of reduction in concentration or degradation levels of mycotoxins, such as aflatoxin B1, deoxynivalenol and zearalenone (ZEA). This study aimed at evaluating the action of commercial POD and POD from soybean bran (SB) and rice bran (RB) in ZEA reduction in a model solution and the characterisation of the mechanism of enzyme action. POD was extracted from SB and RB in phosphate buffer by orbital agitation. Evaluation of the action of commercial POD and POD from SB and RB in ZEA reduction was carried out in phosphate buffer and aqueous solution, respectively. Parameters of (Michaelis-Menten constant) (KM) and maximal rate (Vmax) were determined in the concentration range from 0.16 to 6 µg mL-1. ZEA reduction was determined and the mechanism of enzyme action was characterised by FTIR and high-pressure liquid chromatography-electrospray tandem mass spectrometry. Commercial POD and POD from RB and SB reduced ZEA concentration by 69.9%, 47.4% and 30.6% in 24 h, respectively. KM values were 39.61 and 8.90 µM, whereas Vmax values were 0.170 and 0.011 µM min-1 for commercial POD and POD from RB, respectively. The characterisation of the mechanism of enzyme action showed the oxidoreductive action of commercial POD in the mycotoxin. The use of commercial POD and POD from agro-industrial by-products, such as SB and RB, could be a promising alternative for ZEA biodegradation.