Efficient Expression and Activity Optimization of Manganese Peroxidase for the Simultaneous Degradation of Aflatoxins AFB, AFB, AFG, and AFG.

Aflatoxins (AFs), notorious mycotoxins that pose significant risks to human and animal health, make biodegradation extremely crucial as they offer a promising approach to managing and reducing their harmful impacts. In this study, we identified a manganese peroxidase from (Mnp) through protein similarity analysis, which has the capability to degrade four AFs (AFB, AFB, AFG, and AFG) simultaneously. The gene encoding this enzyme was subject to codon optimization, followed by cold shock induction expression using the pColdII vector, leading to the soluble expression of manganese peroxidase (Mnp) in . This study tackled the problem of inclusion body formation that often occurs during Mnp expression in . After optimizing the degradation conditions, the degradation rates for AFB, AFB, AFG, and AFG were 87.9, 72.8, 77.3, and 85.6%, respectively. Molecular docking and molecular dynamics simulations indicated that Mnp facilitated the degradation of AFs through hydrophobic and polar interactions among various amino acid residues. This research offers novel insights into the rapid discovery of enzymes capable of degrading AFs and establishes a theoretical foundation for the efficient expression of mycotoxin detoxification enzymes.