Enzymatic treatment is an attractive method for mycotoxin detoxification, which ideally prefers the use of one or a few enzymes. However, this is challenged by the diverse structures and co-contamination of multiple mycotoxins in food and feed. Lignin-degrading fungi have been discovered to detoxify organics including mycotoxins. Manganese peroxidase (MnP) is a major enzyme responsible for lignin oxidative depolymerization in such fungi. Here, we demonstrate that eight MnPs from different lignocellulose-degrading fungi (five from , one from , one from , and another from ) could all degrade four major mycotoxins (aflatoxin B, AFB; zearalenone, ZEN; deoxynivalenol, DON; fumonisin B, FB) only in the presence of a dicarboxylic acid malonate, in which free radicals play an important role. The and MnPs behaved similarly in mycotoxins transformation, outperforming the and MnPs. The large evolutionary diversity of these MnPs suggests that mycotoxin degradation tends to be a common feature shared by MnPs. MnP can, therefore, serve as a candidate enzyme for the degradation of multiple mycotoxins in food and feed if careful surveillance of the residual toxicity of degradation products is properly carried out.