Aflatoxin B1 (AFB1) is a highly carcinogenic small molecule produced by Aspergillus flavus and Aspergillus parasiticus which contaminates food crops around the world and, although it is already a major production burden, it is expected to increase in prevalence as climate change accelerates. The Food and Agriculture Organization recommends no more than 15 μg/kg of AFB1 in human food; 10 however, it is difficult to keep concentrations below this level, as mycotoxin contamination can occur at every step of the food production, storage, and distribution process. Many methods have been proposed to combat aflatoxin in the food supply including improving cultivars, better post-harvest handling and transportation, more rapid detection methods, and bioremediation via enzymatic detoxification. The latter method shows great promise for neutralizing contaminated foodstuffs as, unlike many chemical and physical detoxification processes, enzymes can be engineered to be highly specific to a contaminant of interest without destroying the desirable nutritional or organoleptic properties of the food. Specific enzymes, several of which come from the multicopper oxidase families, have been studied and shown to be capable of AFB1 degradation. However, the enzymes discovered to date have insufficient catalytic rates to be of practical use for remediation. In this study, we aim to discover new enzymes in the multicopper oxidase family capable of degrading AFB1 to begin elucidating the structural determinants of function and identifying new leads for enzyme engineering efforts to create efficient and specific enzymes capable of degrading aflatoxin.