Laccases (EC 1.10.3.2) are a family within multicopper oxidases that utilize O2 to perform oxidation reactions on a wide range of target molecules. These reactions are carried out by stripping an electron from their oxidation target at their mononuclear type 1 (T1) copper site and then passing the electron through a series of amino acids, namely His-Cys-His. The electron is passed along this path to the trinuclear type 3 site (T3) where it is stored as a stable redox intermediate until a total of 3 electrons are obtained. O2 is reduced to water once the requisite 4 electrons are accumulated across the T3 and T1 sites. The ability to perform a broad range of oxidation reactions with O2 as an electron acceptor has resulted in laccases evolving to serve a wide range of roles in nature including lignin degradation, lignin biosynthesis, virulence enhancement, immunity, detoxification, and more. They are found across the tree of life as both monomers and as multimeric units and are closely related to other groups including small blue proteins, blue oxidases, and coagulation factors. They have also found broad use in industrial applications ranging from pulp and paper processing, food stabilization, pharmaceutical production, and bioremediation. Previous studies have sought to determine whether aflatoxin could be specifically targeted for enzymatic degradation and several have shown success. However, to-date there has been no enzyme with sufficient activity to explore industrial relevance. Most studies demonstrate incomplete degradation with undefined biological extracts over a varying incubation periods into unknown transformation products. Recently, Guo et al made a significant advance by characterizing the AFB1 laccase oxidation transformation product using a purified enzyme. The resulting transformation product was determined to be aflatoxin Q1 (AFQ1) (Figure ) which is 18-fold less toxic than AFB1. However, even with optimized parameters, the reaction required 12 hours to achieve 96% completion with an catalytic loading of approximately 5% catalytic loading (0.34 μM catalyst with 6.40 μM substrate). For many industrial use cases, a minimum of 99% completion in less than 24-hours with a catalytic loading of <1% would be expected.