Recent advances in microbial laccases for aflatoxins control: Identification, modification, and application

Aflatoxins (AFs) are prevalent carcinogens whose multiple toxicity threatens global food and feed security. Although previous studies have confirmed the ability of microorganisms and enzymes to degrade AFs, microbial laccase remains one of the most intensively investigated enzymes for aflatoxin transformation. Laccases are copper-containing oxidoreductases that catalyze the oxidation of aromatic and non-aromatic compounds. They have been widely employed in papermaking, environmental protection, food processing, and biosensors, and are highly valued for their environmentally friendly properties. In this article, the enzymatic properties of various reported aflatoxin-transforming laccases are systematically compared, and their applications in AFs control, along with recent advances in molecular modification, are reviewed. To date, numerous microbial laccases have been identified with the capacity to transform aflatoxins. Additionally, the crystal structures of two types of aflatoxin-transforming laccases have been resolved, enabling the proposal of catalytic mechanisms. Progress has also been made in protein engineering to enhance the catalytic efficiency and alter the substrate specificity of these enzymes. Furthermore, enzyme immobilization strategies aimed at improving the reusability and stability of aflatoxin-transforming laccases are presented and discussed.