Laccase catalysis for the synthesis of bioactive compounds

The demand for compounds of therapeutic value is increasing mainly because of new applications of bioactive compounds in medicine, pharmaceutical, agricultural, and food industries. This has necessitated the search for cost-effective methods for producing bioactive compounds and therefore the intensification of the search for enzymatic approaches in organic synthesis. Laccase is one of the enzymes that have shown encouraging potential as biocatalysts in the synthesis of bioactive compounds. Laccases are multicopper oxidases with a diverse range of catalytic activities revolving around synthesis and degradative reactions. They have attracted much attention as potential industrial catalysts in organic synthesis mainly because they are essentially green catalysts with a diverse substrate range. Their reaction only requires molecular oxygen and releases water as the only by-product. Laccase catalysis involves the abstraction of a single electron from their substrates to produce reactive radicals. The free radicals subsequently undergo homo- and hetero-coupling to form dimeric, oligomeric, polymeric, or cross-coupling products which have practical implications in organic synthesis. Consequently, there is a growing body of research focused on the synthetic applications of laccases such as organic synthesis, hair and textile dyeing, polymer synthesis, and grafting processes. This paper reviews the major advances in laccase-mediated synthesis of bioactive compounds, the mechanisms of enzymatic coupling, structure-activity relationships of synthesized compounds, and the challenges that might guide future research directions.