Application of bacterial tyrosinases in organic synthesis

Bacterial tyrosinases, as in the case of other bacterial oxidative enzymes, have been found to possess biochemical characteristics that typically make them more suited to applications requiring special operational conditions such as alkaline pH, high or low temperature, the presence of organic solvents, and the presence of inhibitors. Even though a great deal is known about fungal tyrosinases, bacterial tyrosinases still vastly remain underexplored for their potential application in organic synthesis. A literature survey in particular highlights the gaps in our knowledge pertaining to their biochemical properties. Bacterial tyrosinases have not only shown promise in the synthesis of medically important compounds such as L-3,4-dihydroxyphenylalanine (L-DOPA) and melanin but have also seen application in cross-linking reactions of proteins and the polymerization of environmental pollutants. Their ability to catalyse o-hydroxylation reactions have shown some degree of promise in the biocatalytic conversion of resveratrol to piceatannol, tyrosol to hydroxytyrosol, and many more. In this review, we will explore the world of bacterial tyrosinases, their current applications, and future perspectives for the application of these enzymes in organic synthesis.