Tyrosinase efficiently catalyzes the ortho-hydroxylation of monophenols and the oxidation of diphenols without any additional cofactors. Although it is of significant interest for the biosynthesis of catechol derivatives, the rapid catechol oxidase activity and inactivation of tyrosinase have hampered its practical utilization as a monophenol monooxygenase. Here, we prepared a functional tyrosinase and relevant mutants that exhibited a distinguished monophenolase/diphenolase activity ratio and an enhanced catalytic efficiency against L-tyrosine. The enzyme was still highly active in iced water, and its activity was well conserved under mild reaction conditions. In vitro DOPA modification and chitosan/gelatin hydrogel formation were achieved by the enzyme taking advantage of these biocatalytic properties. These results demonstrate the strong potential in biomedical and industrial applications.

Marine-derived and cold-adapted recombinant functional tyrosinase, that is functionally available as a monophenol monooxygenase

255th National Meeting (2018)

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