Abstract
The recombinant tyrosinase from Verrucomicrobium spinosum bacteria has been obtained by heterologous expression in E. coli and isolated in the pure state to determine some of its biochemical properties (the kinetics of the enzymatic reaction, the effect of an inhibitor and activator, and the pH optimum). Coexpression of the genes for tyrosinase and recombinant adhesive mussel protein in one producer strain was used to introduce posttranslational modifications into the adhesive protein. These modifications involved the transformation of tyrosine residues into DOPA residues, which makes the protein capable of molecular adhesion in an aqueous medium.
Published Version
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