Surface immobilization strategies for tyrosinase as biocatalyst applicable to polymer network synthesis

Abstract

Enzymes have recently attracted increasing attention in material research based on their capacity to catalyze the conversion of polymer-bound moieties for synthesizing polymer networks, particularly bulk hydrogels. In this study, the surface immobilization of a relevant enzyme, mushroom tyrosinase, should be explored using glass as model surface. In a first step, the glass support was functionalized with silanes to introduce either amine or carboxyl groups, as confirmed e.g. by X-ray photoelectron spectroscopy. By applying glutaraldehyde and EDC/NHS chemistry, respectively, surfaces have been activated for subsequent successful coupling of tyrosinase. Via protein hydrolysis and amino acid characterization by HPLC, the quantity of bound tyrosinase was shown to correspond to a full surface coverage. Based on the visualized enzymatic conversion of a test substrate at the glass support, the functionalized surfaces may be explored for surface-associated material synthesis in the future.