文摘
A facile method of immobilizing enzymes on activated carbon (AC) is proposed, in which the first step is to coat AC with Concanavalin A (ConA), followed by the adsorption of enzymes. Two model glycoenzymes, horseradish peroxidase and laccase, were immobilized on the ConA adsorbed AC through the tightly specific recognition of ConA to their glycosidic moieties, as confirmed by laser confocal microscopy. The coating layer of ConA reduced the deactivation of enzymes and prevented the leakage of enzymes, as indicated by the significantly improved yield of enzymatic activity. The immobilized enzymes on ConA coated AC appeared an improved stability against pH and temperature, offering an expanded operation “window” for growing applications of the enzymatic catalysis. Finally, the integration of the adsorption capacity of AC and the chemical degradation of laccase promises the efficient removal of aqueous phenol. The improved recovery of enzyme activity, enhanced stability as well as the combination of substrate adsorption and enzymatic reaction make ConA coated AC appealing for various enzymatic catalysis.
