Fundamental studies of glucose oxidase deposition on a Pt electrode

The direct electrodeposition of glucose oxidase (EC 1.1.3.4) on a platinum electrode was investigated as a means for controlled immobilization. The presence of a nonionic detergent, Triton X-100, was found essential to produce a multilayered deposit. Moreover, to work properly, the detergent must be present above its critical micelle concentration. Under these conditions, a deposit of ~50 enzyme layers (480 nm), with surface uniformity of [+ or -] 20 nm, was verified using an electrochemical quartz crystal microbalance and by atomic force microscopy. In the absence of detergent, a layer of 25 nm is formed. Contrary to most previous claims, the deposition, which is potential dependent but optimal at 1.3 V versus AgCl/ Ag electrode, is not electrophoretically driven, but is instead controlled by a lowering of the pH at the electrode surface due to concomitant oxygen evolution.