Abstract
The immobilization of a d-glucose oxidase (β- d-glucose: oxygen 1-oxidoreductase, EC 1.1.3.4) monolayer onto a glassy carbon rotating disc electrode allows the measurement of concentrations in the enzyme's microenvironment and, hence, gives a method of easily following its activity. As it functions, d-glucose oxidase undergoes an autoinactivation which is clearly distinct from inactivation by H 2O 2, and which is more severe as the concentration of the two substrates is increased. It appears that the number of catalytic cycles is fixed at 10 7, irrespective of the concentrations of the two substrates. Kinetically, it is the enzyme-substrate complex which seems to be inactivated. Scavengers of toxic species of O 2 have no effect on the kinetics of autoinactivation. Identical results were found in solution.
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