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The response of an amperometric biosensor at mixed enzyme kinetics anddiffusion limitations was modelled digitally in the case of substrate inhibition. Digitalsimulations were carried out using a finite difference technique. Calculations showedcomplex kinetics of biosensor response. At low enzyme activity and substrate concentration(S0), the response of the sensor looks like it is limited by a simple substrate diffusion. Atsubstrate concentration comparable to the Michaelis-Menten constant (KM), the responsechange shows a maximal value. A sharp response change was indicated at high enzymeactivity and high (4.9 > S0/KM > 4.5) substrate concentration. This was explained by multiconcentrationof substrate generation inside the enzyme layer. This conclusion wasconfirmed by the analytical solution of the simplified biosensor model with externaldiffusion limitation at steady-state conditions. The complex kinetics of response changeproduces different calibration graphs for biosensor response at transition and steady state

Modelling of Amperometric Biosensors in the Case of Substrate Inhibition