Modelling of amperometric biosensors in the case of substrate inhibition

Abstract

The response of an amperometric biosensor at mixed enzyme kinetics and diffusion limitations was modelled digitally in the case of substrate inhibition. Digital simulations were carried out using a finite difference technique. Calculations showed complex 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. At substrate concentration comparable to the Michaelis-Menten constant (KM), the response change shows a maximal value. A sharp response change was indicated at high enzyme activity and high (4.9 > S0/KM > 4.5) substrate concentration. This was explained by multiconcentration of substrate generation inside the enzyme layer. This conclusion was confirmed by the analytical solution of the simplified biosensor model with external diffusion limitation at steady-state conditions. The complex kinetics of response change produces different calibration graphs for biosensor response at transition and steady state.