Sensors · 2006 · 29 citations · 13 references
Life SciencesBiochemistryBiosensorsChemical KineticsEnzymologyBiosensor CalibrationEnzymatic BiosensorsEnzyme AssaysEnzyme InhibitionEnzyme KineticsMichaelis-menten KineticsAmperometric BiosensorsAmperometric Enzymatic BiosensorsAmperometric Enzyme BiosensorsAmperometric SensorsEnzyme ActivityMichaelis ConstantSubstrate InhibitionSubstrate Inhibition Kinetics
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.
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The Development of New Analytical Systems Based on Biocatalysts
Juozas Kulys · Analytical Letters · 1981 · 94 citations