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Modelling of Amperometric Biosensors in the Case of Substrate Inhibition

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...

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Detalles Bibliográficos
Autores principales: Kulys, Juozas, Baronas, Romas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3909412/
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author Kulys, Juozas
Baronas, Romas
author_facet Kulys, Juozas
Baronas, Romas
author_sort Kulys, Juozas
collection PubMed
description 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 (S(0)), the response of the sensor looks like it is limited by a simple substrate diffusion. At substrate concentration comparable to the Michaelis-Menten constant (K(M)), the response change shows a maximal value. A sharp response change was indicated at high enzyme activity and high (4.9 > S(0)/K(M) > 4.5) substrate concentration. This was explained by multi-concentration 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.
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spelling pubmed-39094122014-02-03 Modelling of Amperometric Biosensors in the Case of Substrate Inhibition Kulys, Juozas Baronas, Romas Sensors (Basel) Full Paper 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 (S(0)), the response of the sensor looks like it is limited by a simple substrate diffusion. At substrate concentration comparable to the Michaelis-Menten constant (K(M)), the response change shows a maximal value. A sharp response change was indicated at high enzyme activity and high (4.9 > S(0)/K(M) > 4.5) substrate concentration. This was explained by multi-concentration 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. Molecular Diversity Preservation International (MDPI) 2006-11-07 /pmc/articles/PMC3909412/ Text en © 2006 by MDPI (http://www.mdpi.org). Reproduction is permitted for non-commercial purposes.
spellingShingle Full Paper
Kulys, Juozas
Baronas, Romas
Modelling of Amperometric Biosensors in the Case of Substrate Inhibition
title Modelling of Amperometric Biosensors in the Case of Substrate Inhibition
title_full Modelling of Amperometric Biosensors in the Case of Substrate Inhibition
title_fullStr Modelling of Amperometric Biosensors in the Case of Substrate Inhibition
title_full_unstemmed Modelling of Amperometric Biosensors in the Case of Substrate Inhibition
title_short Modelling of Amperometric Biosensors in the Case of Substrate Inhibition
title_sort modelling of amperometric biosensors in the case of substrate inhibition
topic Full Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3909412/
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