2006
DOI: 10.3390/s6121765
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Modelling the Transport and Kinetics of Electroenzymes at the Electrode/Solution Interface

Abstract: Abstract:The solution phase transport and direct electrode kinetics of electro-enzymes are described in terms of a simple model in which the steady state reaction/diffusion equation for enzyme is solved subject to physically realistic boundary conditions. Two physically realizable situations are described: the semi infinite and the membrane bounded case. Limiting expressions for the reaction flux are derived and the kinetic possibilities discussed geometrically in terms of kinetic case diagrams.

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Cited by 18 publications
(4 citation statements)
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“…Increasing the thickness of the external diffusion layer creates an additional diffusion limitation to the substrates, i.e. , leads to a lowering of the substrate concentration in the enzyme layer and, thereby, increasing the biosensor sensitivity, as well as prolonging the calibration curve of the biosensor [ 23 , 24 ]. This feature can be also noticed in Figure 7 .…”
Section: Resultsmentioning
confidence: 99%
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“…Increasing the thickness of the external diffusion layer creates an additional diffusion limitation to the substrates, i.e. , leads to a lowering of the substrate concentration in the enzyme layer and, thereby, increasing the biosensor sensitivity, as well as prolonging the calibration curve of the biosensor [ 23 , 24 ]. This feature can be also noticed in Figure 7 .…”
Section: Resultsmentioning
confidence: 99%
“…The influence of the white noise-, as well as temperature-induced trend on the calculation of the analyte concentration has been also investigated at internal diffusion limitations by ignoring the external mass transport by diffusion. However, in practical biosensing systems, the diffusion of materials outside the enzyme region is of crucial importance for the biosensor response [ 23 , 24 ].…”
Section: Introductionmentioning
confidence: 99%
“…In this paper we seek to develop a theory accounting for both apparently altered (and potential dependent) Michaelis-Menten constants and for nano-confinement effects. This builds on prior models developed by Lyons [19][20][21] and Bartlett [22][23][24] but is based on bespoke, newly derived kinetic expressions which recognise the surface immobilised nature of the redox enzyme and its reaction with a solution-phase substrate, S. The full kinetic scheme addressed is shown in Figure 1. Our approach emphasises the importance of the active electrode area to the volume of the solution, especially that under nano-confinement.…”
Section: Introductionmentioning
confidence: 99%
“…Oxygen transport in CME with macrohomogenous/ thin-film model [31] Anode S/E/--S-S/diffusion/-E-free /--Electroenzymes at the electrode/solution interface [40] Anode S/E/--S-S/-/-E-free/--Amperometric bioanalytical system for lipase activity assay …”
Section: Introductionmentioning
confidence: 99%