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Dynamic and steady state 1-D model of mediated electron transfer in a porous enzymatic electrode.

Dynamic and steady state 1-D model of mediated electron transfer in a porous enzymatic electrode.

Authors :
Do TQ
Varničić M
Flassig RJ
Vidaković-Koch T
Sundmacher K
Source :
Bioelectrochemistry (Amsterdam, Netherlands) [Bioelectrochemistry] 2015 Dec; Vol. 106 (Pt A), pp. 3-13. Date of Electronic Publication: 2015 Aug 01.
Publication Year :
2015

Abstract

A 1-D mathematical model of a porous enzymatic electrode exhibiting the mediated electron transfer (MET) mechanism has been developed. As a model system, glucose oxidation catalyzed by immobilized glucose oxidase (GOx) in the presence of a co-immobilized tetrathiafulvalene (TTF) mediator in the porous electrode matrix has been selected. The balance equations for potential fields in the electron- and ion-conducting phases as well as concentration field have been formulated, solved numerically and validated experimentally under steady state conditions. The relevant kinetic parameters of the lumped reaction kinetics have been obtained by global optimization. The confidence intervals (CIs) of each parameter have been extracted from the respective likelihood. The parameter study has shown that the parameters related to mediator consumption/regeneration steps can be responsible for the shift of the reaction onset potential. Additionally, the model has shown that diffusion of the oxidized mediator out of the catalyst layer (CL) plays a significant role only at more positive potentials and low glucose concentrations. Only concentration profiles in different layers influence the electrode performance while other state fields like potential distributions in different phases have no impact on the performance. The concentration profiles reveal that all electrodes work through; the observed limiting currents are diffusion-reaction limiting. The normalized electrode activity decreases with an increase of enzyme loading. According to the model, the reason for this observation is glucose depletion along the CL at higher enzyme loadings. Comparison with experiments advices a decrease of enzyme utilization at higher enzyme loadings.<br /> (Copyright © 2015 Elsevier B.V. All rights reserved.)

Details

Language :
English
ISSN :
1878-562X
Volume :
106
Issue :
Pt A
Database :
MEDLINE
Journal :
Bioelectrochemistry (Amsterdam, Netherlands)
Publication Type :
Academic Journal
Accession number :
26257008
Full Text :
https://doi.org/10.1016/j.bioelechem.2015.07.007