Abstract

The working principle of enzyme-based biofuel cells (EBFCs) is the same as that of conventional fuel cells. In an EBFC system, the electricity-production process is very intricate. Analysis requires a mathematical model that can adequately describe the EBFC and predict its performance. This paper develops a dynamic model simulating the discharge performance of the anode for which supported glucose oxidase and mediator immobilize in the EBFC. The dynamic transport behavior of substrate, redox state (ROS) of enzyme, enzyme-substrate complex, and the mediator creates different potential changes inside the anode. The potential-step method illustrates the dynamic phenomena of substrate diffusion, ROS of enzyme, production of enzyme-substrate complex, and reduction of the mediator with different potential changes.

Highlights

  • The operating principle of biofuel cells (BFCs) is similar to that of conventional fuel cells, regarded as potential substitutes for fossil fuels

  • Enzyme-based biofuel cells (EBFCs) are distinguishable from conventional fuel cells by the use of biomass and specific enzymes known as biocatalysts [1,2,3,4,5,6]

  • The power output performance of the tested EBFCs was characterized by two-electrode electrochemical measurements containing 10 mM glucose, used 0.1 M phosphate buffer solution (PBS) pH 7, and 0.1 M citric buffer solution (CBS)

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Summary

Introduction

The operating principle of biofuel cells (BFCs) ( called biological fuel cells) is similar to that of conventional fuel cells, regarded as potential substitutes for fossil fuels. It is evident that when nanostructures of conductive materials are used, the large surface area of these nanomaterials can increase enzyme loading and facilitate reaction kinetics, improving EBFC power density Nanocarbon materials, such as carbon black, carbon nanotubes, carbon nanoballs and carbon aero-gel particles, form three-dimensional electrodes [14,17,18,19,20,21,22,23,24,25]. Irreversible breakdown of the enzyme-substrate complex yields the product (P) [32] For an oxidase such as glucose oxidase, the most studied redox enzyme, (Eox) is active towards the substrate (S) and produces the inactive form (Ered) which can be reactivated by oxidation with the cosubstrate (Mox) to form the reduced mediator (Mred), which subsequently is reoxidized at the electrode surface. This study investigates the process of operating anodes to evaluate the rate determining process, a dynamic model to diagnose EBFC systems based on diffusion, solid and liquid potential supported glucose substrate, glucose oxidase, potassium ferricyanide, and pH 7.0 phosphate buffer (0.1 M), (all anode interactions in EBFC systems)

Chemicals and Materials
Enzyme Electrode Preparation
Electrochemical Measurements
Mathematical Formulation
Results and Discussion
Distribution of Substrate on the Electrode
Distribution of Oxidized Enzyme on the Electrode
Distribution of Enzyme-Substrate Complex on the Electrode
Distribution of Mediator on the Electrode
Conclusions
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