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African Physical Review (2007) 1 Special Issue (Microfluidics):0003 6

A Numerical Simulation of Amperometric Biosensor Effect


of Enzyme Loading and Stirring Strength on Biosensors Performance

A. Benyahia and S. Bacha


Laboratoire de Gnie de lEnvironnement, Universit Abderrahmane MIRA de Bjaia,
Route de Targa Ouzemmour, Algeria

1. Introduction The above equation as well as initial and


boundary conditions are integrated over controlled
Biosensors are defined as analytical devices
volumes according to Finite Volume Method
incorporating a physicochemical transducer (or
(FVM) and the set of algebraic equation are solved
transducing system) and biologically active material
numerically by Thomas algorithm. The algorithm is
integrated with it. The amperometric biosensor is
written in Visual Fortran and run on a Pentium III
one of the types of biosensors which typically rely
PC (733 kHz) processor. The model is applied to
on an enzyme system that catalytically converts an
simulate the response of the biosensors versus many
electrochemically non-active analyte into products
parameters such as the amount of the immobilized
that can be oxidized or reduced at a working
enzyme, the membrane thickness and the thickness
electrode. Modelling of biosensors is of crucial
of the diffusion.
importance in order to understand their behaviour,
which began with the work of Gough et al., [1], G.
3. Influence of the internal resistance on the
Jobst et al., [2] and S.D. Caras et al., [3,4,5]. S.
signal magnitude
Bacha et al. [6.7] developed a model that takes into
account a variety of configuration designs. To study the effect of the internal resistance, a
In the present work, we have developed a diffusion layer thickness is taken deliberately equal
mathematical model in order to describe and to 0. This leads to a value of Bi = . One can see
evaluate the performance of amperometric that the maximal magnitude of the biosensor, which
biosensors. The chosen configuration is the one corresponds to the steady state current, increases
most used nowadays in the design of enzymatic with an increase in the quantity of enzyme. Another
biosensors such as the polymeric matrices as interesting feature is that the maximum current
enzyme supports and the mass production of density does not exceed a limit of 11.56 A/cm2
biosensors by the screen-printing technique. regardless of the amount of immobilized enzyme.
The maximum dimensionless current density max
2. Main Results versus Thiele modulus is linear up to a value of
=2. No further increase of max is obtained
The sensors considered consist of a metallic
beyond this value whatever is the Thieles modulus
electrode surface, a membrane held against the
value.
surface electrode and a diffusion layer adjacent to
the outer surface of the membrane. In the enzyme
4. Effect of external resistance to mass
membrane, the substrate S is concerted to an
transfer
electroactive product P which is detected. Coupling
the enzyme catalysed reaction in enzyme layer with To study the effect of external resistance to mass
the one-dimensional-in-space diffusion, described transfer, values of =7 and =1 are taken to
by Ficks second law, leads to the following perform the simulation. The diffusion layer
equation: thickness e is chosen to ensure value of Bi from
0.5 to 50 (i.e. for diffusion layer thickness e
[C ] 2 [C ] v max
v
[C ] varying from 200 to 2 m). Results show that the
= Dc magnitude of the response increase with the
t x 2
ks + [C ] c
decrease of the diffusion layer thickness, but one
where C may be S or P. should highlight that for Bi=1 and Bi=0.5, there is a
The current density is calculated by estimating peak of 6.6 A/cm2 approximately at t=4s. The
the gradient of the electroactive species at the maximum current density at Bi value equal to 50
surface of electrode.
African Physical Review (2007) 1 Special Issue (Microfluidics):0003 7

(well stirred solutions) is 1.8 times its value at Bi References


value equal to 1 (weak stirred ones).
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5. Conclusion
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and may keep somewhat a regular biosensor signal AICHE Journal 42, No.10, 2967 (1996).
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