2017
DOI: 10.4236/ajac.2017.87036
|View full text |Cite
|
Sign up to set email alerts
|

Reliable Method for Steady-State Concentrations and Current over the Diagnostic Biosensor Transducers

Abstract: A mathematical modelling of diagnostic biosensors system at three basic types of enzyme kinetics is discussed in the presence of diffusion. Enzyme kinetics is adopted to be first order, Michaelis-Menten and ping-pong mechanism. In this paper, approximate analytical solutions are obtained for the non-linear equations under steady-state conditions by using the new Homotopy perturbation method. Simple and closed forms of analytical expressions for concentrations of substrate, product and co-substrate and correspo… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1

Citation Types

0
1
0

Year Published

2018
2018
2020
2020

Publication Types

Select...
2

Relationship

0
2

Authors

Journals

citations
Cited by 2 publications
(1 citation statement)
references
References 22 publications
0
1
0
Order By: Relevance
“…The amperometric responses of the enzyme in the biosensor to different cholesterol concentrations, the rate of substrate degradation and the amount of product formed are very important in the analytical performance of the biosensor. According to Michaelis‐Menten kinetics, the rate of the reaction is increase by increasing the concentration of the substrate while keeping the amount of enzyme in the medium constant and eventually reaches a plateau . To calculate the Michaelis‐Menten constant (Km) (Figure D), a Line weaver Burk plot was drawn (inset of Figure D).…”
Section: Resultsmentioning
confidence: 99%
“…The amperometric responses of the enzyme in the biosensor to different cholesterol concentrations, the rate of substrate degradation and the amount of product formed are very important in the analytical performance of the biosensor. According to Michaelis‐Menten kinetics, the rate of the reaction is increase by increasing the concentration of the substrate while keeping the amount of enzyme in the medium constant and eventually reaches a plateau . To calculate the Michaelis‐Menten constant (Km) (Figure D), a Line weaver Burk plot was drawn (inset of Figure D).…”
Section: Resultsmentioning
confidence: 99%