Apparent Michaelis constant of the enzyme modified porous electrode

DOI10.1007/S10910-007-9237-7MaRDI QIDQ551928zbMATH OpenOpenAlexFDO

Authors I. Kaunietis, R. Šimkus, F. Ivanauskas, Julija Razumiene, Valdas Laurinavicius

Publication date 21 July 2011

Published in Journal of Mathematical Chemistry (Search for Journal in Brave)

Full work available at URL https://doi.org/10.1007/s10910-007-9237-7

zbMATH Keywords

amperometric biosensorscarbonmodelingPQQ-dependent dehydrogenasereaction-diffusion

Mathematics Subject Classification ID

Electrochemistry (78A57)

Recommendations

• scientific article; zbMATH DE number 2233480
• Computer simulation of the steady state currents at enzyme doped carbon paste electrodes
• Numerical study of the effect of some mathematical modeling parameters of single enzyme biosensor based on Michaelis-Menten enzymatic reaction
• Biosensor response at mixed enzyme kinetics and external diffusion limitation in case of substrate inhibition
• Modelling of amperometric biosensors with rough surface of the enzyme membrane

Cites work

• Computer simulation of the steady state currents at enzyme doped carbon paste electrodes
• Modelling of amperometric biosensors with rough surface of the enzyme membrane

Cited in

(4)

• Modeling of electrocatalysis at conducting polymer modified electrodes: nonlinear current-concentration profiles
• Computer simulation of the steady state currents at enzyme doped carbon paste electrodes
• scientific article; zbMATH DE number 2233480 (Why is no real title available?)
• Mechanisms controlling the sensitivity of amperometric biosensors in flow injection analysis systems

This page was built for publication: Apparent Michaelis constant of the enzyme modified porous electrode

Report a bug (only for logged in users!)Click here to report a bug for this page (MaRDI item Q551928)