Issue 24, 2013

High performance enzyme fuel cells using a genetically expressed FAD-dependent glucose dehydrogenase α-subunit of Burkholderia cepacia immobilized in a carbon nanotubeelectrode for low glucose conditions

Abstract

FAD-dependent glucose dehydrogenase (FAD-GDH) of Burkholderia cepacia was successfully expressed in Escherichia coli and subsequently purified in order to use it as an anode catalyst for enzyme fuel cells. The purified enzyme has a low Km value (high affinity) towards glucose, which is 463.8 μM, up to 2-fold exponential range lower compared to glucose oxidase. The heterogeneous electron transfer coefficient (Ks) of FAD-GDH–menadione on a glassy carbon electrode was 10.73 s−1, which is 3-fold higher than that of GOX–menadione, 3.68 s−1. FAD-GDH was able to maintain its native glucose affinity during immobilization in the carbon nanotube and operation of enzyme fuel cells. FAD-GDH–menadione showed 3-fold higher power density, 799.4 ± 51.44 μW cm−2, than the GOX–menadione system, 308.03 ± 17.93 μW cm−2, under low glucose concentration, 5 mM, which is the concentration in normal physiological fluid.

Graphical abstract: High performance enzyme fuel cells using a genetically expressed FAD-dependent glucose dehydrogenase α-subunit of Burkholderia cepacia immobilized in a carbon nanotube electrode for low glucose conditions

Supplementary files

Article information

Article type
Communication
Submitted
24 Jan 2013
Accepted
07 May 2013
First published
07 May 2013

Phys. Chem. Chem. Phys., 2013,15, 9508-9512

High performance enzyme fuel cells using a genetically expressed FAD-dependent glucose dehydrogenase α-subunit of Burkholderia cepacia immobilized in a carbon nanotube electrode for low glucose conditions

D. Fapyane, S. Lee, S. Kang, D. Lim, K. Cho, T. Nam, J. Ahn, J. Ahn, S. Kim and I. S. Chang, Phys. Chem. Chem. Phys., 2013, 15, 9508 DOI: 10.1039/C3CP51864G

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements