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Issue 24, 2013
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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

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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

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Publication details

The article was received on 24 Jan 2013, accepted on 07 May 2013, published on 07 May 2013 and first published online on 07 May 2013


Article type: Communication
DOI: 10.1039/C3CP51864G
Citation: Phys. Chem. Chem. Phys., 2013,15, 9508-9512
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    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

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