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Fapyane, Deby,Lee, Soo-Jin,Kang, Seo-Hee,Lim, Du-Hyun,Cho, Kwon-Koo,Nam, Tae-hyun,Ahn, Jae-Pyoung,Ahn, Jou-Hyeon,Kim, Seon-Won,Chang, In Seop The Royal Society of Chemistry 2013 Physical chemistry chemical physics Vol.15 No.24
<P>FAD-dependent glucose dehydrogenase (FAD-GDH) of <I>Burkholderia cepacia</I> was successfully expressed in <I>Escherichia coli</I> and subsequently purified in order to use it as an anode catalyst for enzyme fuel cells. The purified enzyme has a low <I>K</I><SUB>m</SUB> 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 (<I>K</I><SUB>s</SUB>) of FAD-GDH–menadione on a glassy carbon electrode was 10.73 s<SUP>−1</SUP>, which is 3-fold higher than that of GOX–menadione, 3.68 s<SUP>−1</SUP>. 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<SUP>−2</SUP>, than the GOX–menadione system, 308.03 ± 17.93 μW cm<SUP>−2</SUP>, under low glucose concentration, 5 mM, which is the concentration in normal physiological fluid.</P> <P>Graphic Abstract</P><P>FAD-dependent glucose dehydrogenase (FAD-GDH) of <I>Burkholderia cepacia</I> was successfully expressed in <I>Escherichia coli</I> and subsequently purified in order to use it as an anode catalyst for enzyme fuel cells. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c3cp51864g'> </P>