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 2024-01-20T12:31:07Z 2024-01-20T12:31:07Z 2022-01-25 2013-05 1463-9076 https://pubs.kist.re.kr/handle/201004/128081 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 K-m value (high affinity) towards glucose, which is 463.8 mu M, up to 2-fold exponential range lower compared to glucose oxidase. The heterogeneous electron transfer coefficient (K-s) 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 mu W cm(-2), than the GOX-menadione system, 308.03 +/- 17.93 mu W cm(-2), under low glucose concentration, 5 mM, which is the concentration in normal physiological fluid. English ROYAL SOC CHEMISTRY High performance enzyme fuel cells using a genetically expressed FAD-dependent glucose dehydrogenase alpha-subunit of Burkholderia cepacia immobilized in a carbon nanotube electrode for low glucose conditions Article 10.1039/c3cp51864g 1 PHYSICAL CHEMISTRY CHEMICAL PHYSICS, v.15, no.24, pp.9508 - 9512 PHYSICAL CHEMISTRY CHEMICAL PHYSICS 15 24 9508 9512 N scie scopus 000319576500007 2-s2.0-84878715644 Chemistry, Physical Physics, Atomic, Molecular & Chemical Chemistry Physics Article CATALYTIC SUBUNIT CLONING OXIDASE