Covalent immobilization of FAD and glucose oxidase on carbon electrodes.
The effectiveness of attaching flavin adenine dinucleotide (FAD) via a C bridge to Teflon-bonded carbon black (CB), and the subsequent immobilization of glucose oxidase on the FAD-modified electrodes has been studied by cyclic voltammetry. When FAD alone is bound to the electrode, it undergoes reduction and oxidation at -0.62 and -0.5 V, respectively-values similar to those obtained with free FAD. Compared to the free enzyme, the reduction of FAD as part of the immobilized enzyme is 200 mV more cathodic, while the oxidation potential remains the same in both cases.
Sonawat
H M
HM
Biochemical Fuel Cells Project, Chemical Physics Group, Tata Institute of Fundamental Research, Homi Bhabha Road, Bombay 400 005, India.
Phadke
R S
RS
Govil
G
G