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Covalent immobilization of FAD and glucose oxidase on carbon electrodes
Author(s) -
Sonawat H. M.,
Phadke Ratna S.,
Govil G.
Publication year - 1984
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260260908
Subject(s) - glucose oxidase , covalent bond , chemistry , carbon fibers , electrode , biochemistry , enzyme , organic chemistry , materials science , composite number , composite material
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.