Electron transfer between cellobiose dehydrogenase and graphite electrodes

Electron transfer between the enzyme cellobiose dehydrogenase (CDH) and a flavin adenine dinucleotide (FAD) containing a catalytic active fragment of CDH (FAD-fragment) and a graphite electrode, respectively, was established. The current response in the presence of the enzyme substrate for graphite electrodes with CDH or the FAD-fragment adsorbed on the freshly polished graphite surface were compared with that of electrodes where CDH or the FAD-fragment were crosslinked in a redox polymer at the electrode surface. The initial slope, djd[S]s = 0, where j is the current density and [S]s = 0 the zero substrate concentration, was taken as a measure of the substrate response. For the electrodes with enzymes adsorbed directly on the surface, djd[S]s = 0, was a factor of 3 lower than for electrodes prepared with the polymer mixture. The redox polymer based electrodes, with CDH and with FAD-fragment, both showed a high and close to equal substrate response. In contrast the surface adsorbed CDH gave a much higher substrate response than the FAD-fragment.