Bioelectrocatalysis of Fructose Dehydrogenase at Polyanilline-Modified Electrodes
In this study we have investigated whether it is possible to connect the multi-domain enzyme fructose dehydrogenase FDH with electrodes using the same group of polymers. The interaction of a sulfonated and methoxy-substituted polyanilline with FDH is studied in solution using UV/Vis spectroscopy. It can be demonstrated that electron transfer from the substrate reduced enzyme to the polymer is feasible, but also that this interaction is enhanced by the presence of calcium ions. Subsequently the reaction has been investigated by electrochemical means with all partners in solution verifying the spectroscopic results. In a next step of development the enzyme has been fixed on planar ITO electrodes by means of a polymer layer. Such an enzyme electrode exhibits effective, substrate-induced bioelectrocatalysis starting at rather low potential (~0mV vs Ag/AgCl). The efficiency can be significantly enhanced when macroporous ITO electrodes are used. They have pore size diameters of ~ 300nm and allow incorporation of higher amounts of polymer and enzyme. A current enhancement of ~ 35 is found compared to the flat ITO. The study demonstrates that sulfonated polyanillines can be considered as valuable matrices in connecting redox enzymes with electrodes.
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