Abstract
Flavin-dependent glucose dehydrogenases (FAD-GDH) are oxygen-independent enzymes with high potential to be used as biocatalysts in glucose biosensing applications. Here, we present the construction of an amperometric biosensor and a biofuel cell device, which are based on a thermophilic variant of the enzyme originated from Talaromyces emersonii. The enzyme overexpression in Escherichia coli and its isolation and performance in terms of maximal bioelectrocatalytic currents were evaluated. We examined the biosensor’s bioelectrocatalytic activity in 2,6-dichlorophenolindophenol-, thionine-, and dichloro-naphthoquinone-mediated electron transfer configurations or in a direct electron transfer one. We showed a negligible interference effect and good stability for at least 20 h for the dichloro-naphthoquinone configuration. The constructed biosensor was also tested in interstitial fluid-like solutions to show high bioelectrocatalytic current responses. The bioanode was coupled with a bilirubin oxidase-based biocathode to generate 270 μW/cm2 in a biofuel cell device.
Highlights
glucose dehydrogenase (GDH)) are oxygen-independent enzymes with high potential to be used as biocatalysts in glucose biosensing applications
O2 on aninteolecHtro2Ode2.,4−w6 hAicshthies oxidation of one glucose correlates to one hydrogen peroxide molecule, the concentration of glucose is inferred from the bioelectrocatalytic current caused by the H2O2 electrochemical reaction
While some advances have been presented toward the development of amperometric glucose sensing using T. emersonii glucose dehydrogenase (TeGDH),[30] methods to structurally support the enzyme on the electrodes and its activation at low overpotential are required to allow continuous operation
Summary
GDH) are oxygen-independent enzymes with high potential to be used as biocatalysts in glucose biosensing applications.
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