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Utilization of FAD-Glucose Dehydrogenase from T. emersonii for Amperometric Biosensing and Biofuel Cell Devices

[Image: see text] 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 thermop...

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Detalles Bibliográficos
Autores principales: Cohen, Roy, Bitton, Rachel E., Herzallh, Nidaa S., Cohen, Yifat, Yehezkeli, Omer
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2021
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8631703/
https://www.ncbi.nlm.nih.gov/pubmed/34383460
http://dx.doi.org/10.1021/acs.analchem.1c02157
Descripción
Sumario:[Image: see text] 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/cm(2) in a biofuel cell device.