A High Power Buckypaper Biofuel Cell: Exploiting 1,10-Phenanthroline-5,6-dione with FAD-Dependent Dehydrogenase for Catalytically-Powerful Glucose Oxidation
نویسندگان
چکیده
منابع مشابه
Novel FAD-dependent glucose dehydrogenase for a dioxygen-insensitive glucose biosensor.
A novel FAD-dependent glucose dehydrogenase (FAD-GDH) was found and its enzymatic property for glucose sensing was characterized. FAD-GDH oxidized glucose in the presence of some artificial electron acceptors, except for O2, and exhibited thermostability, high substrate specificity and a large Michaelis constant for glucose. FAD-GDH was applied to an amperometric glucose sensor with Fe(CN)6(3-)...
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In this study, different flavin adenine dinucleotide (FAD)-dependent glucose dehydrogenases (FADGDHs) were characterized electrochemically after "wiring" them with an osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)(2)(PVI)(10)Cl](+) on graphite electrodes. One tested FADGDH was that recently discovered in Glomerella cingulata (GcGDH), another was the recombinant form expressed in Pichia...
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The flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH) from Aspergillus species require suitable redox mediators to transfer electrons from the enzyme to the electrode surface for the application of bioelectrical devices. Although several mediators for FAD-GDH are already in use, they are still far from optimum in view of potential, kinetics, sustainability, and cost-effectiv...
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Enzyme-based biofuel cells (EBFCs) are systems that use a variety of organic compounds to produce electricity through oxido-reductase enzymes, such as oxidase or dehydrogenase as biocatalysts immobilized on electrodes. In this study, a single-chamber EBFC consisting of carbon electrodes that operating at ambient temperature in phosphate buffer, pH 7 is reported. The EBFC anode was based on gluc...
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ژورنال
عنوان ژورنال: ACS Catalysis
سال: 2017
ISSN: 2155-5435,2155-5435
DOI: 10.1021/acscatal.7b00738