Journal
BIOELECTROCHEMISTRY
Volume 106, Issue -, Pages 56-63Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.bioelechem.2015.04.005
Keywords
FAD-dependent glucose dehydrogenase; Bilirubin oxidase; Serum; Glucose; Oxygen
Funding
- National Science Foundation [CHE-1057597]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1057597] Funding Source: National Science Foundation
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Flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH) is emerging as an oxygen-insensitive alternative to glucose oxidase (GOx) as the biocatalyst for bioelectrodes and bioanodes in glucose sensing and glucose enzymatic fuel cells (EFCs). Glucose EFCs, which utilize oxygen as the oxidant and final electron acceptor, have the added benefit of being able to be implanted within living hosts. These can then produce electrical energy from physiological glucose concentrations and power internal or external devices. EFCs were prepared with FAD-GDH and bilirubin oxidase (BOx) to evaluate the suitability of FAD-GDH within an implantable setting. Maximum current and power densities of 186.6 +/- 7.1 mu A cm(-2) and 39.5 +/- 1.3 mu W cm(-2) were observed when operating in human serum at 21 degrees C, which increased to 285.7 +/- 31.3 mu A cm(-2) and 57.5 +/- 5.4 mu W cm(-2) at 37 degrees C. Although good stability was observed with continual near-optimal operation of the EFCs in human serum at 21 degrees C for 24 h, device failure was observed between 13-14 h when continually operated at 37 degrees C. (C) 2015 Elsevier B.V. All rights reserved.
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