Journal
ENERGY & ENVIRONMENTAL SCIENCE
Volume 8, Issue 7, Pages 2069-2074Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c5ee01189b
Keywords
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Funding
- ANR [10-IANN-0-02]
- PICS CNRS [06344]
- Labex ARCANE [ANR-11-LABX-0003-01]
- National Research Foundation, Prime Minister's Office, Singapore
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Horseradish peroxidase (HRP) was immobilized on redox buckypapers followed by electropolymerization of pyrrole-modified concanavalin A enabling the subsequent additional immobilization of the glycoprotein glucose oxidase (GOx). Biocatalytic buckypapers were formed using pyrene-modified 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) or bis-Pyr-ABTS, a redox mediator, as a cross-linker. ABTS-functionalized buckypaper enhances the electron transfer of the bioelectrocatalytic reduction of H2O2 by HRP. Since H2O2 is produced during glucose oxidation by GOx in the presence of oxygen, the bienzymatic GOx-HRP biocathode achieves the complete reduction of oxygen into water. A clearly improved performance of the biocathode was obtained by using an improved biocompatible immobilization strategy, enabling the prevention of enzyme loss while ensuring both diffusion of glucose and O-2 and the local production of H2O2. These freestanding flexible oxygen-reducing biocathodes can operate under physiological conditions and show a high onset potential at 0.60 (+/- 0.01) V. In the presence of glucose (5 mM), such biocathodes exhibit a stable current density output of 1.1 (+/- 0.1) mA cm(-2) at 0.1 V under continuous one-hour discharge. Furthermore, a marked increase in lifetime was observed, the biocathode displaying 64% of its initial electrocatalytic activity after 15 days.
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