Journal
ELECTROANALYSIS
Volume 24, Issue 4, Pages 931-937Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/elan.201100677
Keywords
Laccase; Colloidal gold particles; Carbon black; Oxygen reduction; Enzyme immobilization
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Funding
- AFOSR MURI on Fundamentals and Bioengineering of Enzymatic Fuel Cells (UNM)
- [MR 2D100]
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Functional composites of carbon and gold nanoparticles create a hierarchical architecture that facilitates high enzyme loading. Subsequent immobilization of the multicopper oxidase, Trametes versciolor laccase, was optimal with dithiobis- (succinimidyl propionate), due to the formation of thiol bonds between the protein molecules and gold. The immobilized laccase catalyzed oxygen reduction, with an onset potential of similar to 0.6 V (vs. Ag/AgCl), indicated effective orientation of the enzyme redox center to enable direct electron transport between enzyme and the composite electrode. Current densities in half-cell configurations provide scalable outputs of 50-80 mu A/cm(2) with the optimized electrode design. The methodology herein describes a rapid, facile preparation of gold-decorated carbon composite materials for use as electrode scaffolds that can be integrated into a range of bioelectronic devices.
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