Bifunctional trehalose anode incorporating two covalently linked enzymes acting in series.

Michelle Rasmussen, Richard West, Jim Burgess, Irene Lee, Daniel Alberto Scherson

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

A bienzymatic electrode incorporating trehalase (Tre) and glucose oxidase (GOx) covalently bound to the surface of Pt through a functionalized thiol linker (Tre|GOx|Pt) has been designed and assembled and its catalytic properties examined by chemical and electrochemical methods in aqueous phosphate buffer solutions (PBS, pH 7.4). Exposure of Tre|GOx|Pt to PBS containing trehalose (Tr) and subsequent polarization at 0.6 V versus Ag/AgCl yielded after a few minutes well-defined steady-state currents ascribed to the oxidation of hydrogen peroxide generated by the GOx-mediated oxidation of glucose (Gl) produced by the Tre-mediated dissociation of Tr. Plots of the steady-state currents versus [Tr] over the range examined, i.e., 5-25 mM, were found to be linear. Implications of these results toward the development of an implantable biofuel cell as an autonomous energy conversion device for insects are discussed.

Original languageEnglish
Pages (from-to)7408-7411
Number of pages4
JournalAnalytical chemistry
Volume83
Issue number19
DOIs
Publication statusPublished - 2011 Jan 1
Externally publishedYes

    Fingerprint

ASJC Scopus subject areas

  • Analytical Chemistry

Cite this