4.8 Article

Enzyme-catalyzed biocathode in a photoelectrochemical biofuel cell

Journal

JOURNAL OF POWER SOURCES
Volume 267, Issue -, Pages 617-621

Publisher

ELSEVIER
DOI: 10.1016/j.jpowsour.2014.05.138

Keywords

Biocathode; Horseradish peroxidase; H-2-mesoporphyrin IX; Photoelectrochemical biofuel cell

Funding

  1. Administration of Traditional Chinese Medicine of JiLin Province [YJS-0206]
  2. National Basic Research Program of China (973 Program) [2011CB935702]

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A novel double-enzyme photoelectrochemical biofuel cell (PEBFC) has been developed by taking glucose dehydrogenase (GDH) and horseradish peroxidase (HRP) as the enzyme of the photoanode and biocathode to catalyze the oxidation of glucose and the reduction of oxygen. A H-2-mesoporphyrin IX is used as a dye for a TiO2 film electrode to fabricate a photoanode. The horseradish peroxidase (HRP) is immobilized on a glassy carbon (GC) electrode to construct a biocathode which is used to catalyze the reduction of oxygen in the PEBFC for the first time. The biocathode exhibits excellent electrocatalytic activity in the presence of O-2. The performances of the PEBFC are obtained by current-voltage and power-voltage curves. The short-circuit current density (I-SC), the open-circuit voltage (V-oc), maximum power density (P-max), fill factor (FF) and energy conversion efficiency (eta) are 439 mu A cm(-2), 678 mV, 79 mu W cm(-2), 0.39 and 0.016%, respectively, and the incident photon-to-collected electron conversion efficiency (IPCE) is 32% at 350 nm. The I-SC is higher than that of the PEBFC with Pt cathode, and the V-oc, is higher than that of the dye-sensitized solar cell or the enzyme-catalyzed biofuel cell operating individually, which demonstrates that the HRP is an efficient catalyst for the biocathode in the PEBFC. (C) 2014 Elsevier B.V. All rights reserved.

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