Development of Laccase and Manganese Peroxidase Biocathodes for Microbial Fuel Cell Applications

Sahar Bakhshian
Department of Chemical and Petroleum Engineering, Sharif University of Technology, Tehran, Iran

Hamid-Reza Kariminia
Department of Chemical and Petroleum Engineering, Sharif University of Technology, Tehran, Iran

Ladda ner artikelhttp://dx.doi.org/10.3384/ecp110571197

Ingår i: World Renewable Energy Congress - Sweden; 8-13 May; 2011; Linköping; Sweden

Linköping Electronic Conference Proceedings 57:9, s. 1197-1204

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Publicerad: 2011-11-03

ISBN: 978-91-7393-070-3

ISSN: 1650-3686 (tryckt), 1650-3740 (online)


In this study; we ivestigated how microbial fuel cell (MFC) performance can be affected by laccase and manganese peroxidase (MnP) enzymes as catalysts in the cathode compartment. Commercial laccase was immobilized by crosslinking on chitosan using glutaraldehyde. Immobilized enzyme was settled on graphite electrode previously covered with polymerized methylene blue. Application of this enzymatic electrode was investigated in the cathode chamber of a MFC. Output power density of the MFC in the mentioned situation was 100% higher than that for the graphite electrode. The MnP was first; produced from a white rot fungus isolate and was immobilized on the graphite electrode via adsorption. This modified electrode with MnP was utilized as cathode. The fuel cell with MnP modified graphite electrode and H2O2 as oxidizer yielded the maximum power density of 46 mW/m2 at the current density of 109 mA/m2. This augmentation of MFC performance was due to a higher cathode electrode potential with H2O2 rather than oxygen. The most important function of MnP was to catalyze the reduction of H2O2 and hence diminished activation overpotential loss of the cathode.


Biocathode; Laccase; Manganese peroxidase; Microbial fuel cell


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