Oxidation of laccase for improved cathode biofuel cell performances
(2015) Bioelectrochemistry — Vol. 106, p. 77-87 (2015)
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- Graphite rodswere modified by substituted aryldiazoniumsalts allowing subsequent laccase immobilisation and direct electron transfer at the cathode. Two covalent enzyme immobilisation methods were performed with carboxy and amino substituted grafted groups, either via the formation of an amide bond or a Schiff base between the glycosidic groups of the enzyme and the amino groups on the electrode surface, respectively. Laccase adsorption efficiency was consistently compared to the covalent attachment method on the same carbon surface, showing that the latter method led to a higher immobilisation yield when the electrode surface was functionalised with carboxylic groups, as shown fromboth laccase activitymeasurement towards an organic reducing substrate, ABTS, and quantitative XPS analysis. Both analytical methods led to similar laccase surface coverage estimations. From activity measurements, when laccase was covalently immobilised on the electrode functionalised with carboxylic groups, the surface coverage was found to be 43 ± 2% whereas it was only 10 ± 3% when laccase was adsorbed. Biocatalysed dioxygen reduction current was also higher in the case of covalent immobilisation. For the first time, oxidised laccase performances were compared to unmodified laccase, showing significant improved efficiencywhen using oxidised laccase: the current obtainedwith oxidised laccasewas 141±37 μAcm-2 compared to 28 ± 6 μA cm-2 for unmodified laccase after covalent immobilisation of the enzyme on a graphite electrode functionalised with carboxylic groups. © 2015 Elsevier B.V.
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Zheng, M., Griveau, S., Dupont, C., Genet, M. J., & Jolivalt, C. (2015). Oxidation of laccase for improved cathode biofuel cell performances. Bioelectrochemistry, 106, 77-87. https://doi.org/10.1016/j.bioelechem.2015.06.004 (Original work published 2015)