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Electrochemical characterization of methanol/O2 biofuel cell: Use of laccase biocathode immobilized with polypyrrole film and PAMAM dendrimers

Cardoso, F.P. ; Aquino Neto, S. ; Fenga, P.G. ; Ciancaglini, P. ; De andrade, A.R.

Electrochimica acta, 2013-02, Vol.90, p.90-94 [Periódico revisado por pares]

Elsevier Ltd

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  • Título:
    Electrochemical characterization of methanol/O2 biofuel cell: Use of laccase biocathode immobilized with polypyrrole film and PAMAM dendrimers
  • Autor: Cardoso, F.P. ; Aquino Neto, S. ; Fenga, P.G. ; Ciancaglini, P. ; De andrade, A.R.
  • Assuntos: ABTS ; Biofuel cell ; Dendrimers ; Density ; Electrochemical analysis ; Enzymes ; Fuels ; Immobilization ; Laccase ; Methyl alcohol ; PAMAM ; Polypyrroles ; Pyrrole
  • É parte de: Electrochimica acta, 2013-02, Vol.90, p.90-94
  • Notas: ObjectType-Article-2
    SourceType-Scholarly Journals-1
    ObjectType-Feature-1
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  • Descrição: This paper describes the performance of a mediated electron transfer (MET) biocathode for a methanol/O2 biofuel cell. To this end, we employed PAMAM (polyamidoamine) dendrimers for the immobilization of laccase using 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonate) diammonium salt (ABTS) in solution or entrapped into polypyrrole films. We used the enzyme immobilized onto the carbon platform obtained either in the presence or in the absence of the electropolymerized film to determine kinetic parameters. The results point to a very similar kinetic rate conversion in both situations; however, substrate affinity seems to increase in the bioelectrode containing the entrapped substrate molecules. The electrochemical characterization tests confirmed that the electropolymerized polypyrrole film was able to retain entrapped ABTS molecules. Additionally, laccase provides enhanced catalytic oxidation current for the mediator compared with the control sample containing PAMAM dendrimer only. Compared to the control sample, which gave power density values around 0.7μWcm−2, tests employing ABTS as mediator furnished 6μWcm−2 when the mediator was added in solution and around 25μWcm−2 when it was entrapped into the biocathode layers. Overall, the developed biocathode is environmentally friendly for immobilization of the enzyme laccase, being satisfactorily stable in the kinetic tests and affording good power data in the biofuel cell tests.
  • Editor: Elsevier Ltd
  • Idioma: Inglês

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