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

Cardoso, Franciane Pinheiro; Neto, Sidney Aquino; Fenga, Paula Gonçalves; Ciancaglini, Pietro; Andrade, Adalgisa R. de

doi:10.1016/j.electacta.2012.12.004

Cited by 19 publications

(13 citation statements)

References 34 publications

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“…The loss in current was nil below 2.5 M methanol, it was 30% between 2. acetonitrile, acetone and various alcohols (vide infra). 276 De Andrade et al 277,278 have designed laccase-based EBFCs operating at pH 5 in presence of 100 mM methanol.…”

Section: Effect Of Methanolmentioning

confidence: 99%

“…54 reported the use of carbon cloth modified with polyamidoamine dendrimers for the immobilization of Tv-laccase using ABTS entrapped into polypyrrole films. 278 Minteer et al used a different approach. 510 Their carbon cloth electrode was first coated with a suspension of Nafion® modified with quaternary ammonium salt and containing bilirubin and Mv-BOD, and further soaked in 1 mM Ru(bpy)3 2+ to pre-concentrate the redox mediator in the membrane.…”

Section: Carbon Clothmentioning

confidence: 99%

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O₂Reduction in Enzymatic Biofuel Cells

2017

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Catalytic four-electron reduction of O to water is one of the most extensively studied electrochemical reactions due to O exceptional availability and high O/HO redox potential, which may in particular allow highly energetic reactions in fuel cells. To circumvent the use of expensive and inefficient Pt catalysts, multicopper oxidases (MCOs) have been envisioned because they provide efficient O reduction with almost no overpotential. MCOs have been used to elaborate enzymatic biofuel cells (EBFCs), a subclass of fuel cells in which enzymes replace the conventional catalysts. A glucose/O EBFC, with a glucose oxidizing anode and a O reducing MCO cathode, could become the in vivo source of electricity that would power sometimes in the future integrated medical devices. This review covers the challenges and advances in the electrochemistry of MCOs and their use in EBFCs with a particular emphasis on the last 6 years. First basic features of MCOs and EBFCs are presented. Clues provided by electrochemistry to understand these enzymes and how they behave once connected at electrodes are described. Progresses realized in the development of efficient biocathodes for O reduction relying both on direct and mediated electron transfer mechanism are then discussed. Some implementations in EBFCs are finally presented.

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Section: Effect Of Methanolmentioning

confidence: 99%

Section: Carbon Clothmentioning

confidence: 99%

O₂Reduction in Enzymatic Biofuel Cells

2017

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“…This is called the mediator (MET) type enzyme function electrode reaction, can be adapted to most of the oxidation-reduction enzyme system, the selection of the mediator, modification methods must be important [12][13][14][15][16].…”

Section: Trends In Green Chemistrymentioning

confidence: 99%

Anthraquinone and L-amino Acid Derivatives Schiff Base Cu(II) Complexes as a Mediator between Cathode of Biofuel Cell and Oxygen-reducing Laccase

Takeuchi¹,

Sunaga²,

Akitsu³

2017

Trends in Green chem

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“…Crystallographic data for 0 (CCDC 1455901): C 46 H 32 CuN 2 O 3 , 0.31 × 0.15 × 0.10 mm 3 , M w = 772.27, monoclinic, P2 1 (#4), a = 12.6752(13), b = 7.8327(8), c Fig. 4 showed a spectroelectrochemical proof of mediator function of 0 (reduction of oxygen is at about 540 mV generally [9,10]), and that intermediate species exist in the new complex, in other words, quinone moiety of the ligand should be considered as the anion structure.…”

Section: Methodsmentioning

confidence: 99%

Anthraquinone Derivative Chiral Schiff Base Copper(II) Complexes for Enzyme Type Bio-Fuel Cell Mediators

Takeuchi¹,

Akitsu²

2016

JEE

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Electrochemically, laccase, a family of multi-copper oxidase, has specificity for performing not only one-electron oxidation of phenolic-related compounds but also four-electron reduction of oxygen, which is expected to be a cathode of biofuel cells. We have prepared three amino-acid derivatives (for enhancing affinity to laccase) and one control (just for determining redox behavior of ligands and Cu(II/I)) copper(II) complexes 0-3 having phenolic-related ligands involving anthraquinone moiety. Enhancing current density of electron transfer between the cathode (composed of electron conducting materials such as Nafion and carbon nanotube) and laccase could be observed for all 1-3 acting as good mediators according to (spectro)electrochemical results.

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

Cited by 19 publications

References 34 publications

O₂Reduction in Enzymatic Biofuel Cells

O₂Reduction in Enzymatic Biofuel Cells

Anthraquinone and L-amino Acid Derivatives Schiff Base Cu(II) Complexes as a Mediator between Cathode of Biofuel Cell and Oxygen-reducing Laccase

Anthraquinone Derivative Chiral Schiff Base Copper(II) Complexes for Enzyme Type Bio-Fuel Cell Mediators

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

Cited by 19 publications

References 34 publications

O2Reduction in Enzymatic Biofuel Cells

O2Reduction in Enzymatic Biofuel Cells

Anthraquinone and L-amino Acid Derivatives Schiff Base Cu(II) Complexes as a Mediator between Cathode of Biofuel Cell and Oxygen-reducing Laccase

Anthraquinone Derivative Chiral Schiff Base Copper(II) Complexes for Enzyme Type Bio-Fuel Cell Mediators

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Product

Resources

About

O₂Reduction in Enzymatic Biofuel Cells

O₂Reduction in Enzymatic Biofuel Cells