Designing of cathodes modified with enzymes for the biofuel cell applications

Maciej Klis 1Jerzy Rogalski 2Marcin Karbarz 1Zbigniew Stojek 1Renata Bilewicz 1

1. Warsaw University, Faculty of Chemistry, Pasteura 1, Warszawa 02-093, Poland
2. Maria Curie Sklodowska University, Department of Biochemistry, Pl. Sklodowskiej 3, Lublin 20-031, Poland


Biocatalysts are employed in biofuel cells for the conversion of chemical energy to electrical energy. The enzymes can be used in one of two ways. Either the biocatalysts can generate the fuel substrates for the cell by biocatalytic transformations or metabolic processes, or the biocatalysts may participate in the electron transfer chain between the fuel substrates and the electrode surfaces. Unfortunately, most of redox enzymes do not take part in direct electron transfer with the conductive supports, and therefore a variety of electron mediators are used for the electrical wiring of the biocatalyst to the electrode.


An important condition for the progress in biotechnology is to understand the electrochemical reactions of redox proteins and to control their interactions with gold substrates. Gold is often used as the electrode material due to its inertness. One of the crucial steps in the development of electrodes for biofuel cells is the appropriate immobilization of the enzyme on gold, since its biological activity as well as electrical contact have to be preserved.
Laccase (EC is a blue multi-copper enzyme which catalyses the oxidation of a variety of phenolic and amine compounds simultaneously with the four-electron reduction of molecular oxygen to water. The enzyme active site contains four copper atoms of types I, II, and III, which play different roles in the enzymatic process. Substrates are oxidized near the T1 site, and the electrons are transferred to the T2/T3 cluster, where molecular oxygen is reduced.
We employed several strategies to immobilize laccase on gold, such as electrostatic adsorption on gold clusters, entrappment of the enzyme in poly(N-isopropylacrylamide) gel (NIPA) and covalent attachment to self-assembled organothiols monolayers (SAMs).


In case of NIPA gel matrix the immobilized laccase showed electroactivity at 0.360 V vs. NHE, however, upon binding to 11-mercaptoundecanoic acid (MUA) the Cu center is electroactive at a more positive potential (590 V vs. NHE). The catalytic current of oxygen reduction was observed in case of Au cluster/laccase modified electrode. For the MUA/laccase electrode, for both mediatorless and mediated with 1,1'-ferrocenedimethanol processes, the catalytic oxygen reduction was observed. Hence, best results obtained so far are those based on 11-mercaptoundecanoic acid (MUA) as the molecular bridge.

Legal notice
  • Legal notice:

    Copyright (c) Pielaszek Research, all rights reserved.
    The above materials, including auxiliary resources, are subject to Publisher's copyright and the Author(s) intellectual rights. Without limiting Author(s) rights under respective Copyright Transfer Agreement, no part of the above documents may be reproduced without the express written permission of Pielaszek Research, the Publisher. Express permission from the Author(s) is required to use the above materials for academic purposes, such as lectures or scientific presentations.
    In every case, proper references including Author(s) name(s) and URL of this webpage: must be provided.


Related papers
  1. Recent developments in enzymatic biofuel cells
  2. Biofuel cell based on carbon nanotubes with covalently bonded laccase and glucose dehydrogenase embedded in cubic phase
  3. Tetraazamacrocyclic copper(II) and nickel(II) complexes in host - guest systems.
  4. Free-radical adsorption as a method of binding gold nanoparticles to gold electrode surfaces.
  5. Biofuel cell based on arylated carbon nanotubes
  6. Carbon nanotube nanostructured electrodes for membrane – less biofuel cell based on liquid-crystalline phases as matrices for enzymes
  7. Cyclodextrins as molecular recognition elements in monolayers
  8. A facile preparation of the nanoparticulate film from conductive and nonconductive particles of the opposite charge
  9. Poly-o-aminophenol as laccase mediator and influence of enzyme on the polymer electrodeposition
  10. Bioelectrocatalytic dioxygen reduction at carbon nanotubes – silicate composite film modified electrode
  11. A glucose/O2 biofuel cell based on electrodes modified with liquid-crystalline cubic phases
  12. Redox processes of dithiolated tetraazamacrocyclic complexes of Ni(II) and Cu(II) in solution and immobilized on gold electrodes
  13. Immobilization of molecules: From self-assembled monolayers to polymeric hollow structures
  14. Scanning electrochemical microscopy study of laccase embedded in sol-gel processed silicate film
  15. Nanostructured Carbon Electrodes For Oxygen Reduction Catalyzed By Laccase Without any Mediators
  16. Optimization of culture medium for laccase production by Trametes versicolor
  17. ß-Glucosidases from white rot fungus Phlebia radiata - purification and properties.
  18. Molecular Motions in New Catenanes
  19. New methods of immobilization of oxidases at electrodes
  20. Electron transport through alkanethiolate films decorated with monolayer-protected gold clusters
  21. Fine-tuning of properties of bismacrocyclic dinuclear cyclidene receptors by N-methylation.
  22. Thermoresponsive polymeric hydrogels anchored at gold surfaces and used as matrix for enzymes
  23. Lipidic cubic phase for immobilising enzymes on electrodes
  24. Properties of monolayers of azocrown ethers: Ph -tunable equilibria for compounds with substituents containing mobile protons
  25. Electrocatalytic reduction of dioxygen by redox mediator and laccase immobilised in silicate thin film
  26. Modified Electrodes Based on Lipidic Cubic Phases

Presentation: Poster at SMCBS'2005 Workshop, by Maciej Klis
See On-line Journal of SMCBS'2005 Workshop

Submitted: 2005-07-31 16:22
Revised:   2009-06-07 00:44
© 1998-2021 pielaszek research, all rights reserved Powered by the Conference Engine