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Article Dans Une Revue Langmuir Année : 2011

Multiscale-Tailored Bioelectrode Surfaces for Optimized Catalytic Conversion Efficiency

Résumé

We describe the elaboration of a multiscale-tailored bioelectrocatalytic system. The combination of two enzymes, d-sorbitol dehydrogenase and diaphorase, is studied with respect to the oxidation of d-sorbitol as a model system. The biomolecules are immobilized in an electrodeposited paint (EDP) layer. Reproducible and efficient catalysis of d-sorbitol oxidation is recorded when this system is immobilized on a gold electrode modified by a self-assembled monolayer of 4-carboxy-(2,5,7-trinitro-9-fluorenylidene)malonitrile used as a mediator. The insertion of mediator-modified gold nanoparticles into the EDP film increases significantly the active surface area for the catalytic reaction, which can be further enhanced when the whole system is immobilized in macroporous gold electrodes. This multiscale architecture finally leads to a catalytic device with optimized efficiency for potential use in biosensors, bioelectrosynthesis, and biofuel cells.
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Dates et versions

hal-01941841 , version 1 (02-12-2018)

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Yémima Bon Saint Côme, Hélène Lalo, Zhijie Wang, Mathieu Etienne, Janine Gajdzik, et al.. Multiscale-Tailored Bioelectrode Surfaces for Optimized Catalytic Conversion Efficiency. Langmuir, 2011, 27 (20), pp.12737-12744. ⟨10.1021/la201930m⟩. ⟨hal-01941841⟩
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