AI Article Synopsis
- The study develops a bioelectrocatalytic system that combines two enzymes—D-sorbitol dehydrogenase and diaphorase—to efficiently oxidize D-sorbitol.
- The enzymes are immobilized in an electrodeposited paint layer on a gold electrode modified with a special monolayer that acts as a mediator.
- The use of mediator-modified gold nanoparticles and macroporous gold electrodes significantly enhances the catalytic efficiency, making the system promising for applications in biosensors, bioelectrosynthesis, and biofuel cells.
Article Abstract
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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