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Updated: Feb 27, 2026

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
Published on: July 11, 2012
Bioanode with alcohol dehydrogenase undergoing a direct electron transfer on functionalized gold nanoparticles for an
D Ratautas1, L Tetianec1, L Marcinkevičienė2
1Faculty of Fundamental Sciences, Vilnius Gediminas Technical University, Saulėtekio al. 11, LT-10223 Vilnius, Lithuania; Institute of Biochemistry, Life Sciences Centre, Vilnius University, Saulėtekio al. 7, LT-10223 Vilnius, Lithuania.
Abstract:
In this paper we designed and investigated bioanode with alcohol dehydrogenase (ADH) catalysing oxidation of glycerol and glyceraldehyde. The most effective bioanode was fabricated when ADH was immobilized on gold nanoparticles (AuNPs) modified with 4-aminothiophenol. This electrode catalysed the oxidation of both glycerol and glyceraldehyde thus demonstrating a consecutive two-step process. The bioanode generated the current density of 510µAcm-2 at pH 7.0 and 0V vs. SCE. It was demonstrated that the electrode acted effectively due to the direct electron exchange between heme of ADH and modified AuNPs. The reversible oxidation and reduction of ADH heme proceeded at around -0.05V vs. SCE. The turnover number of the immobilized enzyme was estimated to be 65s-1 which is the same as the catalytic number of the enzyme in solution. To the best of our knowledge those parameters are the highest currently reported for the alcohol dehydrogenase bioanodes operating utilizing a direct electron transfer. As a proof of biofuels cell conception, the bioanode was combined with AuNPs-laccase biocathode. The biofuel cell generated maximum power output of 130µWcm-2 at 0.5V and pH 7.0.
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