Tuning of lipid bilayer fluidity regulates mediated electron transfer reactions of glucose oxidase immobilized on lipid bilayer films on an electrode

Abstract

A ferrocene with double long chains, 2C 16GluFc, was synthesized and mediated electron transfer reactions of glucose oxidase, immobilized on a lipid cast film containing the ferrocene, were examined. A basal plane pyrolytic graphite (BPG) electrode modified with a cast of 2C 16GluFc and a synthetic lipid, dihexadecyldimethylammonium bromide (2C 16N +Br −) gave phase transition dependent cyclic voltammograms. Normal pulse voltammetry proved that the enhancement of the faradaic current at the electrode at temperatures above the phase transition is ascribable to the increase in the apparent diffusion rate constants. Glucose oxidase was immobilized on the cast film of 2C 16GluFc/2C 16N +Br − on BPG and ferrocene-mediated catalytic electron transfer reactions in the presence of glucose were explored. Temperature experiments have revealed that the tunning of the lipid bilayer fluidity between crystal-to-liquid crystalline phase regulates the catalytic electron transfer reaction.