Over 7,000 peer reviewed articles have been published on electrochemical glucose assays and sensors over recent years. Their number makes a full review of the literature, or even of the most recent advances, impossible. Nevertheless, this chapter should acquaint the reader with the fundamentals of the electrochemistry of glucose and provide a perspective of the evolution of the electrochemical glucose assays and monitors helping diabetic people, who constitute about 5 % of the world’s population. Because of the large number of diabetic people, no assay is performed more frequently than that of glucose. Most of these assays are electrochemical. The reader interested also in nonelectrochemical assays used in, or proposed for, the management of diabetes is referred to a 2007 excellent review of Kondepati and Heise [1].

Electrochemical glucose sensors and their applications in diabetes management.

Selective detection in flow analysis based on the combination of immobilized enzymes and chemically modified electrodes

Polypyrrole-hydrogel composites for the construction of clinically important biosensors.

Glucose oxidase (EC 1.1.3.4) is the most widly employed enzyme as analytical reagent. This is the result of (1) its utility in the determination of glucose, an analyte of wide analytical interest, and (2) its relatively low cost and good stability that make the glucose/glucose oxidase system a very convenient model for method development (particularly in the area of biosensors). This review discusses in detail enzyme structure, biocatalysis, enzymes as analytical reagents, properties of glucose oxidase (including a historical account), and the use of glucose oxidase as an analytical reagent in homogeneous systems as well as an immobilized reagent.

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Glucose Oxidase as an Analytical Reagent

A novel FAD-dependent glucose dehydrogenase (FAD-GDH) was found and its enzymatic property for glucose sensing was characterized. FAD-GDH oxidized glucose in the presence of some artificial electron acceptors, except for O2, and exhibited thermostability, high substrate specificity and a large Michaelis constant for glucose. FAD-GDH was applied to an amperometric glucose sensor with Fe(CN)6(3-) as a soluble mediator. The use of a relatively high concentration of Fe(CN)6(3-) resulted in a good linearity between the current response and the glucose concentration, taking into account a large Michaelis constant for Fe(CN)6(3-). The glucose sensor was completely insensitive to O2 and responded linearly to glucose up to 30 mM. Compared to glucose, the response to other saccharides was negligible. The sensor can be stored at room temperature in a desiccator for at least one month without any change in the response or activity.

https://www.tandfonline.com/doi/pdf/10.1271/bbb.70.654

Novel FAD-Dependent Glucose Dehydrogenase for a Dioxygen-Insensitive Glucose Biosensor

Glucose oxidase was immobilized on the surface of a graphite electrode by irreversible adsorption. An electrocatalytic steady-state current for the oxidation of D-glucose was observed using this electrode in the presence of p-benzoquinone as an electron transfer mediator. The electrocatalytic current at 0.5 V vs. SCE was analyzed as a function of the concentrations of D-glucose and p-benzoquinone, and the maximum current, Ismax, and the Michaelis constants (K1 and K2 for D-glucose and p-benzoquinone, respectively) of the electrocatalysis were determined. The dependence of the current on the electrode potential, pH, and temperature was also investigated. The results indicate that the kinetics of the immobilized enzyme are essentially the same as those of the enzyme in the solubilized state. The effect of various electron transfer mediators on the electrocatalytic current was also examined and evaluated in terms of Ismax, K1, and K2 values.

Masugu Kamei

Papers

Electrocatalysis with a Glucose-Oxidase-immobilized Graphite Electrode