Coimmobilization of dehydrogenases and their cofactors in electrochemical biosensors.

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Zhang M, Mullens C, Gorski W

Coimmobilization of dehydrogenases and their cofactors in electrochemical biosensors.

Anal Chem. 2007 Mar 15;79(6):2446-50. Epub 2007 Feb 14.

PubMed ID

17298031 [ View in PubMed

]

Abstract

Enzyme-based reagentless biosensors were developed using the model system of glucose dehydrogenase (GDH) and its nicotinamide adenine dinucleotide cofactor (NAD+). The biosensors were prepared following an approach similar to the concept of molecular imprinting. To this end, the N1-carboxymethyl-NAD+ species were covalently attached to polyamino-saccharide chains of chitosan (CHIT) and allowed to interact with GDH in an aqueous solution. The bioaffinity interactions between the NAD+ and GDH were secured by cross-linking the system with the glutaric dialdehyde (GDI)-modified CHIT. Electron conductive films of such CHIT-NAD+-GDH-GDI-CHIT macrocomplexes (MC) were prepared on glassy carbon (GC) electrodes by adding carbon nanotubes (CNT) and evaporating water. Electrochemical analysis of the GC/CNT-MC electrodes revealed that, in contrast to the oxidase-based electrodes, they acted as oxygen-independent reagentless biosensors. The application of Nafion to such biosensors predictably improved their selectivity and, unexpectedly, enhanced their sensitivity by an order of magnitude.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
NADH	GDH/6PGL endoplasmic bifunctional protein	Protein	Humans	Unknown	Not Available	Details