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Coimmobilization of dehydrogenases and their cofactors in electrochemical biosensors.


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.

SUBMITTER: Zhang M 

PROVIDER: S-EPMC3906728 | biostudies-literature | 2007 Mar

REPOSITORIES: biostudies-literature

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Coimmobilization of dehydrogenases and their cofactors in electrochemical biosensors.

Zhang Maogen M   Mullens Conor C   Gorski Waldemar W  

Analytical chemistry 20070214 6


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  ...[more]

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