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ENZYME ELECTRODE STUDIES OF GLUCOSE-OXIDASE MODIFIED WITH A REDOX MEDIATOR

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UNSPECIFIED (1991) ENZYME ELECTRODE STUDIES OF GLUCOSE-OXIDASE MODIFIED WITH A REDOX MEDIATOR. TALANTA, 38 (1). pp. 57-63. ISSN 0039-9140

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Abstract

Glucose oxidase modified by the covalent attachment of ferrocenecarboxylic acid or ferroceneacetic acid groups undergoes direct oxidation at metal electrodes. Studies of the comparative stability of the two modified enzymes on storage and on electrochemical cycling show that the material modified with ferroceneacetic acid is the more stable. Amperometric studies of enzyme electrodes based on these modified forms of glucose oxidase show that their application in practical biosensors is severely limited by the poor stability of the oxidized form of the covalently attached ferrocene mediator. A comparison of the results obtained with the native enzyme and with that modified with ferroceneacetic acid, for the oxidation of glucose, D-mannose, 2-deoxy-D-glucose, D-xylose and D-galactose, suggests that the modification procedure has little effect on the selectivity of the enzyme.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Journal or Publication Title: TALANTA
Publisher: ELSEVIER SCIENCE BV
ISSN: 0039-9140
Date: January 1991
Volume: 38
Number: 1
Number of Pages: 7
Page Range: pp. 57-63
Publication Status: Published
URI: http://wrap.warwick.ac.uk/id/eprint/22886

Data sourced from Thomson Reuters' Web of Knowledge

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