Enzyme electrode studies of glucose oxidase modified with a redox mediator.
Glucose oxidase modified by the covalent attachment of ferrocenecarboxylic acid or ferrocene-acetic 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.
Bartlett
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Department of Chemistry, University of Warwick, Coventry CV4 7AL, U.K.
Bradford
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VQ
Whitaker
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