Enzyme catalysis at hydrogel-modified electrodes with soluble redox mediator

The kinetics of amperometric enzyme electrodes are reported for glucose oxidase immobilized in three different bovine serum albumin (BSA) hydrogel modified electrodes using as soluble electron mediator either ferrocene sulfonate or a pentammine(pyrazine)ruthenium complex. The effect of hydrogel laye...

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Detalles Bibliográficos
Autor principal: Battaglini, Fernando
Otros Autores: Calvo, E.J
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1994
Acceso en línea:Registro en Scopus
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Registro en la Biblioteca Digital
Aporte de:Registro referencial: Solicitar el recurso aquí
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100 1 |a Battaglini, Fernando 
245 1 0 |a Enzyme catalysis at hydrogel-modified electrodes with soluble redox mediator 
260 |c 1994 
270 1 0 |m Calvo, E.J.; Departamento de Química Inorgánica, Analítica y Química Física, Universidad de Buenos Aires, Ciudad Universitaria, 1420 Buenos Aires, Argentina 
506 |2 openaire  |e Política editorial 
520 3 |a The kinetics of amperometric enzyme electrodes are reported for glucose oxidase immobilized in three different bovine serum albumin (BSA) hydrogel modified electrodes using as soluble electron mediator either ferrocene sulfonate or a pentammine(pyrazine)ruthenium complex. The effect of hydrogel layer thickness, enzyme loading, substrate and redox mediator concentrations on the amperometric response are reported. The kinetic data are analysed in terms of physico-chemical model that takes into account diffusion of substrate, redox mediator and non-linear kinetics in the hydrogel layer and external mass transport in the electrolyte outside the enzyme layer. Analytical solutions for selected conditions are presented and tested with experimental results. Simulated concentration profiles give an insight into the detailed diffusion-kinetic process and allow the conditions under which the analytical equations are valid to be tested. No difference in the enzyme kinetic pattern (ping-pong mechanism for glucose oxidase) is found for soluble enzyme and for immobilized glucose oxidase (GOx). Rate coefficients are reported for the two redox mediators.  |l eng 
593 |a Departamento de Química Inorgánica, Analítica y Química Física, Universidad de Buenos Aires, Ciudad Universitaria, 1420 Buenos Aires, Argentina 
593 |a Department of Chemistry and Biochemistry, Concordia University, 1455 de Maisonneuve Blvd. West, Montreal, Que., Canada 
593 |a Argentine Science Research Council (CONICET), Argentina 
700 1 |a Calvo, E.J. 
773 0 |d 1994  |g v. 90  |h pp. 987-995  |k n. 7  |x 09565000  |t Journal of the Chemical Society, Faraday Transactions 
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