Long-Term Operational Stability of a Mixed Glucose Oxidase-Redox Mediator-Carbon Paste Electrode
- 1 August 1991
- journal article
- research article
- Published by Taylor & Francis in Analytical Letters
- Vol. 24 (8) , 1293-1315
- https://doi.org/10.1080/00032719108052973
Abstract
The amperometric response of a mixed-glucose oxidase-redox mediator-carbon paste electrode, permanently poised at the operating potential, has been investigated in phosphate buffer as a function of glucose concentration over a period of four weeks.Keywords
This publication has 37 references indexed in Scilit:
- Amperometric response to reducing carbohydrates of an enzyme electrode based on oligosaccharide dehydrogenase. Detection of lactose and α-amylaseAnalytica Chimica Acta, 1990
- Conducting organic salt amperometric glucose sensor in continuous-flow monitoring using a wall-jet cellAnalytica Chimica Acta, 1990
- A glucose electrode based on carbon paste chemically modified with a ferrocene-containing siloxane polymer and glucose oxidase, coated with a poly(ester-sulfonic acid) cation-exchangerAnalytica Chimica Acta, 1990
- Construction and Characterization of a Beet Stem Based Biosensor for OxalateAnalytical Letters, 1989
- Miniature Tissue Based Voltammetric BioelectrodesAnalytical Letters, 1988
- Electrocatalytic oxidation of D-gluconate at a ubiquinone-mixed carbon paste electrode with an immobilized layer of D-gluconate dehydrogenase from bacterial membranes.Agricultural and Biological Chemistry, 1987
- Mediated amperometric biosensors for d-galactose, glycolate and l-amino acids based on a ferrocene-modified carbon paste electrodeAnalytica Chimica Acta, 1986
- Electrocatalytic oxidation of glucose at a glucose oxidase-immobilized benzoquinone-mixed carbon paste electrode.Agricultural and Biological Chemistry, 1986
- Effect of internal diffusion in heterogeneous enzyme systems: Evaluation of true kinetic parameters and substrate diffusivityJournal of Theoretical Biology, 1973
- A theoretical model describing steady-state catalysis by enzymes immobilized in spherical gel particles. Experimental study of α-chymotrypsin-sepharoseBiochemical and Biophysical Research Communications, 1971