Aldose dehydrogenase-modified carbon paste electrodes as amperometric aldose sensors
✍ Scribed by Maria Smolander; György Marko-Varga; Lo Gorton
- Book ID
- 102984539
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 747 KB
- Volume
- 302
- Category
- Article
- ISSN
- 0003-2670
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✦ Synopsis
A biosensor using pyrroloquinoline quinone-dependent aldose dehydrogenase (ALDH) as a biological component was developed and used for the measurement of the aldose sugars xylose and glucose. Different immobilization methods for ALDH in carbon paste were studied. The best electrode performance was obtained when ALDH was adsorbed on the surface of a carbon paste electrode. Several mediator compounds were mixed into the carbon paste. The lowest working potential and highest catalytic current were obtained with dimethylferrocene as a mediator. Both storage and operational stability of the ALDH electrodes could be improved by the application of a membrane consisting of a poly(ester-sulfonic acid) cation-exchanger, Eastman AQ-29D. Application of the membrane reduced the non-specific oxidation of fermentation samples on the electrode surface.
📜 SIMILAR VOLUMES
The aim of this work was to improve an aldose-detecting biosensor based on quinoprotein aldose dehydrogenase (ALDH). Polymer-bound ferrocene derivatives with four different structures were studied as electron transfer mediators between the coenzyme of ALDH, pyrroloquinoline qninone (PQQ), and the co
A new enzymatic amperometric sensor for hydrogen peroxide based on a modified carbon paste electrode is described. Horseradish peroxidase and ferrocene mediator were immobilized by dissolution or dispersion in a graphite-paraffin oil paste. To prevent losses of immobilized chemicals under operationa