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Reagentless Biosensor Based on Glucose Oxidase Wired by the Mediator Freely Diffusing in Enzyme Containing Membraneстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: Sekretaryova Alina N., Vokhmyanina Darya V., Chulanova Tatyana O., Karyakina Elena E., Karyakin Arkady A.
- Журнал: Analytical Chemistry
- Том: 84
- Номер: 3
- Год издания: 2012
- Издательство: American Chemical Society
- Местоположение издательства: United States
- Первая страница: 1220
- Последняя страница: 1223
- DOI: 10.1021/ac203056m
- Аннотация: Wiring glucose oxidase in the membrane with an immobilized mediator is possible due to the diffusion ability of the latter, if the enzyme containing membrane is formed according to the proposed protocol, including exposing proteins to water organic mixtures with the high content of organic solvent. In the course of the study, the new glucose oxidase mediator, unsubstituted phenothiazine, was discovered. The diffusion coefficient of the mediator in the resulting membrane is independent of the presence of enzyme. The cyclic voltammograms of the enzyme electrode after appearance of the only glucose in solution obtain a well-defined catalytic shape, which is normally observed for both the enzyme and the mediator in solution. Analytical performances of the resulting biosensor are comparable to the advanced second generation ones, which, however, require covalent linking of the mediator either to the membrane forming polymer or to the enzyme. Even without such covalent linking, the reported biosensor is characterized by an appropriate long-term operational stability allowing reagentless sensing.
- Добавил в систему: Карякин Аркадий Аркадьевич
Прикрепленные файлы
| № | Имя | Описание | Имя файла | Размер | Добавлен |
|---|---|---|---|---|---|
| 1. | Полный текст | AC_mediat_membr.pdf | 599,4 КБ | 29 мая 2012 [Karyakin] |