Abstract
The deactivation of immobilized enzymes is a major lifetime limiting factor in several types of potentially implantable biosensors. The deactivation rate of covalently immobilized glucose oxidase was examined in vitro in mock physiologic environments and in the peritoneal cavity of mice. A first order deactivation model describes the observed exponential decay of the enzyme. Deactivation rate constants ranging from 0.198 to 1.3 per day were measured depending on experimental conditions. Enzymes immobilized on PTFE (Teflon) substrates in the peritoneal cavity of mice exhibited greater catalytic lifetimes than control samples kept in glucose solution in vitro.
Original language | English (US) |
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Pages (from-to) | 791-798 |
Number of pages | 8 |
Journal | Biosensors and Bioelectronics |
Volume | 11 |
Issue number | 8 |
DOIs | |
State | Published - 1996 |
Event | Proceedings of the 1996 4th World Congress on Biosensors - Bangkok, Thailand Duration: May 29 1996 → May 31 1996 |
Keywords
- Enzyme kinetics
- Glucose oxidase deactivation
- In vivo glucose sensors
ASJC Scopus subject areas
- Biotechnology
- Biophysics
- Biomedical Engineering
- Electrochemistry