In vivo and in vitro deactivation rates of PTFE-coupled glucose oxidase

Bruce C. Towe, Eric J. Guilbeau, Jeffrey B. Coburn

Research output: Contribution to journalConference article

9 Scopus citations

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 languageEnglish (US)
Pages (from-to)791-798
Number of pages8
JournalBiosensors and Bioelectronics
Volume11
Issue number8
DOIs
StatePublished - Jan 1 1996
EventProceedings of the 1996 4th World Congress on Biosensors - Bangkok, Thailand
Duration: May 29 1996May 31 1996

Keywords

  • Enzyme kinetics
  • Glucose oxidase deactivation
  • In vivo glucose sensors

ASJC Scopus subject areas

  • Biotechnology
  • Biophysics
  • Biomedical Engineering
  • Electrochemistry

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