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 journalArticle

9 Citations (Scopus)

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 - 1996

Fingerprint

Immobilized Enzymes
Glucose Oxidase
Glucose oxidase
Peritoneal Cavity
Polytetrafluoroethylene
Polytetrafluoroethylenes
Enzymes
Biosensing Techniques
Biosensors
Rate constants
Glucose
Substrates
In Vitro Techniques

Keywords

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

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Electrochemistry

Cite this

In vivo and in vitro deactivation rates of PTFE-coupled glucose oxidase. / Towe, Bruce C.; Guilbeau, Eric J.; Coburn, Jeffrey B.

In: Biosensors and Bioelectronics, Vol. 11, No. 8, 1996, p. 791-798.

Research output: Contribution to journalArticle

Towe, Bruce C. ; Guilbeau, Eric J. ; Coburn, Jeffrey B. / In vivo and in vitro deactivation rates of PTFE-coupled glucose oxidase. In: Biosensors and Bioelectronics. 1996 ; Vol. 11, No. 8. pp. 791-798.
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