In vivo and in vitro deactivation rates of PTFE-coupled glucose oxidase.
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.
Towe
B C
BC
Chemical, Bio, and Materials Engineering Department, Arizona State University, Tempe 85287-6006, USA.
Guilbeau
E J
EJ
Coburn
J B
JB
D000818:Animals; D004800:Enzymes, Immobilized / Q000378:metabolism*; D005260:Female; D005949:Glucose Oxidase / Q000378:metabolism*; D051379:Mice; D010537:Peritoneum / Q000378:metabolism; D011138:Polytetrafluoroethylene
D004800:Enzymes, Immobilized; D011138:Polytetrafluoroethylene; D005949:Glucose Oxidase