1981 Volume 7 Issue 3 Pages 320-323
A glucose sensor was constructed by covering dissolved oxygen sensor with an immobilized glucose oxidase membrane, and its response characteristics were studied. The basic matrix of the membrane was reconstituted collagen fibrils prepared from hide powder.
As the amount of glucose oxidase used for immobilization varied from 2 mg to 10 mg per 100 mg of hide powder, profiles of the calibration curve at 25°C changed remarkably to become favorable to the lower glucose concentrations : with a membrane of 10 mg enzyme per 100 mg hide powder the profile of the calibration curve seemed to be usable for glucose analysis even at 5°C.
The inactivation of enzyme was observed to affect sensor responses seriously at temperatures of 45°C or higher.
The half-life of the apparent activity of the immobilized enzyme increased with increasing amount of enzyme used and with decreasing temperature.
The relative value of apparent enzyme activity at time t was found to be formulated by (Et/E0) app=1/ (1 +Ktn). The value of n ranged from 1.7 to 2.7.