Mj. Danilich et al., ACTIVITY OF FREE AND IMMOBILIZED GLUCOSE-OXIDASE - AN ELECTROCHEMICALSTUDY, Annals of biomedical engineering, 21(6), 1993, pp. 655-668
The activity of free and immobilized glucose oxidase was determined us
ing a sandwich type thin-layer electrochemical cell. The thin-layer ce
ll consisted of a gold electrode deposited on a glass microscope slide
, 165 mum thick Teflon TFE spacers, and a glass cover. Enzyme activity
was determined by using cyclic voltammetry to measure the amount of h
ydrogen peroxide produced in the glucose oxidase catalyzed redox react
ion between glucose and oxygen in the thin-layer cell. The specific ac
tivity of 13.4 nM glucose oxidase in 0.2 M aqueous sodium phosphate, p
H 5.2 at room temperature, was calculated to be 4.34 U/mg GOx. Under t
he same experimental conditions, qualitative detection of the activity
of glucose oxidase covalently immobilized to a thin radiofrequency pl
asma modified poly(etherurethaneurea) film was demonstrated.