Preparation and determination of immobilized catalase

ABSTRACT

Bovine liver catalase was immobilized on nonporous glass beads by covalent bonding. Higher concentration of catalase in the immobilizing solution resulted in higher activities in the immobilized sample. This was found to be true only up to certain limit. The immobilized enzyme activity was determined using the oxygen evolution from 0.01 M hydrogen peroxide. Linear rates were observed during the first 50 seconds because a negligible proportion of the substrate is used up and because enzyme inactivation is too slow to affect the initial rate