ABSTRACT
In this work, the partition effects due to the changes in the microenvironment of catalase by immobilization was studied in the absence of any diffusional resistance. The pH activity profiles were done for both soluble and immobilized catalase. Catalase was immobilized on nonporous glass beads, so the internal diffusional resistance is not considered. The external diffusion effect is also minimized by the continuous stirring through the enzyme assay. The Km value for the immobilized enzyme was also determined at different ionic strengths. The results showed a constant Km and suggested that the microenvironmental changes due to immobilization of catalase by the applied method are negligible and that any kinetic parameter determined is the true intrinsic parameter and not an apparent one