Study on the Activity and Stability of Urease Immobilized via a Saccharide-Concanavalin a Binding

Abstract

In this study, urease was immobilized on chitosan beads via a saccharide-concanavalin A binding. Similarly, the covalent immobilization of urease using glutaraldehyde was also studied for comparison. The aim of the study was to compare the two immobilization method in terms of their optimum temperature, thermal stability, optimum pH and pH stability and also, Michaelis constant(Km) of two immobilized enzyme was compared with each other. The Michaelis constant(Km) for the immobilized urease via affinity bonds was disclosed to be 11.76 mM by Lineweaver-Burk plot, and the highest activity was allowed at 77degC and pH 5-6. Besides, this immobilized enzyme exhibits good thermal and pH stability. The obtained results are much better compared to the free enzyme and the covalent immobilization of urease using glutaraldehyde. Hence, immobilization of urease via affinity bonds could therefore be a versatile tool for immobilization of proteins and would have great promise in clinical as well as industrial use.