Functional ended of poly ( glycidyl methacrylate ) spheres immobilization of glucose oxidase microspheres

In this study, glucose oxidase (E.C.1.1.3.4) (GOD) enzyme was covalently immobilized onto poly(glycıdyl methacrylate) (PGMA) and carboxylic acid ended poly(glycıdyl methacrylate) (PGMA-COOH) mıcrospheres. The effect of pH, temperature, storage stability on the immobilized enzyme was investigated. Optimum pHs for immobilized enzymes were determined as 7.0. Optimum temperatures for PGMA and PGMA-COOH spheres immobilized enzymes were found to be 60.0 and 50.0 oC, respectively. The maximum reaction rate (Vmax) and the Michaelis-Menten constant (Km) was calculated for the immobilized enzymes. Michaelis-Menten constant (Km) for immobilized onto PGMA and immobilized onto PGMA-COOH enzymes were found to be 2.44x10-2 mM, and 3.22x10-2 mM, respectively. In the same way, the maximum reaction rate (Vmax) for immobilized enzymes were found to be 4,44x10-2 mM x min-1, and 4,59x10-2 mM x min-1, respectively. Reuse number and storage stability of glucose oxidase were increased with immobilization.Key Words : Glucose oxidase, enzyme immobilization, covalent binding