title: Bioreactor applications of glucose oxidase covalently bonded on pHEMA membranes.
abstract: Glucose oxidase was immobilized onto poly(2-hydroxyethyl methacrylate) membranes by covalent bonding through epichlorohydrin. The highest immobilization efficiency was found to be 17.4%. The Km values were 5.9 and 8.8 mM for free and bound enzymes, respectively, and the Vmax values were 0.071 and 0.067 mM/min for free and bound enzymes. When the medium was saturated with oxygen Km was not altered significantly but Vmax was. The optimum pHs for the free and bound enzyme were determined to be 5 and 6, respectively, and the optimum temperature was 30 degrees C for both forms. The inactivation constant for the bound enzyme was found to be 1.7 x 10(-4) min-1.
authors.affiliation: Middle East Technical University, Department of Biological Sciences, Ankara, Turkey.
authors.forename: M Y
authors.initials: MY
authors.lastname: Arica
authors.forename: V
authors.initials: V
authors.lastname: Hasirci
mesh_terms: D004800:Enzymes, Immobilized; D004811:Epichlorohydrin / Q000737:chemistry; D005949:Glucose Oxidase / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008567:Membranes, Artificial; D011102:Polyhydroxyethyl Methacrylate; D013696:Temperature
chemical_list: D004800:Enzymes, Immobilized; D008567:Membranes, Artificial; D004811:Epichlorohydrin; D011102:Polyhydroxyethyl Methacrylate; D005949:Glucose Oxidase