title: Immobilization of urease onto chemically modified acrylonitrile copolymer membranes.
abstract: Poly (acrylonitrile-methylmethacrylate-sodium vinylsulfonate) membranes were subjected to seven different chemical modifications. The amounts of new groups incorporated in the membranes with the modifications were determined. Urease was covalently immobilized on the modified membranes. Both the amount of bound protein and relative activity of immobilized urease were measured. The highest activity was found for urease bound to membranes modified with hydroxylammonium sulfate (68%) and hydrazinium sulfate (67%). Optimum pH of free urease was determined to be 5.8. For positively charged membranes, pH optimum was shifted to higher values, while for negatively charged membranes-to lower pH. The charge of the matrix affected also the rate of the enzyme reaction. The highest rate was measured with urease immobilized on membranes modified with hydroxylammonium sulfate and hydrazinium sulfate. The major part of the immobilized enzyme on different modified membranes remained stable-only ca. 20% of enzyme activity was lost for 4 h at 70 degrees C while the free enzyme was totally inactivated.
authors.affiliation: Department of Biotechnology, University Professor Dr A. Zlatarov, Professor Y. Yakimov Str. 1, 8010 Bourgas, Bulgaria. godjevargova@yahoo.com
authors.forename: T
authors.initials: T
authors.lastname: Godjevargova
authors.forename: K
authors.initials: K
authors.lastname: Gabrovska
mesh_terms: D000181:Acrylonitrile; D001709:Biotechnology / Q000379:methods*; D004789:Enzyme Activation; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008567:Membranes, Artificial; D011108:Polymers; D014510:Urease / Q000737:chemistry* / Q000378:metabolism
chemical_list: D004800:Enzymes, Immobilized; D008567:Membranes, Artificial; D011108:Polymers; D014510:Urease; D000181:Acrylonitrile