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Abstract
Urease (E.C 3.5.1.5) was covalently immobilized on activated methoxypolyethyleneglycol-5000 which is linear, uncharged, soluble in water and nonimmunogenic. mPEG is bound to the ε-NH2 groups of Lysin in urease. Previously different molar ratios of urease -Lys / activated-mPEG were searched for immobilization. Storage stabilities, molecular weights and the values of blocked amino groups were determined for each immobilized urease and the best conditions was found 1:3 urease-Lys / activated mPEG. Furthermore physical charcterization, kinetic constants (Km, Vmax), heat and temperature stabilites were also determined.