Immobilization of urease on activated methoxypolyethyleneglycol-5000.
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 epsilon-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 characterization, kinetic constants (Km, Vmax), heat and temperature stabilites were also determined.
Hamarat
S
S
Ege University, Faculty of Science, Biochemistry Department Bornova-Izmir, Turkiye.
Uslan
A H
AH
D004337:Drug Carriers; D004356:Drug Storage; D004795:Enzyme Stability; D004800:Enzymes, Immobilized; D007700:Kinetics; D011092:Polyethylene Glycols; D012044:Regression Analysis; D013696:Temperature; D014510:Urease
D004337:Drug Carriers; D004800:Enzymes, Immobilized; D011092:Polyethylene Glycols; C028210:monomethoxypolyethylene glycol; D014510:Urease