Metallochelate immobilization of urease on to amorphous SiO2
Urease was immobilized onto silica gel and vulcasil activated with Ti4+ and V5+. Higher activity was observed for urease immobilized onto vulcasil compared to that bound to silica gel. The carriers activated with Ti4+ showed activity higher than that of carriers activated with V5+. Activity was affected also by the temperature at which the modified carrier was dried. Lower activities were measured with the carriers heated to 550 °C. The highest activity showed urease metallochelate-bound to vulcasil activated with Ti4+ and dried at 110 °C and the values were close to these of the free enzyme. Thermal stability, pHopt, Topt and kinetic parameters of the immobilized urease were studied. The bound enzyme preserved its activity in wider pH and T intervals and showed higher thermal stability compared to the native one. The highest Vmax of the enzyme reaction was measured for urease metallochelate-bound to vulcasil activated with Ti4+ (dried at 110 °C) and the values were close to these of the free enzyme. The activation energies of the enzymes bound to all types of carriers was ca. 4% smaller than that of the free enzyme.
Journal: Process Biochemistry - Volume 40, Issue 9, September 2005, Pages 3045–3049