Experimental modelling of thermal inactivation of urease.

摘要: Thermal inactivation of jack bean urease (EC 3.5.1.5) was investigated in a 0.1 M phosphate buffer with pH 7. An injection flow calorimetry method adapted for the measurement enzyme activity. The curves were measured temperature range 55 to 87.5 degrees C. exhibited biphasic pattern whole and they well fitted biexponential model. A simultaneous fit all data based on kinetic models that derived from different mechanisms comprised material balances several forms enthalpy balance characterizing initial heating period solution. multitemperature evaluation revealed an adequate model had incorporate at least three reaction steps. It concluded key steps thermal reversible dissociation/denaturation native form into inactive denatured form, irreversible association reactions both forms.