Abstract
The thermal stability of pepsin in a strong acid medium as a function of pH has been investigated using differential scanning calorimetry (DSC), UV absorbance, polyacrylamide gel electrophoresis (PAGE) and MALDI-TOF MS methods. The “two independent two-state transitions model” with view of physiological function of pepsin was used for analyzing thermal denaturation curves. The transition temperature (Tm) values ranging from 305.15 to 319.15K for the first transition and from 322.15 to 349.15K for the second transition in the examined pH range implicating the higher stability at pH 4 are in good agreement with MALDI-TOF MS results. The corresponding maximum, ΔG°(25), was stability obtained at pH 4 with values of 65.3kJmol−1.
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