title: Structural and functional determinants of Mucor miehei protease. V. Enthalpy changes upon thermal denaturation in solution of varying pH.
abstract: The thermal denaturation of Mucor meihei protease was studied as a function of pH by differential scanning calorimetry. In both citric acid-Na2HPO4 and in acetic acid-sodium acetate buffers, maximum thermal stability was at pH 4.0-4.2. However, the maximum enthalpy changes associated with the denaturation process were buffer-dependent and occurred between pH values of 4.7 and 5.7.
mesh_terms: D002151:Calorimetry; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009089:Mucor / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000378:metabolism; D011487:Protein Conformation; D011489:Protein Denaturation; D013816:Thermodynamics
chemical_list: D010447:Peptide Hydrolases