Heat Denaturation of Proteins by DSC

Protein function is greatly influenced by many factors, including the surrounding solvent, temperature, pH, etc. Therefore, the evaluation of protein stability in the presence of solvents and with respect to the pH of the environment is very important. One common method for analyzing protein stability is differential scanning calorimetry (DSC). When the higher-order structure of a protein is irreversibly changed, causing activity loss due to degeneration, this is referred to as thermal denaturation. The result is an endothermic peak in DSC analysis. Using the DSC-60 Plus differential scanning calorimeter, we measured the thermal denaturation temperatures of lysozyme and egg-derived protein, and observed the influence of pH on the thermal denaturation temperature of lysozyme.