DENATURATION OF BOVINE SERUM-ALBUMIN (BSA) AND OVALBUMIN BY HIGH-PRESSURE, HEAT AND CHEMICALS

Both native and denatured protein samples were examined by determining fluorescence and specific rotation, and by polyacrylamide gel electrophoresis (PAGE) and differential scanning calorimetry (DSC). Denaturation of ovalbumin by pressure was much less than by heat or by the chemical denaturants. Ovalbumin was denatured under high pressure, as confirmed by the decrease in its alpha-helical content to 72% and DSC endothermic enthalpy to 61%, but it showed no change in the PAGE pattern. With bovine serum albumin decrease in fluorescence was observed after denaturation by chemicals, but it did not change under high pressure.