Denaturation of Bovine Serum Albumin (BSA) and Ovalbumin by High Pressure, Heat and Chemicals
Article first published online: 25 AUG 2006
Journal of Food Science
Volume 57, Issue 2, pages 288–292, March 1992
How to Cite
HAYAKAWA, I., KAJIHARA, J., MORIKAWA, K., ODA, M. and FUJIO, Y. (1992), Denaturation of Bovine Serum Albumin (BSA) and Ovalbumin by High Pressure, Heat and Chemicals. Journal of Food Science, 57: 288–292. doi: 10.1111/j.1365-2621.1992.tb05478.x
- Issue published online: 25 AUG 2006
- Article first published online: 25 AUG 2006
- Ms received 5/4/91; revised 9/7/91; accepted 10/2/91.
- bovine serum albumin;
- high pressure
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 a-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.