This work was supported by a grant-in-aid for the “Research for the Future” Program from the Japan Society for the Promotion of Science, and by a grant from the Hitachi Scholars hip Foundation to S.P.
Heating of β-Lactoglobulin A Solution in a Closed System at High Temperatures
Article first published online: 20 JUL 2006
Journal of Food Science
Volume 66, Issue 5, pages 647–652, June 2001
How to Cite
Photchanachai, S. and Kitabatake, N. (2001), Heating of β-Lactoglobulin A Solution in a Closed System at High Temperatures. Journal of Food Science, 66: 647–652. doi: 10.1111/j.1365-2621.2001.tb04615.x
- Issue published online: 20 JUL 2006
- Article first published online: 20 JUL 2006
- β-Lactoglobulin A;
- Heating at high temperature;
- heat denaturation;
- heat aggregation
ABSTRACT β-Lactoglobulin A solution at pH 6.4 was heated to 180 °C at the rate of 6 °C/min. By differential scanning calorimetry two independent endothermic peaks were observed. The first peak appeared below 100 °C is corresponded to the thermal denaturation of protein. This conformational change led to the aggregation and polymerization of molecules through disulfide linkage, particularly observed above 100 °C. The second endothermic peak appeared around 150 °C, which was brought by the decomposition of molecules as judged from electrophoresis. Up to 100 °C the viscosity of β-lactoglobulin A solution increased by heating, while the viscosity was reduced beyond 113 °C, due to change in the size of aggregate and decomposition of β-lactoglobulin A molecules.