Relationships of Secondary Structure,Microstructure, and Mechanical Properties of Heat-induced Gel of Soy 11S Golobulin

Secondary structure, microstructure, and mechanical properties of heat induced 11S globulin gel were studied to discover their relationships. Heat-induced 11S globulin gel at 80, 90, and 95°C were comprised of 7.2, 16.6, and 23.8% of α-helix; 19.4, 19.5, and 27.5% of β-sheet, and 73.5, 64.5, and 48.6%, of random coil, respectively. This indicated the gel formed at higher temperatures contained more α-helix and less random coil structures. Micrographs of gels heated at 90 and 95°C had a more extended and integral matrix. Gel strength of heat-induced gels at 90 and 95°C were significantly greater than that of 80°C. These data indicated that the increase in α-helix of heat-induced 11S globulin gel have facilitated the establishment of a good gel matrix.