THERMAL GELATION OF THE 12S CANOLA GLOBULIN

The nature of intermolecular forces responsible for thermal gelation o f the 12S canola globulin was determined by preparing gels under a var iety of environmental influences. The effects of pH, sodium salts and denaturing agents were evaluated by differential scanning calorimetry, small amplitude oscillatory rheology and transmission light microscop y. Gels prepared with 6% protein at alkaline pH values were superior t o gels prepared under acidic conditions. Sodium salts, which promoted protein stability, had an adverse effect on gelation. The addition of guanidine hydrochloride and dithiothreitol to protein dispersions prio r to heating produced inferior gels. Hydrophobic forces and electrosta tic interactions were responsible for the establishment of canola gel networks. Gel stabilization and strengthening were attributed to disul fide bonding, electrostatic interactions and hydrogen bonding.