The nature of intermolecular forces responsible for thermal gelation of the 12S canola globulin was determined by preparing gels under a variety of environmental influences. The effects of pH, sodium salts and denaturing agents were evaluated by differential scanning calorimetry, small amplitude oscillatory theology and transmission light microscopy. Gels prepared with 6% protein at alkaline pH values were superior to 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 prior to heating produced inferior gels. Hydrophobic forces and electrostatic interactions were responsible for the establishment of canola gel networks. Gel stabilization and strengthening were attributed to disulfide bonding, electrostatic interactions and hydrogen bonding.

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