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.