Abstract
A gel prepared by heating pepsin-hydrolyzed soy protein isolate (HSPI) had a higher turbidity and viscosity and less solubility than did its starting hydrolyzate. The gelling characteristics of the heated hydrolyzate were possibly due to hydrophobic interactions, as opposed to peptide bond reformation. The presence of pepsin was found to be necessary for gel formation at 37°C but could be successfully replaced by heat. Incubation of the concentrated HSPI at 95°C for 30 min was optimal for heat-induced gel formation. When soy protein isolate (SPI) was hydrolyzed with papain or bacterial protease, little gelation occurred (either by heat or enzyme induced gelation treatments).
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