ABSTRACT: The gelation of soy peptides produced by the action of papain enzymes on soy glycinin (11S) dispersions (4.7% w/v) was investigated. Cation-exchange chromatography was used to fractionate crude papain. The nonbinding fraction showed no gel-forming activity on the 11S dispersion. Two binding fractions showed gel-forming activity, and the gel strength of both 11S gels was similar. The activity of the crude papain on 11S dispersions produced a slightly stronger gel than one formed with either of the 2 binding fractions. With the crude papain, the rate of gel formation appeared to be strongly influenced by the enzyme concentration, but the maximum gel strength was independent of enzyme concentration. When the temperature was increased, the papain treatment of 11S soy protein produced weaker gels when the measurement was made at the temperature of formation. This dependence of maximum gel strength on temperature was found to be a function of only the measurement temperature and not the gel formation temperature. The degree of protein hydrolysis at maximum gel strength was similar (∼6%) for the gels formed at different temperatures. When the temperature was increased, the elastic modulus G′, the viscous modulus G″, and the degree of viscoelasticity (G″/G′) decreased. This suggested that the gels were formed the by hydrophobic interactions among the peptides. This observation was supported by particle size measurements on samples of gels which were mixed with reagents known for their ability to disrupt hydrophilic/electrostatic, hydrophobic, or disulfide interactions.