The hardness and water‐holding ability of rice globulin gels were intermediate between those of gels of soybean and sesame globulins. Scanning electron micrographs showed that rice globulin gel had a rough network structure composed of small globular particles of protein aggregates. Effects of various reagents on solubilization of proteins from the three gel types were compared. Disulfide bonds and hydrophobic interactions contributed mainly to the stability of rice globulin gels. The contributions of disulfide bonds to both the formation and stability of rice globulin gels were greater than for sesame globulin gels.
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Yuno‐Ohta et al. (1994) studied this question.
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