| Abstract: | ![]()
Heat induced gels can be obtained from partially hydrolyzed soy protein isolate (HSPI). The gel forming ability of each of the HSPI fractions (peptides of varying molecular weight and solubility) were studied, after being separated by preparative Sephadex gel filtration chromatography. The insoluble peptide fraction had no gel forming ability. Peptides larger than 5,000 Daltons, those lower than 5,000 Daltons and a fraction of the very hydrophobic peptides formed weak gels when heated alone. Interactions between several peptide fractions were necessary in order to yield a gel with the strength of the one formed by whole HSPI. A mechanism explaining (1) the action of the proteolytic enzyme in breaking down the protein and (2) the peptide interaction needed for the gel formation, is proposed. |
