Electrophoretic profiles, sulfhydryl(SH)/disulfide (SS) groups content, and surface hydrophobicity (H0) values of whey soybean proteins (WSP) and native soy isolates (NSI) were determined. WSP, composed mainly by Kunitz trypsin inhibitor (KTI), and lectin (L), has a H0 value of 24.0 ± 1.0, which is 6.8 times lower than that of NSI ones, and SH/SS groups content in the same range of NSI. The thermal behavior of WSP and NSI was studied by differential scanning calorimetry (DSC). The WSP thermogram in water, similar to NSI, showed two main peaks (Tp values: 74.0 ± 0.5 C and 90.4 ± 0.8C) attributed to thermal denaturation of KTI and L, respectively. These endotherms are slightly affected by μ, whereas those of NSI are strongly affected (Tp of 7S and 11S peaks increase 17C and 20C respectively, by increasing NaCl concentration from 0 to 1M). WSP has low Ho values not noticeably affected by ionic strength changes, whereas NSI has higher Ho, that increase in saline media and favor intermolecular hydrophobic interactions. The consequent low tendency to protein aggregation by hydrophobic interactions in WSP would explain their lower thermal stability at high μ. Control proteins of both preparations (7S and 11S enriched fractions for NSI, and purified trypsin inhibitors, urease and lectin for WSP) were use to confirm these results.
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Sorgentini et al. (1999) studied this question.
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