Effect of water content on thermal behavior of freeze-dried soy whey and their isolated proteins.

Thermal behavior of lyophilized soy whey (LSW) and whey soy proteins (WSP) at different water contents (WC) was studied by DSC. In anhydrous condition, Kunitz trypsin inhibitor (KTI) and lectin (L) were more heat stable for WSP with respect to LSW sample. The increase of WC destabilized both proteins but differently depending on the sample analyzed. Thermal stability inversion of KTI and L was observed for WSP and LSW at 50.0% and 17.0% WC, respectively, which correspond to the same water-protein content mass ratio (W/P ≈ 1.9). At W/P < 1.9, KTI was more heat stable than L. Before the inversion point, WC strongly modified the peak temperatures (T(p)) of KTI and L for WSP, whereas this behavior was not observed for LSW. The high sugar content was responsible for the thermal behavior of KTI and L in LSW under anhydrous condition and low WC. These results have important implications for the soy whey processing and inactivation of antinutritional factors.

Thermal behavior of soy protein fractions depending on their preparation methods, individual interactions, and storage conditions.

Different soy protein isolates (SPI) and whey soy protein (WSP) samples were obtained from fresh and stored soybean flour. Some samples were subjected to a long, cold storage. DSC thermograms of SPI showed the two characteristic endotherms, corresponding to denaturation of ß-conglycinin and glycinin. Low value of denaturation enthalpy and high glycinin denaturation temperature were related to a reduction of protein solubility of SPI. DSC thermograms of WSP also showed two characteristic endotherms, corresponding to Kunitz trypsin inhibitor and lectin. The methods and conditions of preparation and storage of WSP samples were factors that modified their thermal behavior. Some SPI-WSP mixtures (1:1) exhibited more complex thermograms and higher denaturation temperatures. Thermograms of SPI-denatured WSP mixtures showed that the thermal stabilization of soybean storage proteins was attributed to protein-protein interactions. The differences in the thermal behavior of single or mixed SPI and WSP could not be explained on the basis of mineral content.