Effect of different salts on the foaming properties of model protein systems for infant formula.

This multiscale study aimed to evaluate the effects of different salts (NaCl, KCl, MgCl, and CaCl) on the foaming capacity (FC) and foam stability (FS) of model protein systems (MPS) for infant formula via changes in surface and structural properties. Our results showed that the FC and FS of MPS were increased with the addition of NaCl, KCl, and MgCl, whereas CaCl significantly decreased FC (79.5 ± 10.6%) and increased FS (93.2 ± 2.2%). The surface hydrophobicity was increased and the net charge and surface tension were reduced after the addition of salts. Structural analysis revealed the reduction of intensity of intrinsic fluorescence spectroscopy and UV absorption, and the conversion of α-helix into β-strand, which was attributed to protein agglomeration. Additionally, MgCl and CaCl exhibited larger size and lower net charge compared with NaCl and KCl, indicating a greater ability to bind to charged amino acids and form larger aggregates. Correlation analysis indicated that FC was positively related to adsorbed protein and β-turn and negatively correlated with particle size. In addition, FS showed a positive correlation with β-strand, apparent viscosity, and zeta potential. However, it exhibited a negative correlation with β-turn, α-helix, and sulfhydryl content. These results provide a theoretical reference for further understanding of the effect of salts on the foaming properties of MPS.