Effect of pH on the interactions of sodium caseinate with soy phospholipids in relation to the foaming ability of their mixtures

Stabilization of bubbles and foams

“…Semenova et al [51] have pioneered the use of calorimetry and light scattering to determine the nature of the interactions between proteins and a range of commercially important water-soluble low molecular weight surfactants (LMWS) [52] and phospholipids [53] and they have shown that foam stability can be increased or decreased depending on the molecular weight and size of the complexes formed. Sausse et al [54] have found that polyphenols, whilst not very surface active themselves, can reduce the rate of protein adsorption via formation of higher molecular weight protein-polyphenol complexes.…”

Impact of the structure of polyunsaturated soy phospholipids on the structural parameters and functionality of their complexes with covalent conjugates combining sodium caseinate with maltodextrins

“…Relying on both the literature (Antunes, Marques, Miguel, & Lindman, 2009;Bai, Nichifor, & Bastos, 2010;Schulz, Olubummo, & Binder, 2012;Str€ omstedt, Ringstad, Schmidtchen, & Malmsten, 2010) and our experimental data (Istarova et al, 2005;Semenova et al, 2012Semenova et al, , 2014a we can suggest the contribution of the different kinds of the interactions (electrostatic attraction between opposite charges, hydrogen bonding and predominantly hydrophobic attraction) into the complex formation between the phospholipids and the conjugates. It is significant that, as this takes place, the formed complexes show the same high level of the solubility in an aqueous medium that is inherent to the pure covalent conjugates .…”

Functional Food Compositions Based on Whey Protein Isolate, Fish Oil and Soy Phospholipids

“…Such an association of the proteins in the complexes led to a significant increase in their density (k d ) against the background of minor changes in their sizes (k RG ) ( Table 2). The literature and previous experimental data suggest that such changes in the structural parameters of proteins can be associated with the formation of multiple inter-and intramolecular interactions (hydrophobic, hydrogen, electrostatic) involving PC-FO liposomes [14,15,16,17]. Table 2 Coefficients characterizing the degree of change in the structural parameters of the complex particles formed between phosphatidylcholine liposomes enriched with fish oil (PC-FO) and whey protein isolates (original (WPI) or heat-denatured (WPI 70 )) compared with those of the corresponding proteins in an aqueous medium (pH=7.0, I=0.001 M, 25 °C).…”