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The sodium caseinate (SCN)-maltodextrin (MD) covalent conjugates were prepared by a food-grade process involving the first step of the Maillard reaction. The covalent conjugates were prepared with different weight ratios of biopolymers (R(MD : SCN) = 0.4; 1; 2; 5) in the system using maltodextrins of strongly different dextrose equivalents (DE), i.e., DE = 2 and 10. We have observed that the covalent conjugation of SCN with MD, in contrast to their simple mixing, improved the protein solubility in an aqueous medium in a wide pH range that was more pronounced in the vicinity of the SCN isoelectric point (pH 3.8-4.4). The extent of SCN solubility was mainly governed by the weight/molar ratio of the biopolymers in the covalent conjugates, R(MD : SCN). Data of static multiangle laser light scattering showed that the revealed increase in the solubility of the conjugates could be predominantly attributable to the dramatic increase in their thermodynamic affinity for an aqueous medium. Which was most pronounced for the maltodextrin with the higher DE (DE = 10). The direct relationship between the increase in the solubility of the conjugates and the increase in their foaming ability, as compared against SCN, has been revealed as a rule both at neutral pH and at the pI. In addition, the found improvement in the protein foaming ability was also defined by both the weight/molar ratio (R(MD : SCN)) and the dextrose equivalent of the maltodextrins attached to the protein.

The combination of data obtained from isothermal mixing calorimetry and light scattering allowed us to reveal the relationships between the character of the interactions of casein (β-casein and sodium caseinate (SCN) particles) with phosphatidylcholine (PC) liposomes and their specific properties, such as, the hydrophilic-lipophilic balance of the surface properties, the size, and the architecture. The size distribution diagrams, obtained by dynamic light scattering for the particles of pure PC, β-casein and their complexes, indicated the involvement of both the protein and liposome particles in the complex formation at pH 5.5 and low ionic strength (0.001 M). As this took place, the data of the extraction of the free PC from the aqueous solutions of the complex particles by diethyl ether showed about 90% of the binding of the PC liposomes by the β-casein particles. As a result of the interactions, the complex particles showed markedly higher values of their density, calculated on the basis of the light scattering data, as compared to the ones, which were inherent to the pure protein particles. The generality of the importance of such a structural parameter as the density of the complex (protein + PC) particles for their function as protectors against oxidation for the unsaturated PC was supported by the data obtained for the complex particles formed between SCN and PC liposomes at pH 5.5, 40 °C and the low ionic strength (0.001 M). In addition, the importance of both the density and the architecture of the complex (protein + PC) particles for their susceptibility to the proteolysis in the gastrointestinal tract was illustrated by the example of the proteolysis of the complex (β-casein + PC) particles in the simulated gastrointestinal conditions in vitro.