We report on the effect of potato maltodextrins with variable dextrose equivalent (Paselli SA-2, SA-6 and SA-10) on the surface behavior at the air-water interface of the mixture: legumin+small-molecule surfactant. Distinct in nature small-molecule surfactants (model: sodium salt of capric acid, Na-caprate; and commercially important: a citric acid ester of monoglyceride, CITREM) have been under our consideration. The role of the structure of both of the maltodextrins and the small-molecule surfactants in the effect studied has been elucidated by measurements in a bulk aqueous medium of the enthalpy of their interaction from mixing calorimetry, value of weight average molecular weight of the maltodextrins and the thermodynamics of the pair maltodextrin-solvent and maltodextrin-protein interactions from laser static light scattering. The combined data of mixing calorimetry and light scattering suggest some complex formation between the small-molecule surfactants and the maltodextrins. Predominantly hydrophobic interactions along with hydrogen bonding form the basis of the complexes. The effect of the maltodextrins on the thermodynamics of the protein heat denaturation and thereby on the protein conformational stability in the presence of the small-molecule surfactants has been studied by differential scanning calorimetry. The interrelation between the thermodynamics of intermolecular interactions in a bulk and the surface behavior at the planar air-water interface of the ternary systems (maltodextrin+legumin+small-molecule surfactant) has been elucidated by tensiometry. The effect of the maltodextrins on the surface activity of mixtures of legumin with the small-molecule surfactants is governed by the competitive in relation to the protein interactions with the small-molecule surfactants and a subsequent change in the thermodynamic properties of the both biopolymers, which are favorable to the ternary complex formation.
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