On relationships between molecular structure, interaction and surface behavior in mixture: small-molecule surfactant+protein.
We report on the effect of distinct in nature small-molecule surfactants (model, a sodium salt of capric acid, Na-caprate; and commercially important, a citric acid ester of monoglyceride, CITREM; a sodium salt of stearol-lactoyl lactic acid, SSL (Na(+)); polyglycerol ester, PGE (080)) on molecular properties in a bulk and at the air-water interface of globular legumin and random-coiled micellar sodium caseinate. The role of the structure of both proteins and 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, the change in value of weight average molecular weight of the proteins and the thermodynamics of the pair protein-protein interactions from laser static light scattering as well as, in addition, by measurements of the change in hydrodynamic radius for micellar sodium caseinate from laser dynamic light scattering. The effect of the small-molecule surfactants on the thermodynamics of the protein heat denaturation and thereby on the protein conformational stability has been studied by differential scanning calorimetry in the case of globular legumin. The interrelation between the effects of the small-molecule surfactants on the properties of the proteins in a bulk and at the planar air-water interface has been elucidated by tensiometry. The combined data of mixing calorimetry, differential scanning calorimetry and laser light scattering suggest some complex formation between the small-molecule surfactants and the proteins in a bulk aqueous medium. Predominantly hydrophobic interaction along with electrostatic and hydrogen bonding form the basis of the complex formation. The found effect of the small-molecule surfactants on the surface activity of their mixtures with proteins is governed primarily by both the extent of the protein association, resulting in specific hydrophobicity/hydrophilicity of the surface of the protein associates, and the specific protein conformational stability, for the globular protein, produced by the interaction between the proteins and the small-molecule surfactants.
Antipova
A S.
AS
Institute of Biochemical Physics of Russian Academy of Sciences, Vavilov str. 28, 117813, Moscow, Russia
Semenova
M G.
MG
Belyakova
L E.
LE
Il'in
M M.
MM