α-Lactalbumin−AOT Charge Interactions Tune Phase Structures in Isooctane/Brine Mixtures

Abstract

Self-assembly of the anionic surfactant AOT with the protein alpha-lactalbumin in isooctane/brine mixtures results in phase structures whose type, size, and shape differ considerably from those formed by the surfactant alone. Small-angle X-ray scattering was used to determine the size and shape of these structures for 5.4 < pH < 11.2 and 0.25, 0.33, and 0.4 wt % NaCl. All pH values were above the reported isoelectric point for the protein. The composition of the system (except for salt) was fixed, with 2.5 wt % surfactant in equivolume mixtures of oil and water and either 0 or 0.4 wt % protein. Under these conditions, AOT in the absence of protein always formed spherical, water-in-oil (w/o) microemulsion droplets in the organic phase with no self-assembly in the aqueous phase. In the presence of alpha-lactalbumin, self-assembled structures were formed in both aqueous and organic phases, and the size and shape of these was tuned by both pH and [NaCl]. Protein-surfactant interaction was weakest at the most alkaline pH, with protein-free, spherical droplets forming in the organic phase and surfactant-decorated soluble protein clusters forming in the aqueous phase. As pH was decreased, protein increasingly partitioned to the organic phase and droplets became ellipsoidal and much larger in volume, with these effects enhanced at lower salt concentration. Aqueous structures were also strongly affected by pH, shifting from prolate protein/surfactant aggregates at alkaline pH to oil-in-water, oblate microemulsion droplets at neutral pH. At acidic pH and higher salt concentration, self-assembly shifted toward a third, anisotropic aqueous phase, which contained discoid bilayer structures. It is proposed that hydrophobic attraction causes association of the protein with the surfactant monolayer, and pH and [salt] tune the system via the protein by modifying electrostatic repulsion and monolayer curvature.

The viscosity stability of O/W emulsion containing ^|^alpha;-gel through an ionic-complex system

“…A diffraction pattern derived from a lamellar structure was observed for all samples. Generally, the addition of electrolytes, such as NaCl, to this sort of emulsion system reportedly allows the hydrophilic groups of surfactants to dehydrate, resulting in the shrinkage of the interlamellar distance of the lamellar structures 1,16,17 . Although DSAC is not a salt, shrinkage of the interlamellar distance was observed in a dose-dependent manner.…”

Interaction of α-lactalbumin with lipids and possible implications for its emulsifying properties – A review

“…However, as pH was decreased, protein increasingly partitioned to the organic phase and droplets became ellipsoidal and much larger in volume, with these effects enhanced at lower salt concentration. Therefore, it was proposed that hydrophobic attraction causes association of the protein with the surfactant monolayer, and pH and salt tune the system via the protein by modifying electrostatic repulsion and monolayer curvature (Kim & Dungan, 2009). …”