Effect of alpha-lactalbumin on the phase behavior of AOT-brine-isooctane mixtures : role of charge interactions
We have found that both electrostatic and hydrophobic interactions are involved in the ability of the protein alpha-lactalbumin (alpha-LA) to affect the self-assembly of the anionic surfactant sodium bis(ethylhexyl) sulfosuccinate (AOT, 3.5 wt %) in equivolume mixtures of organic and aqueous solutio...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 21(2005), 13 vom: 21. Juni, Seite 5931-9 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , |
| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2005
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Salts Surface-Active Agents brine Dioctyl Sulfosuccinic Acid 10041-19-7 Lactalbumin 9013-90-5 |
| Zusammenfassung: | We have found that both electrostatic and hydrophobic interactions are involved in the ability of the protein alpha-lactalbumin (alpha-LA) to affect the self-assembly of the anionic surfactant sodium bis(ethylhexyl) sulfosuccinate (AOT, 3.5 wt %) in equivolume mixtures of organic and aqueous solutions. The composition and size of AOT phase structures that form in the presence of 0.35 wt % protein were evaluated as a function of pH and ionic strength. In the absence of protein, AOT forms water-in-oil microemulsion droplets for all pH and salt concentrations studied here. The presence of the protein in the water-in-oil microemulsion phase boosts water solubilization and droplet size, as the spontaneous curvature of the surfactant interface becomes less negative. Aggregates of protein, surfactant, and oil also form in the water-continuous phase. The size and composition of structures in both phases can be tuned in the presence of protein by varying the pH and ionic strength. alpha-LA induces the appearance of an anisotropic surfactant phase at pH <5.8. At intermediate salt concentrations, a third isotropic, viscous aqueous phase appears that contains 55-60% of the protein, 10-14% of the surfactant, and significant amounts of oil. Circular dichroism and fluorescence spectroscopy indicate that the protein contains enhanced alpha-helical secondary structure when self-assembling with surfactant, and has a loosened tertiary structure. The protein does not interact with the surfactant as an unfolded random coil. Although the conformation of alpha-LA in aqueous salt solutions is known to depend on pH, when self-assembling with AOT the protein adopts a structure whose features are quite pH insensitive, and likely reflect an intrinsic interaction with the interface |
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| Beschreibung: | Date Completed 23.06.2006 Date Revised 21.11.2008 published: Print Citation Status MEDLINE |
| ISSN: | 1520-5827 |