Phase diagrams relative to the systems water-lysozime-lithium perfluorononanoate (H2O-LYS-LiPFN), water-bovine serum albumin-sodium taurodeoxycholate (H2O-BSA-NaTDC), and water-gelatin-Quiilaja bark Saponin (H2O-GEL-QBS) have been drawn, at 25 degreesC. Solutions, gels, multiphase systems and solid particles dispersed in gel have been observed. In all cases the presence of protein-surfactant based gels has been observed. Ionic strength and, to a less extent, pH of the solvent medium reduce the width of the gel phase and are responsible for modifications in the equilibrium solution-disperse solid. Optical microscopy, surface tension, optical turbidity, ionic conductivity, emf, NMR, volumetric and viscosity data have been used to characterise the solution and the multiphase regions occurring in the aforementioned systems. Proper combination of the above findings allows drawing some preliminary hypotheses on the mechanisms responsible for the stability of protein-surfactant based gels.
Equilibrium Between Phases in Water - Protein - Surfactant Systems / Palacios, A. C.; SARNTHEIN GRAF, C.; LA MESA, Camillo. - In: COLLOIDS AND SURFACES. A, PHYSICOCHEMICAL AND ENGINEERING ASPECTS. - ISSN 0927-7757. - STAMPA. - 228:(2003), pp. 25-35.
Equilibrium Between Phases in Water - Protein - Surfactant Systems
LA MESA, Camillo
2003
Abstract
Phase diagrams relative to the systems water-lysozime-lithium perfluorononanoate (H2O-LYS-LiPFN), water-bovine serum albumin-sodium taurodeoxycholate (H2O-BSA-NaTDC), and water-gelatin-Quiilaja bark Saponin (H2O-GEL-QBS) have been drawn, at 25 degreesC. Solutions, gels, multiphase systems and solid particles dispersed in gel have been observed. In all cases the presence of protein-surfactant based gels has been observed. Ionic strength and, to a less extent, pH of the solvent medium reduce the width of the gel phase and are responsible for modifications in the equilibrium solution-disperse solid. Optical microscopy, surface tension, optical turbidity, ionic conductivity, emf, NMR, volumetric and viscosity data have been used to characterise the solution and the multiphase regions occurring in the aforementioned systems. Proper combination of the above findings allows drawing some preliminary hypotheses on the mechanisms responsible for the stability of protein-surfactant based gels.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.