Structures and stability of lipid emulsions formulated with sodium caseinate
The physicochemical properties of emulsions play an important role in food systems as they directly contribute to texture, sensory and nutritional properties of foods. Sodium caseinate (NaCas) is a well-used ingredient because of its good solubility and emulsifying properties and its stability durin...
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Elsevier Ltd
2011
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| LEADER | 16547caa a22015737a 4500 | ||
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| 005 | 20230607131856.0 | ||
| 008 | 190411s2011 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-80052864435 | |
| 024 | 7 | |2 cas |a alcohol, 64-17-5; calcium ion, 14127-61-8; casein, 9000-71-9 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a COCSF | ||
| 100 | 1 | |a Huck-Iriart, C. | |
| 245 | 1 | 0 | |a Structures and stability of lipid emulsions formulated with sodium caseinate |
| 260 | |b Elsevier Ltd |c 2011 | ||
| 270 | 1 | 0 | |m Herrera, M.L.; Pabellón de Industrias, Ciudad Universitaria, 1428 Buenos Aires, Argentina; email: lidia@di.fcen.uba.ar |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a The physicochemical properties of emulsions play an important role in food systems as they directly contribute to texture, sensory and nutritional properties of foods. Sodium caseinate (NaCas) is a well-used ingredient because of its good solubility and emulsifying properties and its stability during heating. One of most significant aspects of any food emulsion is its stability. Among the methods used to study emulsion stability it may be mentioned visual observation, ultrasound profiling, microscopy, droplet size distribution, small deformation rheometry, measurement of surface concentration to characterize adsorbed protein at the interface, nuclear magnetic resonance, confocal microscopy, diffusing wave spectroscopy, and turbiscan. They have advantages and disadvantages and provide different insights into the destabilization mechanisms. Related to stability, the aspects more deeply investigated were the amount of NaCas used to prepare the emulsion, and specially the oil-to-protein ratio, the mobility of oil droplets and the interactions among emulsion components at the interface. It is known that the amount of protein required to stabilize oil-in-water emulsions depends, not only on the structure of protein at the interface, and the average diameters of the emulsion droplets, but also on the type of oils and the composition of the aqueous phase. Several authors have investigated the effect of a thickening agent or of a surface active molecule. Factors such as pH, temperature, and processing conditions during emulsion preparation are also very relevant to stability. There is a general agreement among authors that the most stable systems are obtained for conditions that produce size reduction of the droplets, an increase in viscosity of the continuous phase and structural changes in emulsions such as gelation. All these conditions decrease the molecular mobility and slow down phase separation. © 2011 Elsevier B.V. |l eng | |
| 536 | |a Detalles de la financiación: Universidad de Buenos Aires, UBA, X 451 | ||
| 536 | |a Detalles de la financiación: National Science and Technology Development Agency, NSTDA | ||
| 536 | |a Detalles de la financiación: Agencia Nacional de Promoción Científica y Tecnológica, ANPCyT, PICT 0060 | ||
| 536 | |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas, CONICET, PIP 11220080101504 | ||
| 536 | |a Detalles de la financiación: María L. Herrera and Roberto J. Candal are researchers of the National Research Council of Argentina (CONICET). This work was supported by CONICET through Project PIP 11220080101504, by the National Agency for the Promotion of Science and Technology (ANPCyT) through Project PICT 0060, and by the University of Buenos Aires through Project X 451. The authors wish to thank to the Synchrotron Light National Laboratory (LNLS, Campinas, Brazil) for the use of X-ray facilities and the SPES company for providing the concentrated from fish oils. | ||
| 593 | |a Inst. de Quimica Inorgánica, Medio Ambiente y Energía (INQUIMAE), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Ciudad Universitaria, Pabellón 2 Piso 3, C1428EHA Buenos Aires, Argentina | ||
| 593 | |a Facultad de Ciencias Exactas y Naturales (FCEN), Universidad de Buenos Aires (UBA), Ciudad Universitaria, Avda. Intendente Güiraldes, 1428 Buenos Aires, Argentina | ||
| 593 | |a Escuela de Ciencia y Tecnología, Universidad Nacional de San Martín (UNSAM), Campus Miguelete, 25 de Mayo y Francia, CP 1650, San Martín, Provincia de Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a EMULSION |
| 690 | 1 | 0 | |a SODIUM CASEINATE |
| 690 | 1 | 0 | |a STABILITY |
| 690 | 1 | 0 | |a STRUCTURE |
| 690 | 1 | 0 | |a CONVERGENCE OF NUMERICAL METHODS |
| 690 | 1 | 0 | |a DROP BREAKUP |
| 690 | 1 | 0 | |a EMULSIONS |
| 690 | 1 | 0 | |a GELATION |
| 690 | 1 | 0 | |a NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY |
| 690 | 1 | 0 | |a OILS AND FATS |
| 690 | 1 | 0 | |a PHASE INTERFACES |
| 690 | 1 | 0 | |a PHASE SEPARATION |
| 690 | 1 | 0 | |a PROTEINS |
| 690 | 1 | 0 | |a SODIUM |
| 690 | 1 | 0 | |a STABILITY |
| 690 | 1 | 0 | |a STRUCTURE (COMPOSITION) |
| 690 | 1 | 0 | |a DESTABILIZATION MECHANISMS |
| 690 | 1 | 0 | |a DIFFUSING-WAVE SPECTROSCOPY |
| 690 | 1 | 0 | |a DROPLET SIZE DISTRIBUTIONS |
| 690 | 1 | 0 | |a NUTRITIONAL PROPERTIES |
| 690 | 1 | 0 | |a OIL-IN-WATER EMULSIONS |
| 690 | 1 | 0 | |a PHYSICOCHEMICAL PROPERTY |
| 690 | 1 | 0 | |a SODIUM CASEINATE |
| 690 | 1 | 0 | |a SURFACE-ACTIVE MOLECULES |
| 690 | 1 | 0 | |a EMULSIFICATION |
| 690 | 1 | 0 | |a ALCOHOL |
| 690 | 1 | 0 | |a CALCIUM ION |
| 690 | 1 | 0 | |a CASEIN |
| 690 | 1 | 0 | |a CASEINATE |
| 690 | 1 | 0 | |a FAT DROPLET |
| 690 | 1 | 0 | |a LIPID EMULSION |
| 690 | 1 | 0 | |a UNCLASSIFIED DRUG |
| 690 | 1 | 0 | |a WATER OIL CREAM |
| 690 | 1 | 0 | |a CONFOCAL LASER MICROSCOPY |
| 690 | 1 | 0 | |a FLOCCULATION |
| 690 | 1 | 0 | |a FLOW KINETICS |
| 690 | 1 | 0 | |a IONIC STRENGTH |
| 690 | 1 | 0 | |a MOLECULAR STABILITY |
| 690 | 1 | 0 | |a NUCLEAR MAGNETIC RESONANCE |
| 690 | 1 | 0 | |a PARTICLE SIZE |
| 690 | 1 | 0 | |a PHASE SEPARATION |
| 690 | 1 | 0 | |a PHYSICAL PHASE |
| 690 | 1 | 0 | |a PROTEIN CONTENT |
| 690 | 1 | 0 | |a PROTEIN STRUCTURE |
| 690 | 1 | 0 | |a REVIEW |
| 690 | 1 | 0 | |a SPECTROSCOPY |
| 690 | 1 | 0 | |a TEMPERATURE SENSITIVITY |
| 690 | 1 | 0 | |a VISCOELASTICITY |
| 690 | 1 | 0 | |a X RAY CRYSTALLOGRAPHY |
| 650 | 1 | 7 | |2 spines |a PH |
| 700 | 1 | |a Álvarez-Cerimedo, M.S. | |
| 700 | 1 | |a Candal, R.J. | |
| 700 | 1 | |a Herrera, M.L. | |
| 773 | 0 | |d Elsevier Ltd, 2011 |g v. 16 |h pp. 412-420 |k n. 5 |p Curr. Opin. Colloid Interface Sci. |x 13590294 |w (AR-BaUEN)CENRE-4369 |t Current Opinion in Colloid and Interface Science | |
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