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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Detalles Bibliográficos
Autores: Huck Iriart, Cristián, Álvarez Cerimedo, María Soledad, Candal, Roberto Jorge, Herrera, Maria Lidia
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2011
País:Argentina
Institución:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/71564
Acceso en línea:http://hdl.handle.net/11336/71564
Access Level:acceso abierto
Palabra clave:Emulsion
Sodium Caseinate
Stability
Structure
https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
Descripción
Sumario: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.