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New insights about flocculation process in sodium caseinate-stabilized emulsions

Huck-Iriart, Cristián, Montes-de-Oca-Ávalos, Juan, Herrera, María Lidia, Candal, Roberto Jorge, Pinto-de-Oliveira, Cristiano Luis, Linares-Torriani, Iris
Food research international 2016 v.89 pp. 338-346
X-radiation, casein, confocal laser scanning microscopy, droplet size, droplets, emulsions, flocculation, homogenization, hydrophobic bonding, light scattering, micelles, models, protein content, sodium caseinate, sucrose, sunflower oil
Flocculation process was studied in emulsions formulated with 10wt.% sunflower oil, 2, 5 or 7.5wt.% NaCas, and with or without addition of sucrose (0, 5, 10, 15, 20 or 30wt.%). Two different processing conditions were used to prepare emulsions: ultraturrax homogenization or further homogenization by ultrasound. Emulsions with droplets with diameters above (coarse) or below (fine) 1μm were obtained. Emulsions were analyzed for droplet size distribution by static light scattering (SLS), stability by Turbiscan, and structure by confocal laser scanning microscopy (CLSM) and small angle X-ray scattering (SAXS). SAXS data were fitted by a theoretical model that considered a system composed of poly dispersed spheres with repulsive interaction and presence of aggregates. Flocculation behavior was caused by the self-assembly properties of NaCas, but the process was more closely related to interfacial protein content than micelles concentration in the aqueous phase. The results indicated that casein aggregation was strongly affected by disaccharide addition, hydrophobic interaction of the emulsion droplets, and interactions among interfacial protein molecules. The structural changes detected in the protein micelles in different environments allowed understanding the macroscopic physical behavior observed in concentrated NaCas emulsions.