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Colloidal properties of sodium caseinate-stabilized nanoemulsions prepared by a combination of a high-energy homogenization and evaporative ripening methods
Nanoemulsions stabilized by sodium caseinate (NaCas) were prepared using a combination of a high-energy homogenization and evaporative ripening methods. The effects of protein concentration and sucrose addition on physical properties were analyzed by dynamic light scattering (DLS), Turbiscan analysi...
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Published in: | Food research international 2017-10, Vol.100 (Pt 1), p.143-150 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Nanoemulsions stabilized by sodium caseinate (NaCas) were prepared using a combination of a high-energy homogenization and evaporative ripening methods. The effects of protein concentration and sucrose addition on physical properties were analyzed by dynamic light scattering (DLS), Turbiscan analysis, confocal laser scanning microscopy (CLSM) and small angle X-ray scattering (SAXS). Droplets sizes were smaller (~100nm in diameter) than the ones obtained by other methods (200 to 2000nm in diameter). The stability behavior was also different. These emulsions were not destabilized by creaming. As droplets were so small, gravitational forces were negligible. On the contrary, when they showed destabilization the main mechanism was flocculation. Stability of nanoemulsions increased with increasing protein concentrations. Nanoemulsions with 3 or 4wt% NaCas were slightly turbid systems that remained stable for at least two months. According to SAXS and Turbiscan results, aggregates remained in the nano range showing small tendency to aggregation. In those systems, interactive forces were weak due to the small diameter of flocs.
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•Sodium caseinate nanoemulsions were prepared by a three-step method.•Stability behavior was different from that of conventional emulsions.•Creaming of individual particles was negligible.•When unstable, the main mechanism of destabilization was flocculation.•Sedimentation of protein flocs occurred in particular conditions. |
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ISSN: | 0963-9969 1873-7145 |
DOI: | 10.1016/j.foodres.2017.06.035 |