Stabilization of oil-water emulsions with protein concentrates from the microalga Tetradesmus obliquus.

The present work used water-soluble protein concentrates from the microalga Tetradesmus obliquus to stabilize sunflower oil emulsions. Microalgal cells were disrupted by sonication, and proteins were separated from the biomass using two methods, isoelectric and solvent precipitations. The protein extracts were concentrated by lyophilization, and the concentrates were used to produce emulsions with three amounts of Tetradesmus obliquus protein concentrate (TobPC) (0.1, 0.5, and 1.0% w/v). Emulsions were homogenized through sonication and characterized for creaming index, optical microscopy, size distribution, ζ-potential, and rheology. Isoelectric precipitation resulted in TobPC with a high protein content (51.46 ± 2.37%) and a better dispersibility profile. Emulsion stability was higher for both the isoelectric TobPC and control systems than for the TobPC solvent. Solvent TobPC does not efficiently stabilize emulsions at low protein concentrations that showed microscopically larger oil droplets and flocculation spots. A high phase separation velocity was observed for solvent TobPC, probably due to the higher hydrodynamic droplet diameters. The increase in TobPC content in the emulsions resulted in more stable emulsions for all samples. Therefore, Tetradesmus obliquus protein concentrates are a potential emulsifying agent.

Heteroaggregation of lipid droplets coated with sodium caseinate and lactoferrin.

Formation and characterization of droplet heteroaggregates were investigated by mixing two emulsions previously stabilized by proteins oppositely charged. Emulsions were composed of 5vol.% of sunflower oil and 95vol.% of sodium caseinate or lactoferrin aqueous dispersions. They were produced using ultrasound with fixed power (300W) and sonication time (6min). Different volume ratios (0-100%) of sodium caseinate-stabilized emulsion (droplet diameter around 1.75µm) to lactoferrin-stabilized emulsion (droplet diameter around 1.55µm) were mixed under conditions that both proteins showed opposite charges (pH7). Influence of ionic strength (0-400mM NaCl) on the heteroaggregates stability was also evaluated. Creaming stability, zeta potential, microstructure, mean particle diameter and rheological properties of the heteroaggregates were measured. These properties depended on the volume ratio (0-100%) of sodium caseinate to lactoferrin-stabilized emulsion (C:L) and the ionic strength. In the absence of salt, different zeta potential values were obtained, rheological properties (viscosity and elastic moduli) were improved and the largest heteroaggregates were formed at higher content of lactoferrin-stabilized emulsion (60-80%). The system containing 40 and 60vol.% of sodium caseinate and lactoferrin stabilized emulsion, respectively, presented good stability against phase separation besides showing enhanced rheological and size properties due to extensive droplets aggregation. Phase separation was observed only in the absence of sodium caseinate, demonstrating the higher susceptibility of lactoferrin to NaCl. The heteroaggregates produced may be useful functional agents for texture modification and controlled release since different rheological properties and sizes can be achieved depending on protein concentrations.