Design of microcapsules with bilberry seed oil, cold-set whey protein hydrogels and anthocyanins: Effect of pH and formulation on structure formation kinetics and resulting microstructure during purification processing and storage.

Encapsulation of polar and non-polar bioactive compounds from bilberries was achieved by designing microcapsules with bilberry seed oil (BSO) distributed in an aqueous phase of anthocyanins (AC) stabilized by whey protein isolate (WPI). Non-thermal emulsification method (o/w/o) was developed and the effect of pH (3 or 4.5), concentration of WPI (8.4-10.8% w/w), addition of AC (72-216 ppm) and emulsifier on the structure-forming kinetics, resulting microstructure during storage and after centrifugation and washing was investigated. Agglomeration of BSO was observed in all microcapsules at pH 4.5 due to slow gelling process and in samples at pH 3 at low concentrations of WPI (≤8.4%). Capsules with pH 3 (9.6-10.8% WPI) had weak structures but as the gelling process was faster, it generated an even distribution of BSO droplets. All samples at pH 4.5 and samples with WPI concentration ≥10.8% at pH 3 exhibited intact structures after centrifugation and washing.

Effect of anthocyanins on lipid oxidation and microbial spoilage in value-added emulsions with bilberry seed oil, anthocyanins and cold set whey protein hydrogels.

The objective of this work was to explore the storage properties of a structured oil-in-water emulsion containing both water- and fat-soluble bioactive compounds from bilberries (Vaccinium myrtillus L.). Bilberry seed oil (BSO) was dispersed in a continuous aqueous phase of anthocyanins (AC) and whey protein isolate. The microstructure was evaluated using light microscopy and the effect of anthocyanins on lipid oxidation and microbial growth was investigated. The results showed that it was possible to generate a stable emulsion structure that resisted phase separation during 25 weeks of storage. Gas chromatography-mass spectrometry measurements of the fatty acids in the BSO during storage showed that AC had a protective effect against lipid oxidation. The AC did not have an antimicrobial effect against the investigated strains Zygosaccharomyces bailii (ATCC 42476) and Aspergillus niger (ATCC 6275 (M68)).

Surface-directed structure formation of ß-lactoglobulin inside droplets.

The morphology of ß-lactoglobulin structures inside droplets was studied during aggregation and gelation using confocal laser scanning microscopy (CLSM) equipped with a temperature stage and transmission electron microscopy (TEM). The results showed that there is a strong driving force for the protein to move to the interface between oil and water in the droplet, and the ß-lactoglobulin formed a dense shell around the droplet built up from the inside of the droplets. Less protein was found inside the droplets. The longer the ß-lactoglobulin was allowed to aggregate prior to gel formation, the larger the part of the protein went to the interface, resulting in a thicker shell and very little material being left inside the droplets. The droplets were easily deformed because no network stabilizes them. When 0.5% emulsifier, polyglycerol polyresinoleat (PGPR), was added to the oil phase, the ß-lactoglobulin was situated both inside the droplets and at the interface between the droplets and the oil phase; when 2% PGPR was added, the ß-lactoglobulin structure was concentrated to the inside of the droplets. The possibility to use the different morphological structures of ß-lactoglobulin in droplets to control the diffusion rate through a ß-lactoglobulin network was evaluated by fluorescence recovery after photobleaching (FRAP). The results show differences in the diffusion rate due to heterogeneities in the structure: the diffusion of a large water-soluble molecule, FITC-dextran, in a dense particulate gel was 1/4 of the diffusion rate in a more open particulate ß-lactoglobulin gel in which the diffusion rate was similar to that in pure water.