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Surface-Directed Structure Formation of beta-Lactoglobulin Inside Droplets

C. Ohgren ; Niklas Lorén (Institutionen för kemi- och bioteknik, Teknisk ytkemi ; SuMo Biomaterials) ; A. Altskar ; Anne-Marie Hermansson (Institutionen för kemi- och bioteknik, Teknisk ytkemi ; SuMo Biomaterials)
Biomacromolecules (1525-7797). Vol. 12 (2011), 6, p. 2235-2242.
[Artikel, refereegranskad vetenskaplig]

The morphology of beta-lactoglobulin structures inside droplets was studied during aggregation and gelation using confocal laser scanning microscopy (CISM) 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 beta-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 beta-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 beta-lactoglobulin was situated both inside the droplets and at the interface between the droplets and the oil phase; when 2% PGPR was added, the beta-lactoglobulin structure was concentrated to the inside of the droplets. The possibility to use the different morphological structures of beta-lactoglobulin in droplets to control the diffusion rate through a beta-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 beta-lactoglobulin gel in which the diffusion rate was similar to that in pure water.

Nyckelord: heat-induced aggregation, whey proteins, spinodal decomposition, fluorescence recovery, particulate gels, milk protein, mixed gels, kinetics, gelation, encapsulation

Denna post skapades 2011-07-05. Senast ändrad 2017-01-27.
CPL Pubid: 143106


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Institutioner (Chalmers)

Institutionen för kemi- och bioteknik, Teknisk ytkemi (2005-2014)
SuMo Biomaterials


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Chalmers infrastruktur