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Surface-directed structure formation of β-lactoglobulin inside droplets
RISE, SP – Sveriges Tekniska Forskningsinstitut, SP Sveriges tekniska forskningsinstitut, SIK – Institutet för livsmedel och bioteknik.
RISE, SP – Sveriges Tekniska Forskningsinstitut, SP Sveriges tekniska forskningsinstitut, SIK – Institutet för livsmedel och bioteknik.
RISE, SP – Sveriges Tekniska Forskningsinstitut, SP Sveriges tekniska forskningsinstitut, SIK – Institutet för livsmedel och bioteknik.
RISE, SP – Sveriges Tekniska Forskningsinstitut, SP Sveriges tekniska forskningsinstitut, SIK – Institutet för livsmedel och bioteknik.
2011 (English)In: Biomacromolecules, ISSN 1525-7797, E-ISSN 1526-4602, Vol. 12, no 6, 2235-2242 p.Article in journal (Refereed) Published
Abstract [en]

The morphology of β-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 β-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 β-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 β-lactoglobulin was situated both inside the droplets and at the interface between the droplets and the oil phase; when 2% PGPR was added, the β-lactoglobulin structure was concentrated to the inside of the droplets. The possibility to use the different morphological structures of β-lactoglobulin in droplets to control the diffusion rate through a β-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 β-lactoglobulin gel in which the diffusion rate was similar to that in pure water.

Place, publisher, year, edition, pages
2011. Vol. 12, no 6, 2235-2242 p.
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:ri:diva-29266DOI: 10.1021/bm200320cOAI: oai:DiVA.org:ri-29266DiVA: diva2:1087491
Available from: 2017-04-07 Created: 2017-04-07 Last updated: 2017-04-07Bibliographically approved

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