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| 2. |
- Bernin, Diana, 1979, et al.
(författare)
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Microstructure of polymer hydrogels studied by pulsed field gradient NMR diffusion and TEM methods
- 2011
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Ingår i: Soft Matter. - : Royal Society of Chemistry (RSC). - 1744-683X .- 1744-6848. ; 7:12, s. 5711-5716
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Tidskriftsartikel (refereegranskat)abstract
- The microstructure of various alginate gels have been studied by pulsed field gradient NMR (PFG NMR) and transmission electron microscopy (TEM). The reduced diffusivity of dendrimer diffusion within the gels has been obtained from PFG NMR diffusion experiments. The polymer strand radius, an important microstructural property, has been extracted from various diffusion models. The results agree well with the polymer strand radii obtained from image analysis of the corresponding TEM micrographs.
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| 3. |
- Ohgren, C., et al.
(författare)
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Surface-Directed Structure Formation of beta-Lactoglobulin Inside Droplets
- 2011
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Ingår i: Biomacromolecules. - : American Chemical Society (ACS). - 1525-7797 .- 1526-4602. ; 12:6, s. 2235-2242
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Tidskriftsartikel (refereegranskat)abstract
- 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.
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| 4. |
- Öhgren, Camilla, et al.
(författare)
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Surface-directed structure formation of β-lactoglobulin inside droplets
- 2011
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Ingår i: Biomacromolecules. - : American Chemical Society (ACS). - 1525-7797 .- 1526-4602. ; 12:6, s. 2235-2242
-
Tidskriftsartikel (refereegranskat)abstract
- 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.
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