Phase Separation and Association of Globular Protein Aggregates in the Presence of Polysaccharides: 1. Mixtures of Preheated β-Lactoglobulin and κ-Carrageenan at Room Temperature
Autor: | Philippe Croguennoc, Allan H. Clark, and Dominique Durand, Taco Nicolai |
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Rok vydání: | 2001 |
Předmět: |
chemistry.chemical_classification
Globular protein Size-exclusion chromatography Analytical chemistry Surfaces and Interfaces Protein aggregation Condensed Matter Physics Polysaccharide law.invention Dilution chemistry Optical microscope law Phase (matter) Electrochemistry General Materials Science Static light scattering Spectroscopy |
Zdroj: | Langmuir. 17:4372-4379 |
ISSN: | 1520-5827 0743-7463 |
DOI: | 10.1021/la001674q |
Popis: | Mixtures of globular protein (β-lactoglobulin) aggregates and polysaccharides (κ-carrageenan) were studied using dynamic and static light scattering, size exclusion chromatography, and optical microscopy. Above a critical κ-carrageenan concentration the protein aggregates phase separate and form spherical microdomains, which slowly sediment. The effect of concentration and size of the protein aggregates was investigated. The phase separation is initially reversible upon dilution, but the microdomains become progressively more stable until after several days they can no longer be redissolved. |
Databáze: | OpenAIRE |
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