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Light Scattering Study of Turbid Heat-Set Globular Protein Gels Using Cross-Correlation Dynamic Light Scattering

✍ Scribed by Taco Nicolai; Claus Urban; Peter Schurtenberger

Publisher: Elsevier Science
Year: 2001
Tongue: English
Weight: 92 KB
Volume: 240
Category: Article
ISSN: 0021-9797
DOI: 10.1006/jcis.2001.7672

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✦ Synopsis

The structure factor of aqueous solutions of the globular protein β-lactoglobulin was determined as a function of heating time at 76 • C. We show how the effect of multiple scattering on the scattered light intensity can be effectively corrected using cross-correlation dynamic light scattering even if the transmission is only 1%. The structure factor of aggregated and gelled proteins can be described by the Ornstein-Zernike equation. The system is characterized by a correlation length that increases with heating time and stabilizes some time after the gel is formed. The correlation length of the protein gels decreases with decreasing concentration. Measurements after progressive dilution of a sample close to the gel point showed that the protein aggregates are initially interpenetrated and disinterpenetrate upon dilution.

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