Aggregation, gelation and phase separation of heat denatured globular proteins

Dominique Durand, Jean Christophe Gimel and Taco Nicolai

Physica A: Statistical Mechanics and its Applications, 2002, vol. 304, issue 1, 253-265

Abstract: β-lactoglobulin is a globular protein which aggregates after a heat-induced denaturation. It may be considered as a good model system to investigate the processes of aggregation, gelation and phase separation which play a major role in the chemical physics of complex systems. We present here the main results of an extensive study of the denaturation of this protein in various experimental conditions: pH, ionic strength, concentration, temperature, and presence or not of polyoside. The structure and distribution of β-lactoglobulin aggregates were characterized by dynamic and static light scattering, small angle neutron scattering and size exclusion chromatography. Microscopy was used to study the effect of phase separation on the morphology. The competition between phase separation and aggregation/gelation process is discussed.

Keywords: Globular proteins; Aggregates; Gels; Phase separation (search for similar items in EconPapers)
Date: 2002
References: View complete reference list from CitEc
Citations:

Downloads: (external link)
http://www.sciencedirect.com/science/article/pii/S0378437101005143
Full text for ScienceDirect subscribers only. Journal offers the option of making the article available online on Science direct for a fee of $3,000

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:eee:phsmap:v:304:y:2002:i:1:p:253-265

DOI: 10.1016/S0378-4371(01)00514-3

Access Statistics for this article

Physica A: Statistical Mechanics and its Applications is currently edited by K. A. Dawson, J. O. Indekeu, H.E. Stanley and C. Tsallis

More articles in Physica A: Statistical Mechanics and its Applications from Elsevier
Bibliographic data for series maintained by Catherine Liu ().