Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Bovine β-lactoglobulin/fatty acid complexes: binding, structural, and biological properties

Bovine β-lactoglobulin/fatty acid complexes: binding, structural, and biological properties Ligand-binding properties of β-lactoglobulin (β-lg) are well documented, but the subsequent biological functions are still unclear. Focusing on fatty acids/β-lg complexes, the structure-function relationships are reviewed in the light of the structural state of the protein (native versus non-native aggregated proteins). After a brief description of β-lg native structure, the review takes an interest in the binding properties of native β-lg (localization of binding sites, stoichiometry, and affinity) and the way the interaction affects the biological properties of the protein and the ligand. The binding properties of non-native aggregated forms of β-lg that are classically generated during industrial processing are also related. Structural changes modify the stoichiometry and the affinity of β-lg for fatty acids and consequently the biological functions of the complex. Finally, the fatty acid-binding properties of other whey proteins (α-lactalbumin, bovine serum albumin) and some biological properties of the complexes are also addressed. These proteins affect β-lg/fatty acids complex in whey given their competition with β-lg for fatty acids. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Dairy Science & Technology Springer Journals

Bovine β-lactoglobulin/fatty acid complexes: binding, structural, and biological properties

Loading next page...
 
/lp/springer-journals/bovine-lactoglobulin-fatty-acid-complexes-binding-structural-and-hb01E95ckE

References (126)

Publisher
Springer Journals
Copyright
Copyright © 2014 by INRA and Springer-Verlag France
Subject
Chemistry; Food Science; Agriculture; Microbiology
ISSN
1958-5586
eISSN
1958-5594
DOI
10.1007/s13594-014-0160-y
Publisher site
See Article on Publisher Site

Abstract

Ligand-binding properties of β-lactoglobulin (β-lg) are well documented, but the subsequent biological functions are still unclear. Focusing on fatty acids/β-lg complexes, the structure-function relationships are reviewed in the light of the structural state of the protein (native versus non-native aggregated proteins). After a brief description of β-lg native structure, the review takes an interest in the binding properties of native β-lg (localization of binding sites, stoichiometry, and affinity) and the way the interaction affects the biological properties of the protein and the ligand. The binding properties of non-native aggregated forms of β-lg that are classically generated during industrial processing are also related. Structural changes modify the stoichiometry and the affinity of β-lg for fatty acids and consequently the biological functions of the complex. Finally, the fatty acid-binding properties of other whey proteins (α-lactalbumin, bovine serum albumin) and some biological properties of the complexes are also addressed. These proteins affect β-lg/fatty acids complex in whey given their competition with β-lg for fatty acids.

Journal

Dairy Science & TechnologySpringer Journals

Published: Feb 27, 2014

There are no references for this article.