1. How the presence of a small molecule affects the complex coacervation between lactoferrin and -lactoglobulin
- Author
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Pascaline Hamon, Guilherme M. Tavares, Antônio Fernandes de Carvalho, Thomas Croguennec, Saïd Bouhallab, UMR 1253 Science et Technologie du lait et l'oeuf, Institut National de la Recherche Agronomique (INRA), Laboratory of Research in Milk Products, Universidade Federal de Vicosa (UFV), Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, INRA, Université Européenne deBretagne (Collège Doctoral International), Conseil Régional deBretagne and the federal Brazilian funding agency CNPq, and Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)
- Subjects
comportement d'agrégation ,Static Electricity ,industrie agro-alimentaire ,02 engineering and technology ,Lactoglobulins ,010402 general chemistry ,β-Lactoglobulin ,01 natural sciences ,Biochemistry ,Anilino Naphthalenesulfonates ,²-lactoglobulin ,produit laitier ,hétéroprotéine ,Structural Biology ,Molar ratio ,[SDV.IDA]Life Sciences [q-bio]/Food engineering ,Animals ,Binding site ,Molecular Biology ,lactotransferrin ,beta lactoglobuline ,Coacervate ,biology ,Ligand ,Chemistry ,Lactoferrin ,assemblage de protéine ,lactoferrine ,General Medicine ,Binding ,ITC ,021001 nanoscience & nanotechnology ,Fluorescence ,Small molecule ,agrégation ,0104 chemical sciences ,Macromolecular assembly ,Crystallography ,dairy product ,Complex coacervation ,biology.protein ,encapsulation ,Cattle ,ANS ,0210 nano-technology ,coacervation ,[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition - Abstract
Heteroprotein complex coacervation corresponds to the formation of two liquid phases in equilibrium induced by the interaction of two oppositely charged proteins. The more concentrated phase known as coacervate phase, has attracted interest from several fields of science due to its potential applications for example for encapsulation and delivery of bioactives. Prior such application, it is necessary to understand how the presence of small ligands affects the complex coacervation. In this work, we report on the interaction of small ligand with individual proteins β-lactoglobulin (β-LG) and lactoferrin (LF) and consequences on their complex coacervation. ANS (8-Anilinonaphthalene-1-sulfonic acid), a fluorescent probe, was used as model ligand. While ANS did not interact with β-LG, it presented two sets of binding sites with LF inducing its self-aggregation. Depending on its concentration, ANS modulated the shape of β-LG-LF macromolecular assembly. Coacervates were observed for ANS/LF molar ratio
- Published
- 2017