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Polyphenol-beta-casein complexes at the air/water interface and in solution: effects of polyphenol structure.
J Agric Food Chem. 2008 Oct 22; 56(20):9600-11.JA

Abstract

The interactions between proteins and plant polyphenols are responsible for astringency and haze formation in beverages and may participate in foam stabilization. The effect of phenolic compounds with different structures, namely, catechin (C), epicatechin (Ec), epigallocatechin (Egc), epicatechin gallate (EcG), and epigallocatechin gallate (EgcG), on the surface properties at the air/liquid interface of beta-casein, chosen as model protein, were monitored by tensiometry and ellipsometry. The formation of complexes in the bulk phase was measured by electrospray ionization mass spectrometry (ESI-MS). Adsorption of polyphenols from pure solution was not observed. Surface pressure, surface concentration, and dilational modulus of the protein adsorption layer were greatly modified in the presence of galloylated flavanol monomers (EcG and EgcG) but not of lower molecular weight polyphenols (<306 g/mol). The formation of polyphenol-protein aggregates in the bulk, as evidenced by ESI-MS and light scattering experiments, was related to the slowdown of protein adsorption.

Authors+Show Affiliations

INRA UMR 614 Fractionnement des Agro-Ressources et Environnement (FARE) INRA/Universite de Reims Champagne Ardennes, Centre de Recherche en Environnement et Agronomie, 2 Esplanade R. Garros, BP 224, F-51686 Reims, France. Veronique.Aguie@reims.inra.frNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18826319

Citation

Aguié-Béghin, V, et al. "Polyphenol-beta-casein Complexes at the Air/water Interface and in Solution: Effects of Polyphenol Structure." Journal of Agricultural and Food Chemistry, vol. 56, no. 20, 2008, pp. 9600-11.
Aguié-Béghin V, Sausse P, Meudec E, et al. Polyphenol-beta-casein complexes at the air/water interface and in solution: effects of polyphenol structure. J Agric Food Chem. 2008;56(20):9600-11.
Aguié-Béghin, V., Sausse, P., Meudec, E., Cheynier, V., & Douillard, R. (2008). Polyphenol-beta-casein complexes at the air/water interface and in solution: effects of polyphenol structure. Journal of Agricultural and Food Chemistry, 56(20), 9600-11. https://doi.org/10.1021/jf801672x
Aguié-Béghin V, et al. Polyphenol-beta-casein Complexes at the Air/water Interface and in Solution: Effects of Polyphenol Structure. J Agric Food Chem. 2008 Oct 22;56(20):9600-11. PubMed PMID: 18826319.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Polyphenol-beta-casein complexes at the air/water interface and in solution: effects of polyphenol structure. AU - Aguié-Béghin,V, AU - Sausse,P, AU - Meudec,E, AU - Cheynier,V, AU - Douillard,R, Y1 - 2008/10/01/ PY - 2008/10/2/pubmed PY - 2008/12/25/medline PY - 2008/10/2/entrez SP - 9600 EP - 11 JF - Journal of agricultural and food chemistry JO - J Agric Food Chem VL - 56 IS - 20 N2 - The interactions between proteins and plant polyphenols are responsible for astringency and haze formation in beverages and may participate in foam stabilization. The effect of phenolic compounds with different structures, namely, catechin (C), epicatechin (Ec), epigallocatechin (Egc), epicatechin gallate (EcG), and epigallocatechin gallate (EgcG), on the surface properties at the air/liquid interface of beta-casein, chosen as model protein, were monitored by tensiometry and ellipsometry. The formation of complexes in the bulk phase was measured by electrospray ionization mass spectrometry (ESI-MS). Adsorption of polyphenols from pure solution was not observed. Surface pressure, surface concentration, and dilational modulus of the protein adsorption layer were greatly modified in the presence of galloylated flavanol monomers (EcG and EgcG) but not of lower molecular weight polyphenols (<306 g/mol). The formation of polyphenol-protein aggregates in the bulk, as evidenced by ESI-MS and light scattering experiments, was related to the slowdown of protein adsorption. SN - 1520-5118 UR - https://www.unboundmedicine.com/medline/citation/18826319/Polyphenol_beta_casein_complexes_at_the_air/water_interface_and_in_solution:_effects_of_polyphenol_structure_ L2 - https://doi.org/10.1021/jf801672x DB - PRIME DP - Unbound Medicine ER -