Interaction of flavan-3-ol derivatives and different caseins is determined by more than proline content and number of proline repeats
| Autor: | Adrie H. Westphal, Jean-Paul Vincken, Harry Gruppen, Peter J. T. Dekker, Maxime C. Bohin, Annelise M. Tripp, Harry T. W. M. van der Hijden |
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| Rok vydání: | 2014 |
| Předmět: |
binding
Proline Stereochemistry complexation Biochemie Flavan-3-ol astringency precipitation Biochemistry food proteins Analytical Chemistry gallate chemistry.chemical_compound Phenols Levensmiddelenchemie Organic chemistry Gallic acid polyphenols VLAG Flavonoids chemistry.chemical_classification Food Chemistry Plant Extracts Caseins General Medicine procyanidins Monomer chemistry Polymerization Polyphenol polymerization Composition (visual arts) fluorescence Procyanidin A1 Food Science |
| Zdroj: | Food Chemistry 158 (2014) Food Chemistry, 158, 408-416 |
| ISSN: | 0308-8146 |
| DOI: | 10.1016/j.foodchem.2014.02.145 |
| Popis: | Interactions of Type A and B flavan-3-ol dimers (procyanidins) and several monomeric flavan-3-ols, with α-casein and β-casein, were investigated. Binding affinities measured were related to the ligands structure, including several properties (e.g. intrinsic flexibility (number of rotatable bonds) and hydrophobicity), and to the amino-acid composition of the caseins. A monomeric flavan-3-ol esterified with gallic acid (EGCG) had a five to ten times higher affinity to caseins compared to the non-galloylated dimeric flavan-3-ols. In this case, the larger number of rotatable bonds in EGCG might be accountable for this difference. Comparing flavan-3-ol dimers, intrinsic flexibility did not consistently promote interactions, as procyanidin A1 displayed a higher affinity to α-casein than the supposedly more flexible B-type dimers investigated. Despite its higher content of proline, compared to α-casein, β-casein did not always have a higher affinity for the ligands investigated (e.g. no interaction with procyanidin A1 detected). These results suggest that more factors than proline content and the number of proline repeats govern phenolic-casein interactions. |
| Databáze: | OpenAIRE |
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