Interaction of flavan-3-ol derivatives and different caseins is determined by more than proline content and number of proline repeats

M.C. Bohin, J.P. Vincken, A.H. Westphal, A.M. Tripp, Peter Dekker, H.T.W.M. Hijden, H. Gruppen

Research output: Contribution to journalArticleAcademicpeer-review

14 Citations (Scopus)

Abstract

Interactions of Type A and B flavan-3-ol dimers (procyanidins) and several monomeric flavan-3-ols, with a-casein and ß-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 a-casein than the supposedly more flexible B-type dimers investigated. Despite its higher content of proline, compared to a-casein, ß-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.
Original languageEnglish
Pages (from-to)408-416
JournalFood Chemistry
Volume158
DOIs
Publication statusPublished - 2014

Keywords

  • food proteins
  • binding
  • astringency
  • polymerization
  • precipitation
  • complexation
  • fluorescence
  • procyanidins
  • polyphenols
  • gallate

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