Polyphenols, astringency and proline-rich proteins.

G Luck; H Liao; N J Murray; H R Grimmer; E E Warminski; M P Williamson; T H Lilley; E Haslam

doi:10.1016/0031-9422(94)85061-5

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Polyphenols, astringency and proline-rich proteins.

G Luck·H Liao·N J Murray·H R Grimmer·E E Warminski·M P Williamson·T H Lilley·E Haslam

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Abstract

Recent, NMR and precipitation, studies of molecular recognition of proline-rich proteins and peptides by plant polyphenols are described and rationalized. The action of polysaccharides and caseins in the moderation of the astringent response, which is engendered by polyphenols present in foodstuffs and beverages, is described. The possible influence of plant cell wall glycoproteins on the process of lignification is discussed in the light of the observed affinity of phenolic substrates for prolyl residues in protein structures.

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Amino Acid Sequence Astringents Caseins Chemical Precipitation Flavonoids Lignin Magnetic Resonance Spectroscopy Molecular Sequence Data Peptides Phenols Plants Polymers Polyphenols Polysaccharides Proline-Rich Protein Domains Tea Journal Article Research Support, Non-U.S. Gov't

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G Luck, H Liao, N J Murray, H R Grimmer, E E Warminski, M P Williamson, T H Lilley, E Haslam. 1994. Polyphenols, astringency and proline-rich proteins.. https://doi.org/10.1016/0031-9422(94)85061-5

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