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Polyphenols, astringency and proline-rich proteins

G Luck1, H Liao, N J Murray

  • 1Department of Chemistry, University of Sheffield, U.K.

Phytochemistry
|September 1, 1994
PubMed
Summary
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Plant polyphenols bind to proline-rich proteins, influencing taste perception and potentially lignification. Polysaccharides and caseins moderate the astringency caused by these polyphenols.

Area of Science:

  • Biochemistry
  • Plant Biology
  • Food Science

Background:

  • Plant polyphenols are widely found in food and beverages.
  • Polyphenols interact with proteins, affecting sensory properties like astringency.
  • Proline-rich proteins are key components in these interactions.

Purpose of the Study:

  • To describe and rationalize molecular recognition between plant polyphenols and proline-rich proteins.
  • To explain the role of polysaccharides and caseins in moderating polyphenol-induced astringency.
  • To discuss the potential influence of plant cell wall glycoproteins on lignification.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy studies.
  • Precipitation assays.
  • Analysis of molecular interactions and affinities.

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Main Results:

  • Demonstrated molecular recognition between plant polyphenols and proline-rich peptides/proteins.
  • Identified the moderating effects of polysaccharides and caseins on astringency.
  • Observed affinity of phenolic substrates for prolyl residues, suggesting a role in lignification.

Conclusions:

  • Plant polyphenols bind to proline-rich proteins, impacting astringency.
  • Polysaccharides and caseins can mitigate the astringent effects of polyphenols.
  • The interaction between phenolics and proline residues may influence plant cell wall processes like lignification.