Does flavor impact function? Potential consequences of polyphenol-protein interactions in delivery and bioactivity of flavan-3-ols from foods

Physiol Behav. 2012 Nov 5;107(4):591-7. doi: 10.1016/j.physbeh.2012.02.020. Epub 2012 Feb 23.

Abstract

Astringency is a component of the overall flavor experienced when consuming polyphenol rich foods and beverages such as tea, wine, cocoa and select fruits. Following consumption, the astringent sensation results from the well documented ability of polyphenols to bind to salivary proline rich proteins (PRP) and facilitate their precipitation in the oral cavity. In a similar fashion, polyphenols are also known to non-specifically bind food and other biological proteins. While much is known regarding the polyphenol-protein interactions leading to astringency, significantly less information is available regarding the impact of these polyphenol-protein interactions with food or other biological proteins on relevant physiological outcomes. This paper focuses on the interactions between flavan-3-ols, one of the most abundant dietary polyphenol forms, with proteins in food, salivary PRP and other physiological proteins. The physiological implications of these interactions in food and through the gut will be discussed in relation to manipulation of flavan-3-ol bioavailability, metabolism and biological activities including inhibition of digestive enzymes in the gut.

MeSH terms

  • Astringents / metabolism
  • Biological Availability
  • Digestive System / drug effects
  • Digestive System / enzymology
  • Enzyme Inhibitors / pharmacokinetics
  • Enzyme Inhibitors / pharmacology
  • Flavonoids / chemistry
  • Flavonoids / pharmacokinetics*
  • Flavonoids / pharmacology
  • Humans
  • Molecular Structure
  • Polyphenols / chemistry
  • Polyphenols / pharmacokinetics*
  • Polyphenols / pharmacology
  • Protein Binding
  • Proteins / metabolism*
  • Taste

Substances

  • Astringents
  • Enzyme Inhibitors
  • Flavonoids
  • Polyphenols
  • Proteins
  • flavan-3-ol