Nutritional Consequences of the Reactions Between Proteins and Oxidized Polyphenolic Acids

  • Richard F. Hurrell
  • Paul-André Finot
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 177)


The chemical and enzymatic browning reactions of plant polyphenols and their effects on amino acids and proteins are reviewed. A model system of casein and oxidizing caffeic acid has been studied in more detail. The effects of pH, time, caffeic acid level and the presence or not of tyrosinase on the decrease of FDNB-reactive lysine are described. The chemical loss of lysine, methionine and tryptophan and the change in the bioavailability of these amino acids to rats has been evaluated in two systems : pH 7.0 with tyrosinase and pH 10.0 without tyrosinase. At pH 10.0, reactive lysine was more reduced. At pH 7.0 plus tyrosinase methionine was more extensively oxidized to its sulphoxide. Tryptophan was not chemically reduced under either condition. At pH 10.0 there was a decrease in the protein digestibility which was responsible for a corresponding reduction in tryptophan availability and partly responsible for lower methionine availability. Metabolic transit of casein labelled with tritiated lysine treated under the same conditions indicated that the lower lysine availability in rats was due to a lower digestibility of the lysine-caffeoquinone complexes.


Phenolic Acid Caffeic Acid Chlorogenic Acid Protein Digestibility Quinic Acid 
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Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • Richard F. Hurrell
    • 1
  • Paul-André Finot
    • 1
  1. 1.Reseach DepartmentNestlé Products Technical Assistance Co. Ltd.La Tour de PeilzSwitzerland

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