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The peptide-catalyzed Maillard reaction: characterization of 13C reductones.

Authors
  • Garbe, Leif Alexander
  • Würtz, Alexander
  • Piechotta, Christian T
  • Tressl, Roland
Type
Published Article
Journal
Annals of the New York Academy of Sciences
Publication Date
Apr 01, 2008
Volume
1126
Pages
244–247
Identifiers
DOI: 10.1196/annals.1433.046
PMID: 18448823
Source
Medline
License
Unknown

Abstract

The reaction pathways of amino acids and reducing sugars are now fully understood. The focus in the last few years, however, has turned to the reaction of peptides and proteins with reducing sugars. We have investigated the reaction of gamma-aminobutanoic acid, the heptapeptide Nalpha-Acetyl-Lys-Lys-beta-Ala-Lys-beta-Ala-Lys-Gly, and the model protein beta-casein in Maillard reactions with 1-13C arabinose. Characterization of 13C-labeled acetic acid and norfuraneol by gas chromatography-mass spectrometry and nuclear magnetic resonance revealed new formation pathways. The results demonstrate significant differences in the labeling pattern of the products depending on the amine used, indicating different formation pathways of acetic acid and norfuraneol.

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