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The Peptide‐catalyzed Maillard Reaction
Author(s) -
Garbe Leif Alexander,
Würtz Alexander,
Piechotta Christian T.,
Tressl Roland
Publication year - 2008
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1433.046
Subject(s) - maillard reaction , chemistry , acetic acid , arabinose , peptide , amino acid , amine gas treating , mass spectrometry , catalysis , casein , biochemistry , organic chemistry , chromatography , fermentation , xylose
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 γ‐aminobutanoic acid, the heptapeptide Nα‐Acetyl‐Lys‐Lys‐β‐Ala‐Lys‐β‐Ala‐Lys‐Gly, and the model protein β‐casein in Maillard reactions with 1‐ 13 C arabinose. Characterization of 13 C‐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.