Czech J. Food Sci., 2009, 27(10):S153-S155 | DOI: 10.17221/962-CJFS

Release of Protein-Bound N-ε -(γ -glutamyl)-Lysine during Simulated Gastrointestinal Digestion

M. Hellwig*, J. Löbner, A. Schneider, U. Schwarzenbolz, T. Henle
Institute of Food Chemistry, Technische Universität Dresden, D-01062 Dresden, Germany *E-mail: michael.hellwig@chemie.tu-dresden.de

N-ε -(γ -glutamyl)-lysine is a crosslinking amino acid formed in food mainly during treatment with microbial transglutaminase (mTG). The purpose of this study was to investigate to which amount isopeptides are detectable in a low-molecular weight peptide fraction after simulated gastrointestinal digestion. Casein, which had been enriched with N-ε -(γ-glutamyl)-lysine by mTG to different extents, was subjected to simulated gastrointestinal digestion and the resulting peptide mixture fractionated into a low- and a high molecular weight fraction (below or above 200-500 Da, respectively) using semipreparative gel permeation chromatography. N-ε -(γ-glutamyl)-lysine was analysed in these fractions by RP-HPLC after enzymatic hydrolysis and derivatisation with phenyl isothiocyanate. N-ε -(γ-glutamyl)-lysine was found nearly exclusively in the high-molecular weight fraction, indicating that dietary N-ε -(γ-glutamyl)-lysine present in mTG-modified food proteins is not available for absorption in the intestine.

Keywords: crosslinking; isopeptide; transglutaminase; simulated gastrointestinal digestion

Published: June 30, 2009  Show citation

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Hellwig M, Löbner J, Schneider A, Schwarzenbolz U, Henle T. Release of Protein-Bound N-ε -(γ -glutamyl)-Lysine during Simulated Gastrointestinal Digestion. Czech J. Food Sci. 2009;27(Special Issue 1):S153-155. doi: 10.17221/962-CJFS.
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