Release of Protein-Bound N-ε -(γ -glutamyl)-Lysine during Simulated Gastrointestinal Digestion
M. Hellwig,
J. Löbner,
A. Schneider,
U. Schwarzenbolz and
T. Henle
Additional contact information
J. Löbner: Institute of Food Chemistry, Technische Universität Dresden, D-01062 Dresden, Germany *E-mail: michael.hellwig@chemie.tu-dresden.de
A. Schneider: Institute of Food Chemistry, Technische Universität Dresden, D-01062 Dresden, Germany *E-mail: michael.hellwig@chemie.tu-dresden.de
U. Schwarzenbolz: Institute of Food Chemistry, Technische Universität Dresden, D-01062 Dresden, Germany *E-mail: michael.hellwig@chemie.tu-dresden.de
T. Henle: Institute of Food Chemistry, Technische Universität Dresden, D-01062 Dresden, Germany *E-mail: michael.hellwig@chemie.tu-dresden.de
Czech Journal of Food Sciences, 2009, vol. 27, issue SpecialIssue1, S153-S155
Abstract:
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 (search for similar items in EconPapers)
Date: 2009
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Persistent link: https://EconPapers.repec.org/RePEc:caa:jnlcjf:v:27:y:2009:i:specialissue1:id:962-cjfs
DOI: 10.17221/962-CJFS
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