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

Author

Listed:
  • M. Hellwig
  • 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)

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.

Suggested Citation

  • M. Hellwig & J. Löbner & A. Schneider & U. Schwarzenbolz & T. Henle, 2009. "Release of Protein-Bound N-ε -(γ -glutamyl)-Lysine during Simulated Gastrointestinal Digestion," Czech Journal of Food Sciences, Czech Academy of Agricultural Sciences, vol. 27(SpecialIs), pages 153-155.
    • Handle: RePEc:caa:jnlcjf:v:27:y:2009:i:specialissue1:id:962-cjfs
    DOI: 10.17221/962-CJFS
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