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Immunological behavior of in vitro digested egg-white lysozyme.

Rodrigo Jiménez-Saiz1, Sara Benedé, Beatriz Miralles

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Hen egg lysozyme (LYS) remains allergenic after simulated digestion. Specific peptide fragments and intact LYS retain IgE-binding and immune-stimulating properties, contributing to its allergenicity.

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Area of Science:

  • Food Allergy Research
  • Protein Biochemistry
  • Immunology

Background:

  • Lysozyme (LYS) from hen egg possesses antimicrobial properties.
  • LYS is recognized as a significant food allergen, particularly in egg allergies.
  • Understanding LYS allergenicity requires investigating its behavior during digestion.

Purpose of the Study:

  • To identify peptides generated from in vitro gastrointestinal digestion of LYS.
  • To assess the IgE-binding capacity and biological activity of these peptides.
  • To elucidate the mechanisms underlying LYS allergenicity.

Main Methods:

  • Simulated in vitro gastrointestinal digestion of LYS.
  • IgE-binding assays, basophil degranulation tests, and peripheral blood mononuclear cell stimulation.
  • High-Performance Liquid Chromatography-Mass Spectrometry/Mass Spectrometry (HPLC-MS/MS) for fragment identification.
  • Matrix-Assisted Laser Desorption/Ionization-Time of Flight/Time of Flight (MALDI-TOF/TOF) for immunoreactive product analysis.

Main Results:

  • In vitro gastric and gastroduodenal digests of LYS retained IgE-binding ability.
  • Basophil activation capacity and T-cell immunogenicity were preserved in digested LYS.
  • Allergenic activity was linked to persistent intact LYS, specific fragments like f(24-129), and disulfide-linked peptides containing epitopes f(57-83) and f(108-122).

Conclusions:

  • The pH during gastric digestion significantly influences subsequent duodenal digestion of LYS.
  • Gastric hydrolysis conditions affect the exposure of key allergenic epitopes.
  • These findings contribute to understanding the factors enhancing LYS's allergenic potential.