Identification of a peptide in enzymatic hydrolyzate of cheese that inhibits ovalbumin permeation in Caco-2 cells

J Agric Food Chem. 2006 Sep 6;54(18):6904-8. doi: 10.1021/jf061191d.

Abstract

Because the first step in the triggering of food allergy is the permeation of the allergen through the intestine, enhancement of the intestinal barrier function is thought to be effective for preventing food allergy. In this study, a peptide that inhibits ovalbumin (OVA) permeation in an in vitro Caco-2 cell model was isolated from enzymatic hydrolyzate of cheese (EHC). Amino acid sequence analysis identified the active peptide as GPIVLNPWDQ, a sequence identical to amino acids 102-111 of alphas2-casein. The decapeptide significantly inhibited OVA permeation at a concentration of 10(-6) M. In addition, it was found that a pentapeptide half, NPWDQ, is essential for the inhibitory activity because NPWDQ but not GPIVL had nearly the same inhibitory activity as GPIVLNPWDQ. The possibility exists that EHC and/or peptides possessing the NPWDQ sequence can be practically applied to the prevention of food allergy.

MeSH terms

  • Allergens / metabolism*
  • Amino Acid Sequence
  • Caco-2 Cells
  • Caseins / chemistry
  • Caseins / metabolism
  • Cheese / analysis*
  • Humans
  • Hydrolysis
  • Intestinal Absorption / drug effects*
  • Ovalbumin / metabolism*
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Peptide Fragments / pharmacology*
  • Peptide Hydrolases / metabolism

Substances

  • Allergens
  • Caseins
  • Peptide Fragments
  • Ovalbumin
  • Peptide Hydrolases