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* Graduate School of Biosphere Science, Hiroshima University, Hiroshima 739-8528, Japan
Department of Food and Life-Science, Takasaki University of Health and Welfare, Takasaki 370-0033, Japan
Graduate School of Agriculture, Hokkaido University, Sapporo 060-8589, Japan
Corresponding author:
S. Tanabe; e-mail:
stanabe{at}hiroshima-u.ac.jp.
A peptide that inhibits ß-lactoglobulin absorption in an in vitro Caco-2 cell model was isolated from Edam cheese. By 1 H-NMR and N-terminal amino acid analyses, the active compound was identified as Asp-Lys-Ile-His-Pro-Phe. The sequence of the hexapeptide is the same as the amino acid sequence of residues 47-52 of ß-casein. The hexapeptide shows remarkable inhibition of ß-lactoglobulin transport at a concentration of 10-7M. The possibility exists that this peptide can be applied practically to the prevention of milk-sensitive allergy.
Key Words: allergen absorption ß-lactoglobulin Edam cheese cows milk allergy
Abbreviation key: ß-Lg = ß-lactoglobulin, DMEM = Dulbeccos modified Eagles medium, FCS = fetal calf serum, FITC = fluorescein isothiocyanate, HBSS = Hanks balanced salt solution, ODS = octadecylsilyl, OVA = ovalbumin, PBS = 10 mM phosphate buffered saline, TEER = transepithelial electrical resistance, TFA = trifluoroacetic acid
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