Isolation and structural elucidation of a peptide derived from Edam cheese that inhibits beta-lactoglobulin transport.
A peptide that inhibits beta-lactoglobulin absorption in an in vitro Caco-2 cell model was isolated from Edam cheese. By 1H-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 beta-casein. The hexapeptide shows remarkable inhibition of beta-lactoglobulin transport at a concentration of 10(-7)M. The possibility exists that this peptide can be applied practically to the prevention of milk-sensitive allergy.
Tanabe
S
S
Graduate School of Biosphere Science, Hiroshima University, Hiroshima 739-8528, Japan. stanabe@hiroshima-u.ac.jp
Tesaki
S
S
Watanabe
J
J
Fukushi
E
E
Sonoyama
K
K
Kawabata
J
J
D000485:Allergens / Q000378:metabolism; D000595:Amino Acid Sequence; D018938:Caco-2 Cells; D002611:Cheese / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007408:Intestinal Absorption / Q000187:drug effects*; D007782:Lactoglobulins / Q000276:immunology / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D016269:Milk Hypersensitivity / Q000517:prevention & control; D010455:Peptides / Q000737:chemistry* / Q000302:isolation & purification* / Q000494:pharmacology
D000485:Allergens; D007782:Lactoglobulins; D010455:Peptides