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

被引:15
|
作者
Tanabe, Soichi [1 ]
Isobe, Nana
Miyauchi, Eiji
Kobayashi, Shoko
Suzuki, Masayuki
Oda, Munehiro
机构
[1] Hiroshima Univ, Grad Sch Biosphere Sci, Higashihiroshima 7398528, Japan
[2] Takasaki Univ Hlth & Welfare, Dept Food & Life Sci, Takasaki, Gumma 3700033, Japan
[3] Meiji Dairies Corp, Div Res & Dev, Food Sci Inst, Kanagawa 2500862, Japan
关键词
enzymatic hydrolyzate of cheese; allergen; permeation; Caco-2; alpha s(2)-casein; ovalbumin;
D O I
10.1021/jf061191d
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
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 alpha s(2)-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.
引用
收藏
页码:6904 / 6908
页数:5
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