In vitro digestion of major allergen in salmon roe and its peptide portion with proteolytic resistance

被引:10
作者
Fujita, Shingo [1 ]
Shimizu, Yutaka [1 ]
Kishimura, Hideki [1 ]
Watanabe, Kazuhiko [2 ]
Hara, Akihiko [1 ]
Saeki, Hiroki [1 ]
机构
[1] Hokkaido Univ, Fac Fisheries Sci, Hakodate, Hokkaido 0418611, Japan
[2] Watanabe Kazuhiko Pediat Clin, Sapporo, Hokkaido 0030026, Japan
关键词
Food allergen; Salmon roe; Allergenicity; Digestibility; beta '-component; Yolk protein; Proteolytic tolerance; IgE-binding ability; YOLK PROTEINS; OOCYTE MATURATION; FOOD ALLERGENS; DIGESTIBILITY; VITELLOGENIN; STABILITY; PURIFICATION; PEANUT;
D O I
10.1016/j.foodchem.2011.07.099
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
A fish yolk protein, beta'-component (beta'-c), is the major allergen in chum salmon roe. The effect of proteolysis on the allergenicity of beta'-c was estimated. Changes in the IgE-binding ability of beta'-c upon pepsin and trypsin digestion were investigated by monitoring the proteolytic cleavage. In the pepsin-trypsin digestion of chum salmon yolk protein, the beta'-c contained therein was degraded in a manner similar to that of other yolk proteins, but digestion fragments with a molecular mass of >10 kDa remained throughout the digestion process. Specifically, the peptide sequence between 31-Y and 119-Q (10 kDa) was stable to pepsin-trypsin digestion and the portion showed high IgE-binding ability. As a result, pepsin-trypsin digestion had little effect on the IgE-binding ability of beta'-c. These results suggest that beta'-c reaches the small intestine in the form of high-molecular-mass components with IgE-binding ability in vivo. (C) 2011 Elsevier Ltd. All rights reserved.
引用
收藏
页码:644 / 650
页数:7
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