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In vitro digestion of major allergen in salmon roe and its peptide portion with proteolytic resistance
Title: | In vitro digestion of major allergen in salmon roe and its peptide portion with proteolytic resistance |
Authors: | Fujita, Shingo Browse this author | Shimizu, Yutaka Browse this author →KAKEN DB | Kishimura, Hideki Browse this author →KAKEN DB | Watanabe, Kazuhiko Browse this author | Hara, Akihiko Browse this author →KAKEN DB | Saeki, Hiroki Browse this author →KAKEN DB |
Keywords: | Food allergen | Salmon roe | Allergenicity | Digestibility | β′-component | Yolk protein | Proteolytic tolerance | IgE-binding ability |
Issue Date: | 1-Feb-2012 |
Publisher: | Elsevier |
Journal Title: | Food Chemistry |
Volume: | 130 |
Issue: | 3 |
Start Page: | 644 |
End Page: | 650 |
Publisher DOI: | 10.1016/j.foodchem.2011.07.099 |
Abstract: | A fish yolk protein, β′-component (β′-c), is the major allergen in chum salmon roe. The effect of proteolysis on the allergenicity of β′-c was estimated. Changes in the IgE-binding ability of β′-c upon pepsin and trypsin digestion were investigated by monitoring the proteolytic cleavage. In the pepsin–trypsin digestion of chum salmon yolk protein, the β′-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 β′-c. These results suggest that β′-c reaches the small intestine in the form of high-molecular-mass components with IgE-binding ability in vivo. |
Type: | article (author version) |
URI: | http://hdl.handle.net/2115/49874 |
Appears in Collections: | 水産科学院・水産科学研究院 (Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 佐伯 宏樹
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