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

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/49874

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)

Submitter: 佐伯 宏樹

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