Back to Search Start Over

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

Authors :
Fujita, Shingo
Shimizu, Yutaka
Kishimura, Hideki
Watanabe, Kazuhiko
Hara, Akihiko
Saeki, Hiroki
Source :
Food Chemistry. Feb2012, Vol. 130 Issue 3, p644-650. 7p.
Publication Year :
2012

Abstract

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 >10kDa remained throughout the digestion process. Specifically, the peptide sequence between 31-Y and 119-Q (10kDa) 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. [Copyright &y& Elsevier]

Details

Language :
English
ISSN :
03088146
Volume :
130
Issue :
3
Database :
Academic Search Index
Journal :
Food Chemistry
Publication Type :
Academic Journal
Accession number :
65345251
Full Text :
https://doi.org/10.1016/j.foodchem.2011.07.099