Digestibility and immunoreactivity of soybean β-conglycinin and its deglycosylated form

被引:53
作者
Amigo-Benavent, Miryam [1 ]
Clemente, Alfonso [2 ]
Ferranti, Pasquale [3 ]
Caira, Simonetta [3 ]
Dolores del Castillo, M. [1 ]
机构
[1] CSIC UAM, Inst Invest Ciencias Alimentac, Dept Food Anal & Bioact, Madrid 28049, Spain
[2] EEZ CSIC, Dept Physiol & Biochem Anim Nutr, Granada 18100, Spain
[3] Univ Naples Federico 2, Dept Food Sci, I-80055 Portici, NA, Italy
关键词
beta-Conglycinin; Deglycosylation; Glycan moieties; In vitro immunoreactivity; In vitro digestibility; Soybean; FOOD ALLERGENS; GLYCINE-MAX; IN-VITRO; ALPHA-SUBUNIT; SOY; STABILITY; PROTEINS; DIGESTION; PRODUCTS; ANTIGENICITY;
D O I
10.1016/j.foodchem.2011.06.015
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
IgE-mediated allergy to soybean may be connected to an incomplete protein digestion causing an inappropriate immune response in the gut. The aim of this study was to gain insight on the digestibility and immunoreactivity of beta-conglycinin and its deglycosylated form. To achieve this goal both proteins were digested mimicking gastrointestinal physiological conditions. Digests were characterised by SDS-PAGE, MALDI-TOF-MS and immunological assays. Data on IgG binding western blot provided key information related to the composition of the digests indicating that whereas deglycosylated beta-conglycinin was completely removed by gastrointestinal digestion, alpha and beta subunits of beta-conglycinin glycoprotein partially survive the process of digestion. Such differential digestive behaviour might be influenced by glycan moieties, at least to some extent, and should be an additional factor to be considered on its potential allergenicity. Results also support the existence of linear epitopes in the three subunits (alpha, alpha', and beta) of both protein forms. (C) 2011 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1598 / 1605
页数:8
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