Stability of sunflower 2S albumins and LTP to physiologically relevant in vitro gastrointestinal digestion

被引：21

作者：

Berecz, Bernadett ^{[1
,2
]}

Mills, E. N. Clare ^{[1
,4
]}

Paradi, Istvan ^{[2
]}

Lang, Ferenc ^{[2
]}

Tamas, Laszlo ^{[2
]}

Shewry, Peter R. ^{[3
]}

Mackie, Alan R. ^{[1
]}

机构：

[1] Inst Food Res, Norwich NR4 7UA, Norfolk, England

[2] Eotvos Lorand Univ, Dept Plant Physiol & Mol Plant Biol, H-1117 Budapest, Hungary

[3] Rothamsted Res, Harpenden AL5 2JQ, Herts, England

[4] Univ Manchester, Manchester Interdisciplinary Bioctr, Manchester M1 7DN, Lancs, England

来源：

FOOD CHEMISTRY | 2013年 / 138卷 / 04期

基金：

英国生物技术与生命科学研究理事会;

关键词：

Helianthus annuus L; Sunflower; 2S albumins; nsLTP; SFA8; In vitro digestion; Food allergy; LIPID TRANSFER PROTEIN; SEED STORAGE PROTEINS; MAJOR ALLERGEN; BRAZIL NUT; IMMUNOREACTIVITY; BER-E-1; L;

D O I：

10.1016/j.foodchem.2012.12.034

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

In order for a protein to elicit a systemic allergic response it must reach the circulatory system through the intestinal mucosa as a sufficiently large fragment with adequate structural integrity. Sunflower LTP and 2S albumins (SFA8 and three mixed fractions of Alb1 and Alb2) were digested in simulated gastric fluid (SGF) for 2 h and the conditions were then changed to mimic the intestinal environment for a further 2 h digestion. The effects of phosphatidylcholine (PC) and emulsification on the digestibility of the proteins were investigated. PC protected all of the proteins studied against both gastric and intestinal digestive enzymes but to different extents. Emulsification of SFA8 resulted in strong protection against digestion, which was further enhanced by the presence of PC in the SGF. These results highlight the importance of considering real food structures such as emulsified systems and also the gastrointestinal environment that proteins are exposed to once consumed when assessing allergenicity. (C) 2012 Elsevier Ltd. All rights reserved.

引用

页码：2374 / 2381

页数：8

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