Effect of heat treatment on the potential allergenicity and conformational structure of egg allergen ovotransferrin

被引:104
|
作者
Tong, Ping [1 ]
Gao, Jinyan [2 ]
Chen, Hongbing [1 ]
Li, Xin [1 ]
Zhang, Yin [1 ]
Jian, Shan [1 ]
Wichers, Harry [3 ]
Wu, Zhihua
Yang, Anshu
Liu, Fahui [1 ]
机构
[1] Nanchang Univ, Sino German Joint Res Inst, State Key Lab Food Sci & Technol, Nanchang 330047, Peoples R China
[2] Nanchang Univ, Dept Food Sci, Nanchang 330047, Peoples R China
[3] Wageningen UR, NL-6700 AA Wageningen, Netherlands
基金
中国国家自然科学基金;
关键词
Allergeniciry; Egg allergy; Heat treatment; Ovotransferrin; Protein structure; PROTEIN ISOLATE; WHITE PROTEINS; FOOD ALLERGY; ANTIGENICITY; LACTOGLOBULIN; MANAGEMENT; STABILITY; CHILDREN;
D O I
10.1016/j.foodchem.2011.08.084
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
The aim of this research was to assess heat induced changes of the potential allergenicity and the structure of ovotransferrin (OVT). Changes in conformational structure of OVT were characterised by circular dichroism (CD) spectroscopy, ultraviolet (UV) absorption spectroscopy and fluorescence spectroscopy. A reversible unfolding structure was found at 55-60 degrees C. followed by the loss of secondary structure at 70-80 degrees C. Cleavage and rearrangements of disulphide bonds occurred when heated above 80 degrees C. The indirect enzyme-linked immunosorbent assay (ELISA) of heat-treated OVT with egg allergic patients' sera and specific rabbit polyclonal antibodies against native OVT showed that the potential allergenicity of OVT correlated well with the structural changes. Allergenicity increased with the unfolding of its structure, and decreased with the cleavage of disulphide bonds and the rearrangements of disulphide bonds. The results suggested that conformational changes of OVT induced by heat treatment significantly influenced the allergenicity of OVT, and the potential allergenicity of heated OVT is related to individual patient characteristics. (C) 2011 Elsevier Ltd. All rights reserved.
引用
收藏
页码:603 / 610
页数:8
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