X-ray and light scattering study of the structure of large protein aggregates at neutral pH

被引：78
作者：
Pouzot, M
Nicolai, T
Visschers, RW
Weijers, M
机构：
[1] Wageningen Ctr Food Sci, NL-6700 AN Wageningen, Netherlands
[2] Univ Maine, CNRS, UMR, F-72085 Le Mans 9, France
[3] Univ Wageningen & Res Ctr, Dept Agrotechnol & Food Sci, Lab Phys Chem & Colloid Sci, NL-6703 HB Wageningen, Netherlands
[4] NIZO Food Res, NL-6718 ZB Ede, Netherlands
来源：
FOOD HYDROCOLLOIDS | 2005年 / 19卷 / 02期
关键词：
globular proteins; ovalbumin; beta-lactoglobulin; ionic strength; SAXS; light scattering; structure;
D O I：
10.1016/j.foodhyd.2004.06.003
中图分类号：
O69 [应用化学];
学科分类号：
081704 ;
摘要：
The structure of large ovalbumin and beta-lactoglobulin aggregates formed after heat-denaturation at neutral pH was studied using a combination of light and small-angle X-ray scattering. The effect of the electrostatic interactions was investigated by varying the ionic strength. The results were compared with images obtained using cryo-TEM. The structure of ovalbumin aggregates is compatible with that of semi-flexible strings of monomers that are more flexible and increasingly branched with increasing ionic strength. The persistence length increases with decreasing ionic strength. beta-lactoglobulin aggregates consist of clusters of primary aggregates that are formed in the first step of the aggregation process. At low ionic strength the association of primary aggregates is mostly head to tail, while with increasing ionic strength denser clustering of the primary aggregates is observed. (C) 2004 Elsevier Ltd. All rights reserved.
引用
收藏
页码：231 / 238
页数：8
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