Influence of the ionic strength on the heat-induced aggregation of the globular protein β-lactoglobulin at pH 7

被引：93

作者：

Baussay, K ^{[1
]}

Le Bon, C ^{[1
]}

Nicolai, T ^{[1
]}

Durand, D ^{[1
]}

Busnel, JP ^{[1
]}

机构：

[1] Univ Maine, CNRS, UMR, F-72085 Le Mans 9, France

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2004年 / 34卷 / 1-2期

关键词：

globular protein; beta-lactoglobulin; aggregation; gel; light scattering;

D O I：

10.1016/j.ijbiomac.2003.11.003

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The influence of the ionic strength on the structure of beta-lactoglobulin aggregates formed after heating at pH 7 has been studied using static and dynamic light scattering. The native protein depletion has been monitored using size exclusion chromatography. Above a critical association concentration (CAC) well-defined clusters are formed containing about 100 monomers. The CAC increases with decreasing ionic strength. The so-called primary aggregates associate to form self similar semi-flexible aggregates with a large scale structure that is only weakly dependent on the ionic strength. The local density of the aggregates increases with increasing ionic strength. At a critical gel concentration, C-g, the size of the aggregates diverges. C-g decreases from 100 g/l without added salt to 1 g/l at 0.4 M NaCl. For C > C-g the system gels except at high ionic strength close to C-g where the gels collapse under gravity and a precipitate is formed. (C) 2003 Elsevier B.V. All rights reserved.

引用

页码：21 / 28

页数：8

共 33 条

[1] The effect of temperature and ionic strength on the dimerisation of beta-lactoglobulin [J].