On the Crucial Importance of the pH for the Formation and Self-Stabilization of Protein Microgels and Strands

被引:65
作者
Tuan Phan-Xuan [1 ]
Durand, Dominique [1 ]
Nicolai, Taco [1 ]
Donato, Laurence [2 ]
Schmitt, Christophe [2 ]
Bovetto, Lionel [2 ]
机构
[1] Univ Maine, CNRS, UMR, F-72085 Le Mans 9, France
[2] Nestle Res Ctr, Dept Food Sci & Technol, CH-1000 Lausanne, Switzerland
关键词
BETA-LACTOGLOBULIN; LIGHT-SCATTERING; GLOBULAR-PROTEINS; X-RAY; AGGREGATION; KINETICS; DENATURATION; GELATION; RANGE;
D O I
10.1021/la203357p
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Stable suspensions of protein microgels are formed by heating salt-free beta-lactoglobulin solutions at concentrations up to about C = 50 g. L(-1) if the pH is set within a narrow range between 5.75 and 6.1. The internal protein concentration of these spherical particles is about 150 g . L(-1) and the average hydrodynamic radius decreases with increasing pH from 200 to 75 nm. The formation of the microgels leads to an increase of the pH, which is a necessary condition to obtain stable suspensions. The spontaneous increase of the pH during microgel formation leads to an increase of their surface charge density and inhibits secondary aggregation. This self-stabilization mechanism is not sufficient if the initial pH is below 5.75 in which case secondary aggregation leads to precipitation. Microgels are no longer formed above a critical initial pH, but instead short, curved protein strands are obtained with a hydrodynamic radius of about 15-20 nm.
引用
收藏
页码:15092 / 15101
页数:10
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