Polymères, Colloïdes, Interfaces, UMR CNRS Université du Maine, Le Mans, France.
Biomacromolecules. 2011 Feb 14;12(2):450-6. doi: 10.1021/bm101238r. Epub 2010 Dec 29.
Globular protein gels with a variety of structures were prepared by heating β-lactoglobulin solutions at different concentrations and different ionic strengths. The structure was analyzed in terms of the pair correlation function of the protein concentration, and the volume fraction of the gels was determined. A strong coarsening of the gel structure was observed upon increasing the NaCl concentration between 0.1 and 0.25 M. The mean square displacement of spherical particles with diameters between 0.2 and 2 μm was determined in solutions and in gels by multiparticle tracking of confocal laser scanning microscopy images. Brownian diffusion or trapping of spheres with different sizes was observed, depending on the gel structure. In few cases the diffusion was anomalous. The relationship between gel structure and particle mobility is discussed.
通过在不同浓度和不同离子强度下加热β-乳球蛋白溶液,制备了具有各种结构的球状蛋白凝胶。根据蛋白质浓度的对关联函数和凝胶的体积分数来分析结构。当 NaCl 浓度在 0.1 到 0.25 M 之间增加时,凝胶结构明显变粗。通过共焦激光扫描显微镜图像的多粒子跟踪,在溶液和凝胶中确定了直径在 0.2 到 2 μm 之间的球形粒子的均方位移。根据凝胶结构观察到不同大小的球体的布朗扩散或捕获。在少数情况下,扩散是异常的。讨论了凝胶结构与颗粒迁移率之间的关系。