Yu Shaoyong, Yao Ping, Jiang Ming, Zhang Guangzhao
The Key Laboratory of Molecular Engineering of Polymers and Department of Macromolecular Science, Fudan University, Shanghai 200433, China.
Biopolymers. 2006 Oct 5;83(2):148-58. doi: 10.1002/bip.20539.
Ovalbumin and lysozyme are two main proteins in hen egg white with the isoelectric points of 4.8 and 11, respectively. Herein we report the manufacture of stable, narrowly distributed nanogels (hydrodynamic radius about 100 nm) using a novel and convenient method: ovalbumin and lysozyme solutions were mixed at pH 5.3, the mixture solution was adjusted to pH 10.3, then subsequently stirred and heated. The nanogels were characterized using a combination of techniques. The nanogels have spherical shape and core-shell structure. The core is mainly composed of lysozyme and the shell is mainly composed of ovalbumin. The proteins in the nanogels are in denatured states and they are bound by intermolecular hydrophobic interactions, hydrogen bonds, and disulfide bonds. The charges of the nanogels can be modulated by the pH of the medium. The electrostatic repulsion of ovalbumin molecules on the nanogel surface stabilizes the nanogels in aqueous solution. The formation mechanism of the nanogels is discussed.
卵清蛋白和溶菌酶是鸡蛋清中的两种主要蛋白质，其等电点分别为4.8和11。在此，我们报告了一种使用新颖便捷的方法制备稳定、分布窄的纳米凝胶（流体动力学半径约为100 nm）：在pH 5.3下将卵清蛋白和溶菌酶溶液混合，将混合溶液调节至pH 10.3，然后搅拌并加热。使用多种技术对纳米凝胶进行了表征。纳米凝胶呈球形且具有核壳结构。核主要由溶菌酶组成，壳主要由卵清蛋白组成。纳米凝胶中的蛋白质处于变性状态，它们通过分子间疏水相互作用、氢键和二硫键结合。纳米凝胶的电荷可通过介质的pH值进行调节。纳米凝胶表面卵清蛋白分子的静电排斥作用使纳米凝胶在水溶液中稳定。讨论了纳米凝胶的形成机制。
