粘度测量和Avramov模型间接测定蛋白质玻璃化转变温度的可能性

K. Monkos
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引用次数: 2

摘要

摘要本文介绍了鸡蛋清溶菌酶、牛ß-乳球蛋白、人和猪免疫球蛋白IgG水溶液在5℃~ 55℃范围内的粘度测定结果。根据Avramov模型得出的公式,分析了蛋白质溶液的粘度-温度依赖性。阿夫拉莫夫方程的参数之一是玻璃化转变温度Tg。结果表明,对于所有被研究的蛋白质,溶液的Tg随着浓度的增加而增加。为了确定干燥蛋白的玻璃化转变温度Tg,p,采用了一种改进的戈登-泰勒方程。该方程给出了Tg与溶液浓度之间的关系,Tg,p和依赖于蛋白质-溶剂相互作用强度的参数是拟合参数。由此确定所研究的干蛋白的玻璃化转变温度范围为227.3 K(牛ß-乳球蛋白)至260.6 K(蛋清溶菌酶)。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
On the Possibility of Indirect Determination of the Glass Transition Temperature of Proteins from Viscosity Measurements and Avramov's Model
Abstract The paper presents the results of viscosity determinations on aqueous solutions of hen egg-white lysozyme, bovine ß-lactoglobulin, human and porcine immunoglobulin IgG at a wide range of concentrations and at temperatures ranging from 5oC to 55oC. Viscosity-temperature dependence of the proteins solutions is analyzed based on a formula resulting from the Avramov's model. One of the parameters in the Avramov's equation is the glass transition temperature Tg. It turns out that for all studied proteins, the Tg of the solution increases with increasing concentration. To determine the glass transition temperature of the dry protein Tg,p, a modified form of the Gordon-Taylor equation is used. This equation gives the relationship between Tg and the concentration of the solution, and Tg,p and a parameter dependent on the strength of protein-solvent interaction are fitting parameters. Thus determined the glass transition temperature for the studied dry proteins is in the range from 227.3 K (for bovine ß-lactoglobulin) to 260.6 K (for hen egg-white lysozyme).
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