Polyakov V I, Kireyeva O K, Tolstoguzov V B
Nahrung. 1985;29(2):153-60. doi: 10.1002/food.19850290210.
The thermodynamic compatibility of proteins belonging to different classes according to Osborne has been investigated in aqueous media. Phase equilibrium for water--ovalbumin--soybean globulin fraction, water--ovalbumin--casein, water--casein--gliadin and water--casein--soybean globulin fraction systems has been investigated. The data obtained were analysed according to the theoretical concepts of Scott, Patterson and Prausnitz concerning the effect of polymer molar masses and the solvent quality on the phase equilibrium in similar systems. The analysis performed indicates that these concepts can be applied to the water--protein A--protein B systems. The phase equilibrium in water--protein A--protein B systems has some distinctive features as compared to that in systems containing two synthetic polymers in the single solvent. Firstly, proteins are usually compatible in a broader concentration range as compared to common polymers. Moreover, the separation of water--protein A--protein B systems into two phases often results in a considerable concentration of one of the protein components. Apparently, the latter fact can be associated with the marked difference in the interaction parameter of proteins belonging to different classes with the solvent, and, hence, with the marked difference in the hydrophilicity of the proteins investigated.
在水性介质中，已对根据奥斯本分类属于不同类别的蛋白质的热力学相容性进行了研究。研究了水 - 卵清蛋白 - 大豆球蛋白组分、水 - 卵清蛋白 - 酪蛋白、水 - 酪蛋白 - 麦醇溶蛋白以及水 - 酪蛋白 - 大豆球蛋白组分体系的相平衡。根据斯科特、帕特森和普劳斯尼茨关于聚合物摩尔质量和溶剂性质对类似体系相平衡影响的理论概念，对所得数据进行了分析。所进行的分析表明，这些概念可应用于水 - 蛋白质A - 蛋白质B体系。与在单一溶剂中含有两种合成聚合物的体系相比，水 - 蛋白质A - 蛋白质B体系的相平衡具有一些独特的特征。首先，与普通聚合物相比，蛋白质通常在更宽的浓度范围内具有相容性。此外，水 - 蛋白质A - 蛋白质B体系分成两相往往会导致一种蛋白质组分的浓度相当高。显然，后一事实可能与属于不同类别的蛋白质与溶剂的相互作用参数的显著差异有关，因此，与所研究蛋白质的亲水性的显著差异有关。
