Ruppert S, Sandler S I, Lenhoff A M
Center for Molecular and Engineering Thermodynamics, Department of Chemical Engineering, University of Delaware, Newark, Delaware 19716, USA.
Biotechnol Prog. 2001 Jan-Feb;17(1):182-7. doi: 10.1021/bp0001314.
A correlation between the osmotic second virial coefficient and the solubility of proteins is derived from classical thermodynamics to support an empirical relation previously found by Wilson and co-workers (1). The model is based on the equality of fugacities of the protein in the equilibrium phases, with the details of the model depending on the standard state used. The parameters in this model have been fitted to data for several systems, mainly with lysozyme as the protein. The model is found to describe experimental data, with variations in protein concentration, salt type and concentration, temperature, and pH, both qualitatively and quantitatively. Agreement between the model and the experimental data is very good for protein solubilities up to 30 mg/mL. Above this value the model underpredicts the experimental data, probably as a result of multibody interactions that are not included in the model here. Variations of the model parameters with protein type, temperature, pH, and salt type are discussed.
从经典热力学推导了渗透第二维里系数与蛋白质溶解度之间的相关性，以支持威尔逊及其同事先前发现的经验关系(1)。该模型基于平衡相中蛋白质逸度的相等性，模型的细节取决于所使用的标准状态。该模型中的参数已根据几个系统的数据进行了拟合，主要以溶菌酶作为蛋白质。发现该模型在定性和定量上都能描述蛋白质浓度、盐类型和浓度、温度以及pH值变化时的实验数据。对于高达30mg/mL的蛋白质溶解度，该模型与实验数据的一致性非常好。高于此值时，该模型对实验数据的预测偏低，这可能是由于模型中未包含的多体相互作用所致。讨论了模型参数随蛋白质类型、温度、pH值和盐类型的变化。
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