Agena S M, Bogle I D, Pessoa F L
Department of Chemical and Biochemical Engineering, University College London, Torrington Place, London, WC1E 7JE, United Kingdom.
Biotechnol Bioeng. 1997 Jul 5;55(1):65-71. doi: 10.1002/(SICI)1097-0290(19970705)55:1<65::AID-BIT8>3.0.CO;2-V.
Modeling of the properties of biochemical components is gaining increasing interest due to its potential for further application within the area of biochemical process development. Generally protein solution properties such as protein solubility are expressed through component activity coefficients which are studied here. The original UNIQUAC model is chosen for the representation of protein activity coefficients and, to the best of our knowledge, this is the first time it has been directly applied to protein solutions. Ten different protein-salt-water systems with four different proteins, serum albumin, alphacymotrypsin, beta-lactoglobulin and ovalbumin, are investigated. A root-mean-squared deviation of 0.54% is obtained for the model by comparing calculated protein activity coefficients and protein activity coefficients deduced from osmotic measurements through virial expansion. Model predictions are used to analyze the effect of salt concentrations, pH, salt types, and temperature on protein activity coefficients and also on protein solubility and demonstrate consistency with results from other references.
由于生化成分特性建模在生化过程开发领域具有进一步应用的潜力，因此越来越受到关注。一般来说，蛋白质溶液的特性，如蛋白质溶解度，是通过组分活度系数来表示的，本文对此进行了研究。选择原始的UNIQUAC模型来表示蛋白质活度系数，据我们所知，这是该模型首次直接应用于蛋白质溶液。研究了十种不同的蛋白质-盐-水体系，其中包含四种不同的蛋白质，即血清白蛋白、α-胰凝乳蛋白酶、β-乳球蛋白和卵清蛋白。通过比较计算得到的蛋白质活度系数和通过维里展开从渗透压测量推导得到的蛋白质活度系数，该模型的均方根偏差为0.54%。模型预测用于分析盐浓度、pH值、盐类型和温度对蛋白质活度系数以及蛋白质溶解度的影响，并证明与其他参考文献的结果一致。
