Institute for Chemical and Bioengineering, Department of Chemistry and Applied Bioscience, ETH Zurich, 8093 Zurich, Switzerland.
J Chromatogr A. 2013 Jul 12;1298:26-34. doi: 10.1016/j.chroma.2013.04.074. Epub 2013 Apr 30.
One of the main peculiarities in protein chromatography is that the adsorbing proteins and the adsorbent pores have comparable sizes. This has the consequence that the pore accessibility depends not only on the solute size but also on the loading conditions of the adsorbent because protein adsorption significantly reduces the size of the pores. A model that accounts for the pore size distribution of the stationary phase and for the pore shrinkage due to protein adsorption has been developed to describe mass transport and adsorption in the porous particles. This model has been shown to be equivalent to the general rate model (GRM) in the case of processes under highly diluted conditions with little adsorption. This implies that the model parameters determination follows the same procedure as for the classical GRM. The new pore model has been applied and compared to the GRM for the simulation of lysozyme breakthrough experiments and for the prediction of 5% dynamic binding capacity values solely based on static capacity measurements.
蛋白质层析的一个主要特点是，吸附蛋白质和吸附剂孔具有可比的尺寸。这意味着孔可及性不仅取决于溶质尺寸，还取决于吸附剂的装载条件，因为蛋白质吸附会显著减小孔的尺寸。已经开发出一种模型来描述多孔颗粒中的质量传递和吸附，该模型考虑了固定相的孔径分布和由于蛋白质吸附引起的孔收缩。在吸附量较小的高度稀释条件下，该模型与一般速率模型（GRM）等效。这意味着模型参数的确定与经典 GRM 相同。已经应用了新的孔模型，并将其与 GRM 进行比较，以模拟溶菌酶突破实验，并仅基于静态容量测量来预测 5%动态结合容量值。
