Developing a chromatographic column model for bovine serum albumin on strong anion-exchanger Source30Q using data from confocal laser scanning microscopy.

A systematic approach for the development of a column model for protein purification is introduced. The approach includes phenomenological investigations of mass transfer and adsorption behaviour applying confocal laser scanning microscopy (CLSM). Insights from CLSM measurements are then implemented mathematically into a single particle model which is coupled afterwards with a column model (i.e. general rate model). Finally, the general rate model is used to predict the results from pulse and frontal analysis in a chromatographic column. The applied exemplary chromatographic system is bovine serum albumin (BSA) on strong anion-exchanger Source30Q at neutral pH value.