These last few decades, membranes and monoliths have been increasingly used as stationary phases for chromatography. Their fast mass transfer is mainly based on convection, which leads to reduced diffusion, which is usually observed in resins. Nevertheless, poor flow distribution, which causes inefficient binding, remains a major challenge for the development of both membrane and monolith devices. Moreover, the comparison of membranes and monoliths for biomolecule separation has been very poorly investigated. In this paper, the separation of two proteins, bovine serum albumin (BSA) and lactoferrin (LF), with similar sizes, but different isoelectric points, was investigated at a pH of 6.0 with a BSA-LF concentration ratio of 2/1 (2.00 mg·mL−1
BSA and 1.00 mg·mL−1
LF solution) using strong cation exchange membranes and monoliths packed in the same housing, as well as commercialized devices. The feeding flow rate was operated at 12.0 bed volume (BV
)/min for all devices. Afterward, bound LF was eluted using a phosphate-buffered saline solution with 2.00 M NaCl. Using membranes in a CIM housing from BIA Separations (Slovenia) with porous frits before and after the membrane bed, higher binding capacities, sharper breakthrough curves, as well as sharper and more symmetric elution peaks were obtained. The monolith and commercialized membrane devices showed lower LF binding capacity and broadened and non-symmetric elution peaks.
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