The rapid growth of single-use technology in the bioprocessing industry can be attributed to multiple advantages over traditional stainless-steel facilities including low cost of ownership, low risk of cross-contamination, added flexibility and easy disposal. The shift towards single-use systems (SUS) in the biopharmaceutical manufacturing industry has led to increasing instances of replacement of traditional resin-based chromatography with single-use chromatography during contaminant removal steps for bioprocessing of monoclonal antibody (mAb) and other biologics.<br/>A study of the underlying protein binding propensities for commercially available single-use anion exchange chromatography media (including quaternary ammonium (Q), primary amine (PA) and guanidinium (Gu) functionality) at various buffer composition, pH and salt conditions uncovers the robustness of protein binding by these chemistries. A combination of various orthogonal bioanalytical approaches (including gel electrophoresis and mass spectroscopy) were used to characterize the performance of these medias during upstream and downstream purification of mAb from a cell culture fluid. Further investigation revealed that the superior contaminant (host cell protein (HCP), DNA) removal performance of a salt-tolerant, Gu-functionalized AEX media was correlated to its robust protein binding attributes.

Fundamentals of host cell protein removal by single use AEX chromatography in mAb purification

ACS Fall 2021

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