Protein adsorption and separation with monomodal and multimodal anion exchange chromatography resins. Part I. Multicomponent adsorption properties and frontal chromatography

BACKGROUND Multimodal ion exchangers, containing ligands combining charged and hydrophobic moieties, exhibit enhanced separation compared to monomodal exchangers under low loading conditions. Commercial applications often require high protein loads such conditions have not been investigated extensively, especially for multimodal anion exchangers. This work compares adsorption by frontal chromatography a commercial (Nuvia HP-Q) two aPrime Capto Adhere) using bovine serum albumin (BSA) monomer dimer as model. RESULTS Greater dimer–monomer selectivity is observed Nuvia Adhere than HP-Q at loads. However, binary isotherms show higher binding capacity greater HP-Q, despite having the same ligand density. Higher salt concentrations reduce strength in all cases, but this reduction less pronounced resins. As result, increases latter concentrations. Confocal laser scanning microscopy shows that, during co-adsorption, displacement of occurs each resin. becomes very slow resins sequential adsorption. The give poorer chromatography, accompanied recovery substantial on-column formation aggregates. CONCLUSION model proteins studied varies with concentration load. At loads, can result aggregate negatively impacting kinetics competitive separation. © 2022 Authors. Journal Chemical Technology Biotechnology published John Wiley & Sons Ltd on behalf Society Industry (SCI).