Reversible Concanavalin A (Con A) ligands immobilization on metal chelated macroporous cellulose monolith and its selective adsorption for glycoproteins.

The present work deals with the development of novel affinity monolith with reversible protein ligands for protein chromatography. As for the formation of reversible ligands, Concanavalin A (Con A) is chelated with Cu(II)-iminodiacetic acid (IDA) immobilized macroporous cellulose monolith (MCM) for glycoprotein adsorption. The reversible immobilization is realized by Cu ions, which bridge affinity ligands and support by strong chelation interaction.

Fabrication and characterization of aligned macroporous monolith for high-performance protein chromatography.

In the present study, a freeze casting method combined with particle accumulation was applied to fabricate the aligned macroporous monolith for high-performance protein chromatography. For the preparation, the reactive colloids were first prepared by using glycidyl methacrylate and ethylene glycol dimethacrylate as monomers. Subsequently, these colloids accumulated regularly and polymerized into the aligned macroporous monolith.