title: Comparative study of strong anion exchangers: structure-related chromatographic performances.
abstract: Chromatographic performances are highly influenced by operational parameters. New ion exchangers have tailored matrices providing low backpressure and allowing high flow velocity. By systematic frontal analysis and selectivity determination at different flow rates, we suggested an independent evaluation of major anion exchangers to facilitate media selection, and investigated the relationship between (i) surface modification and (ii) chromatographic performances. Structure-extended resins showed higher binding capacities compared to resins with conventional ligands directly attached to the matrix. Moreover, they maintained mainly high capacities even with extremely high flow velocities. Ligand accessibility was therefore largely enhanced, allowing proteins to interact and bind under harsh conditions. High throughput resins can be used for purification of high volume and high concentration feedstock in limited time. This results in higher productivity and could contribute to cost reduction.
authors.affiliation: EA4135, ESTBB, Université de Bordeaux, 146 rue Léo Saignat, 33076 Bordeaux cedex, France.
authors.forename: Jerome
authors.initials: J
authors.lastname: Pezzini
authors.forename: Charlotte
authors.initials: C
authors.lastname: Cabanne
authors.forename: Xavier
authors.initials: X
authors.lastname: Santarelli
mesh_terms: D000818:Animals; D002417:Cattle; D002852:Chromatography, Ion Exchange / Q000191:economics / Q000295:instrumentation* / Q000379:methods*; D003207:Conalbumin / Q000737:chemistry / Q000302:isolation & purification; D011485:Protein Binding; D012117:Resins, Synthetic / Q000737:chemistry* / Q000191:economics; D012709:Serum Albumin / Q000737:chemistry / Q000302:isolation & purification
chemical_list: D012117:Resins, Synthetic; D012709:Serum Albumin; D003207:Conalbumin