Bayramoğlu, GülayŞenel, Ayşegül ÜlküYalçın, EmineArıca, M. Yakup2020-06-252020-06-252006closedAccess0959-81031097-0126https://doi.org/10.1002/pi.1905https://hdl.handle.net/20.500.12587/3667Poly(GMA/MMA) beads were synthesized from glycidyl methacrylate (GMA) and methyl methacrylate (MMA) in the presence of a cross-linker (i.e. ethyleneglycol dimethacrylate) (EGDMA) via suspension polymerization. The epoxy groups of the poly(GMA/MMA) beads were converted into amino groups with either ammonia or 1,6-diaminohexane (i.e. spacer-arm). An L-histidine ligand was then covalently immobilized on the aminated (poly(GMA/MMA)-AH) and/or the spacer-arm attached (poly(GMA/MMA)-SAH) beads using glutaric dialdehyde as a coupling agent. Both affinity adsorbents were used in human serum albumin (HSA) adsorption/desorption studies under defined pH, ionic strength or temperature conditions in a batch reactor. The spacer-arm attached affinity adsorbent resulted in an increase in the adsorption capacity to HSA when compared to the aminated counterpart (i.e. poly(GMA/MMA)-AH). The maximum adsorption capacities of the affinity adsorbents were found to be significantly high, i.e. 43.7 and 80.2 mg g(-1) (of the beads), while the affinity constants, evaluated by the Langmuir model, were 3.96 x 10(-7) and 9.53 x 10(-7) molL(-1) for poly(GMA/MMA) -AH and poly(GMA/MMA)-SAH, respectively. The adsorption capacities of the affinity adsorbents were decreased for HSA by increasing the ionic strength, adjusted with NaCl. The adsorption kinetics of HSA were analysed by using pseudo-first and pseudo-second-order equations. The second-order equation fitted well with the experimental data. (c) 2005 Society of Chemical Industry.eninfo:eu-repo/semantics/closedAccesspoly(GMA/MMA) beadsspacer-armhistidineaffinity adsorbentshuman serum albuminadsorptionArticle551404810.1002/pi.19052-s2.0-30444450438Q1WOS:000234608100007Q2