Alacabey, IhsanAcet, OmurOnal, BurcuDikici, EmrahKarakoc, VeyisGurbuz, FatmaAlkan, Huseyin2024-04-242024-04-2420210170-08391436-2449https://doi.org/10.1007/s00289-020-03392-0https://hdl.handle.net/11468/14356Cryogels with embedded natural adsorbent are new trend of chromatographic media for separation of biomolecules. In this report, experimental determination of immunoglobulin G (IgG) purification by Cu2+-attached pumice particles unified cryogel (Cu2+-PPUC) was performed. For this purpose, after preparation of Cu2+-attached pumice particles, they were unified with 2-hydroxyethyl methacrylate monomers to produce Cu2+-PPUC through polymerization of gel-forming precursors at subzero temperatures. IgG separation experiments were accomplished in a continuous column system. The highest binding capacity (596.8 mg/g) was obtained by working with 0.02 M phosphate buffer at pH 6.0. The chemical analysis of pumice was examined by X-ray fluorescence spectrometer. Scanning electron microscopy was performed to identify the morphology of Cu2+-PPUC. Langmuir adsorption model was best fitted to interaction when compared to Freundlich model. Temkin model was utilized to characterize adsorption, energetically. Purification ability of Cu2+-PPUC for IgG was shown with high selectivity via reducing SDS-PAGE electrophoresis.eninfo:eu-repo/semantics/closedAccessComposite CryogelsPumice ParticlesImacIgg SeparationPumice particle interface: a case study for immunoglobulin G purificationPumice particle interface: a case study for immunoglobulin G purificationArticle781055935607WOS:0005757250000032-s2.0-8509211289110.1007/s00289-020-03392-0Q1Q2