Alacabey, IhsanAcet, OmurOnal, BurcuDikici, EmrahKarakoc, VeyisGurbuz, FatmaOdabasi, Mehmet2025-02-152025-02-1520210170-08391436-2449https://doi.org/10.1007/s00289-020-03392-0https://hdl.handle.net/20.500.12514/5935Acet, Omur/0000-0003-1864-5694; karakoc, veyis/0000-0002-2511-6478; ODABASI, Mehmet/0000-0002-3288-132X; Alkan, Huseyin/0000-0002-0761-6436; DIKICI, EMRAH/0000-0002-3086-8156; ALACABEY, ihsan/0000-0002-3080-2296; ONAL ACET, Burcu/0000-0003-2408-8660Cryogels 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.en10.1007/s00289-020-03392-0info:eu-repo/semantics/closedAccessComposite CryogelsPumice ParticlesImacIgg SeparationArticle781055935607Q2Q2WOS:0005757250000032-s2.0-8509211289110