1. Pumice particle interface: a case study for immunoglobulin G purification
- Author
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Veyis Karakoç, Hüseyin Alkan, İhsan Alacabey, Emrah Dikici, Ömür Acet, Mehmet Odabaşı, Fatma Gurbuz, Burcu Önal, and Teknik Bilimler Meslek Yüksekokulu
- Subjects
inorganic chemicals ,Polymers and Plastics ,Scanning electron microscope ,Pumice Particles ,02 engineering and technology ,010402 general chemistry ,01 natural sciences ,symbols.namesake ,Adsorption ,Pumice ,Materials Chemistry ,Composite Cryogels ,chemistry.chemical_classification ,Biomolecule ,Langmuir adsorption model ,General Chemistry ,021001 nanoscience & nanotechnology ,Condensed Matter Physics ,IgG Separation ,0104 chemical sciences ,Electrophoresis ,chemistry ,Polymerization ,symbols ,Particle ,IMAC ,0210 nano-technology ,Nuclear chemistry - Abstract
Cryogels 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.
- Published
- 2020