Pumice particle interface: a case study for immunoglobulin G purification
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Pumice particle interface: a case study for immunoglobulin G purification İhsan Alacabey1 · Ömür Acet2 · Burcu Önal2 · Emrah Dikici2 · Veyis Karakoç3 · Fatma Gürbüz4 · Hüseyin Alkan5 · Mehmet Odabaşı2 Received: 16 June 2020 / Revised: 20 August 2020 / Accepted: 24 September 2020 © Springer-Verlag GmbH Germany, part of Springer Nature 2020
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 C u2+-attached pumice particles unified cryogel 2+ (Cu -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. Keywords Composite cryogels · Pumice particles · IMAC · IgG separation
* Hüseyin Alkan [email protected] 1
Vocational School of Health Services, Mardin Artuklu University, Mardin, Turkey
2
Chemistry Department, Faculty of Arts and Science, Aksaray University, Aksaray, Turkey
3
Eldivan Vocational School of Health Services, Cankiri Karatekin University, Cankiri, Turkey
4
Department of Environmental Engineering, Aksaray University, Aksaray, Turkey
5
Biochemistry Division, Faculty of Pharmacy, Dicle University, Diyarbakır, Turkey
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Vol.:(0123456789)
Polymer Bulletin
Introduction Immunoglobulin G (IgG), which is significant molecule therapeutically, is one of main constituents of human serum [1]. It is one of the most important antibodies for industrial production (27 tons/year) [2]. IgG is required for preservation against pathogenic factors such as fungi, bacteria, viruses [3]. It has a liability in the treatment of some important health problems such as idiopathic purpura, autoimmune and chronic inflammatory illnesses, immunodeficiency and cancer treatment [1]. And also, it can cross the human placenta to protect the newborn infants for the first few months. Due to its good specificity and abundance against antigens, IgG has become the major antibody in terms of clinical and immunological studies [4, 5]. Because of the some important features mentioned above, effective purification of this valuable biomolecule for the demanded purity is a big bottleneck for pharmaceutical industry [5]. Different techniques have been operated by researcher
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