Pumice particle interface: a case study for immunoglobulin G purification
Yükleniyor...
Tarih
2020
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Springer Science and Business Media Deutschland GmbH
Erişim Hakkı
info:eu-repo/semantics/embargoedAccess
Özet
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.
Açıklama
Anahtar Kelimeler
Composite Cryogels, IgG Separation, IMAC, Pumice Particles
Kaynak
Polymer Bulletin
WoS Q Değeri
Q2
Scopus Q Değeri
Q1
Cilt
-
Sayı
-
