title: PHEMA based composite cryogels with loaded hydrophobic beads for lysozyme purification.
abstract: The purpose of this study is to synthesize megaporous cryogel loaded with hydrophobic affinity beads which can be utilized for the purification of lysozyme from chicken egg-white. N-methacryloyl-(L)-tryptophan methylester (MATrp) was used as the hydrophobic ligand. In the first step, poly(glycidyl methacrylate-N-methacryloyl-(L)-tryptophan methyl-ester) [PGMATrp] beads (2.2 μm in diameter) were produced by dispersion polymerization. In the second step, the poly(2-hydroxyethyl methacrylate) (PHEMA) cryogel loaded with PGMATrp beads [PHEMA/PGMATrp composite cryogel] was polymerized initiated by N,N,N',N'-tetramethylene diamine (TEMED) and ammonium persulfate (APS) at -12°C. Lysozyme adsorption capacity of the PHEMA/PGMATrp composite cryogel (332.7 mg/g polymer) was improved significantly due to the loading of PGMATrp beads into the cryogel structure. The hydrophobic MATrp comonomer played a vital role in this binding mechanism. The PHEMA/PGMATrp composite cryogel could be used many times without decreasing the lysozyme adsorption amount significantly. The main advantage of the PHEMA/PGMATrp composite cryogel is the high adsorption capacity.
authors.affiliation: Department of Chemistry, Biochemistry Division, Hacettepe University, Ankara, Turkey.
authors.forename: Deniz
authors.initials: D
authors.lastname: Türkmen
authors.affiliation: Department of Chemistry, Biochemistry Division, Hacettepe University, Ankara, Turkey. Electronic address: denizli@hacettepe.edu.tr.
authors.forename: Adil
authors.initials: A
authors.lastname: Denizli
mesh_terms: D002846:Chromatography, Affinity; D059985:Cryogels / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D009113:Muramidase / Q000737:chemistry* / Q000302:isolation & purification*; D011102:Polyhydroxyethyl Methacrylate / Q000737:chemistry*
chemical_list: D059985:Cryogels; D011102:Polyhydroxyethyl Methacrylate; D009113:Muramidase
keywords: Affinity chromatography; Cryogels; Lysozyme purification; Particle loading; Protein purification