Affinity microspheres and their application to lysozyme adsorption: Cibacron Blue F3GA and Cu(II) with poly(HEMA‐EGDMA)

Denizli, Fatma; Deni̇zli̇, Adil; Arıca, M. Yakup

doi:10.1002/(sici)1097-0126(199905)48:5<360::aid-pi142>3.0.co;2-#

Cited by 17 publications

(9 citation statements)

References 27 publications

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“…Electrostatic interactions may be important for protein retention in hydrophobic interaction chromatography 4. 6, 13, 21 Figure 6 shows the amount of lipase adsorbed onto phenylalanine‐containing poly(HEMA/MAPA‐5) membranes at different pH values. The maximum lipase adsorption value was obtained at pH 7.0.…”

Section: Resultssupporting

confidence: 89%

“…The ligand‐carrying membranes used in biomolecule chromatography are the most frequently obtained after chemical modification of natural and synthetic polymeric membranes such as chitin, chitosan, cellulose acetate, acrylic polymers, poly(vinyl alcohol) or inorganic glass hollow fibres 18–21. We suggest here a novel method of introducing a hydrophobic ligand into the polymer membrane structure via copolymerisation of HEMA monomer with a ligand‐carrying comonomer, ie methacrylamidophenylalanine.…”

Section: Resultsmentioning

confidence: 99%

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Membrane with incorporated hydrophobic ligand for hydrophobic interaction with proteins: application to lipase adsorption

Bayramoğlu

Deni̇zli̇

Arıca

2002

Polymer International

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In this study, phenylalanine as a hydrophobic ligand was covalently attached on a co‐monomer, methacryloyl chloride. Then, poly(2‐hydroxyethyl methacrylate‐co‐methacrylamido‐phenylalanine), poly(HEMA/MAPA), membranes were prepared by UV‐initiated photopolymerization of 2‐hydroxyethyl methacrylate and methacrylamido‐phenylalanine. The lipase adsorption of these poly(HEMA/MAPA) membranes was determined by changing the hydrophobic ligand density, pH, temperature and concentration of lipase in the adsorption medium. The lipase adsorption capacity of the membranes increased as the ligand density on the membrane surface increased. The non‐specific adsorption of lipase on the poly(2‐hydroxyethyl methacrylate) membranes was negligible (12 µg cm−2 of membrane). The adsorption phenomena appeared to follow a typical Langmuir isotherm. The maximum adsorption capacity (Qm) of the poly(HEMA/MAPA‐5) membrane for lipase was 215 µg cm−2 of membrane. The equilibrium constant (kd) value was 1.43 mg ml−1. The lipase could repeatedly be adsorbed and desorbed on the affinity membrane without any significant loss in the adsorption capacity of the membrane. © 2002 Society of Chemical Industry

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Section: Resultssupporting

confidence: 89%

Section: Resultsmentioning

confidence: 99%

Membrane with incorporated hydrophobic ligand for hydrophobic interaction with proteins: application to lipase adsorption

Bayramoğlu

Deni̇zli̇

Arıca

2002

Polymer International

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“…IMAC is an effective analytical and preparative separation method for therapeutic proteins, peptides, nucleic acids, hormones, and enzymes 19–23. The separation is based on the interaction of a Lewis acid (electron pair donor), i.e., a chelated metal ion, with an electron acceptor group on the surface of the protein 24–26.…”

Section: Introductionmentioning

confidence: 99%

“…18 IMAC is an effective analytical and preparative separation method for therapeutic proteins, peptides, nucleic acids, hormones, and enzymes. [19][20][21][22][23] The separation is based on the interaction of a Lewis acid (electron pair donor), i.e., a chelated metal ion, with an electron acceptor group on the surface of the protein. [24][25][26] Proteins are assumed to interact mainly through the imidazole group of histidine and, to a lesser extent, the indoyl group of tryptophan and the thiol group of cysteine.…”

Section: Introductionmentioning

confidence: 99%

New generation polymeric nanospheres for catalase immobilization

Akgöl

Öztürk

Deni̇zli̇

2009

J of Applied Polymer Sci

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Monosize poly(2-hydroxyethyl methacrylate-co-N-methacryloly-L-histidinemethylester) [mon-poly (HEMA-MAH)] nanospheres were prepared via surfactant-free emulsion polymerization method. L-Histidine groups of the mon-poly(HEMA-MAH) nanospheres were chelated with Fe 3þ ions. Mon-poly(HEMA-MAH) nanospheres were characterized by Fourier transform infrared spectroscopy, proton NMR, and scanning electron microscopy. Particle size of the mon-poly(HEMA-MAH) nanospheres was measured by Zeta Sizer. Elemental analysis of MAH for nitrogen was estimated as 0.94 mmol/g polymer. The catalase immobilized onto the mon-poly(HEMA-MAH)-Fe 3þ nanospheres resulted in increasing the enzyme stability with time. Optimum operational temperature for both immobilized preparations was the same, and the temperature profiles of the immobilized preparations were significantly broader. It was observed that enzyme could be repeatedly adsorbed and desorbed on the monpoly(HEMA-MAH)-Fe 3þ nanospheres without loss of adsorption capacity or enzymic activity.

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“…When General Peng-The Huai signed the armistice, he did so with the title of "commander of the Chinese volunteer army" despite the fact that he was a general and the vice president of the People's Revolutionary Military Committee of China. 49 …”

Section: Depiction Of Chinese In the Turkish War Narrativesmentioning

confidence: 99%

Perceptions of China in the Turkish Korean War Narratives

Üngör

2006

Turkish Studies

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Affinity microspheres and their application to lysozyme adsorption: Cibacron Blue F3GA and Cu(II) with poly(HEMA‐EGDMA)

Cited by 17 publications

References 27 publications

Membrane with incorporated hydrophobic ligand for hydrophobic interaction with proteins: application to lipase adsorption

Membrane with incorporated hydrophobic ligand for hydrophobic interaction with proteins: application to lipase adsorption

New generation polymeric nanospheres for catalase immobilization

Perceptions of China in the Turkish Korean War Narratives

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