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Öğe Affinity separation of plasma proteins using a newly synthesized methacrylamidoalanine incorporated porous pHEMA membranes(Marcel Dekker Inc, 2002) Yavuz, H.; Patir, S.; Say, R.; Arica, Y.; Denizli, A.In this study, we synthesized a novel adsorbent to obtain high protein-adsorption capacity utilizing 2-methacrylamidoalanine (MAAL) containing membrane. Amino acid-ligand MAAL was synthesized by using methacrylochloride and alanine. Then, poly(2-hydroxyethylmethacrylate-co-2-methacrylamidoalanine) [p(HEMA-co-MAAL)] membranes were prepared by UV-initiated photopolymerization of HEMA and MAAL in the presence of an initiator (azobisisobutyronitrile, AIBN). Synthesized MAAL was characterized by nuclear magnetic resonance spectroscopy. p(HEMA-co-MAAL) membranes were characterized by swelling studies, porosimeter, scanning electron microscopy, Fourier transform-infra red spectroscopy, and elemental analysis. These membranes have macropores in the size range 5-10 mum. Different metal ions including Zn(II), Ni(II), Co(II), and Cu(II) were chelated on these membranes. p(HEMA-co-MAAL) were used in the adsorption of human serum albumin (HSA) from aqueous media containing different amounts of albumin (0.1-5.0 mg L-1) and at different pH values (4.0-8.0). The maximum HSA adsorption was observed at pH 5.0. The nonspecific adsorption of HSA on the pHEMA membranes was negligible 0.9 mug cm(-2). MAAL incorporation significantly increased the HSA adsorption (1.76 mg cm(-2)). The HSA adsorption capacities of the metal-incorporated membranes were Greater than that of the p(HEMA-co-MAAL) membranes under the same conditions. Higher HSA adsorption capacity was observed from the human plasma (2.88 mg HSA cm(-2)).Öğe Dye-affinity hollow-fibres and their lysozyme adsorption-desorption characteristics(John Wiley & Sons Ltd, 2001) Şenel, S.; Akgöl, S.; Arica, Y.; Denizli, A.Dye-affinity adsorption is increasingly used for protein separation. Hollow-fibres have advantages as adsorbents in comparison to conventional bead supports because they are not compressible and can eliminate internal diffusion limitations. The aim of this study was to explore in detail the performance of polyamide hollow-fibres to which Reactive Green HE-4BD was attached for adsorption of lysozyme. The hollow-fibre was characterized by scanning electron microscopy. These dye-carrying hollow-fibres (26.3 mu mol g(-1)) were used in the lysozyme adsorption-elution studies. The effect of initial concentration of lysozyme and medium pH on the adsorption efficiency of dye-attached hollow-fibres was studied in a batch system. The non-specific adsorption of lysozyme on the polyamide hollow-fibres was 1.8 mgg(-1). Reactive Green HE-4BD attachment significantly increased the lysozyme adsorption up to 41.1 mgg(-1). Langmuir adsorption model was found to be applicable in interpreting lead adsorption by Reactive Green HE-4BD attached hollow fibres. Significant amount of the adsorbed lysozyme (up to 95%) was eluted in lh in the elution medium containing 1.0M NaSCN at pH 8.0. In order to determine the effects of adsorption conditions on possible conformational changes of lysozyme structure, fluorescence spectrophotometry was employed. We concluded that polyamide dye-affinity hollow-fibres can be applied for lysozyme adsorption without causing any significant conformational changes. Repeated adsorption-elution processes showed that these dye-attached hollow-fibres are suitable for lysozyme adsorption. (C) 2001 Society of Chemical Industry.Öğe Heavy metal separation capacity of a porous methacrylamidophenylalanine containing membrane based on a polyhydroxyethyl methacrylate matrix(Marcel Dekker Inc, 2001) Denizli, A.; Say, R.; Patir, S.; Arica, Y.The abilities of various sorbent materials for heavy metal removal have been reported in the literature. We have developed a novel approach to obtain high metal-sorption capacity utilizing a membrane containing 2-methacrylamidophenylalanine. Metal-complexing ligand 2-methacrylamidophenylalanine (MAPA) was synthesized through the use methacrylo chloride and phenylalanine. Then, poly(2-hydroxyethyhmethacrylate-co-2-methacrylamidophenylalanine) (p(HEMA-co-MAPA)) membranes were prepared by UV-initiated photopolymerization of HEMA and MAPA in the presence of the initiator azobisisobutyronitrile. MAPA monomer was characterized by nuclear magnetic resonance spectroscopy. p(HEMA-co-MAPA) membranes were characterized by swelling studies, scanning electron microscopy, Fourier transform infrared spectroscopy, and elemental analysis. These membranes have large pores; the micropore dimensions are approximately 5-10 mum. p(HEMA-co-MA-PA) affinity membranes with a swelling ratio of 133.2% and containing 18.9 mmol MAPA/m(2) were used in the removal of the heavy-metal ions of copper, nickel, and mercury from aqueous media containing different amounts of these ions (5-600 mg/L) and at different pH values (2.0-7.0). The maximum adsorption capacities of heavy metal ions onto the MAPA-containing membranes under noncompetitive conditions were 23.8 = mmol/m(2) for Cu(II), 29.1 mmol/m(2) for Ni(II), and 50.3 mmol/m(2) for Hg(II). The affinity order was Hg(II) > Ni(II) > Cu(II). The adsorption of heavy metal ions increased with increasing pH and reached a plateau value at approximately pH 5.0. Adsorption of heavy metal ions from artificial wastewater was also studied. The adsorption capacities were 11.9 mmol/m(2) for Cu(II), 7.33 mmol/m(2) for Ni(II), and 9.79 mmol/m(2) for Hg(II). Desorption of heavy metal ions was performed using 0.1 M HNO3. The p(HEMA-co-MAPA) membranes are suitable for more than five cycles without noticeable loss of capacity.Öğe Poly(hydroxyethyl methacrylate-co-methacrylamidoalanine) membranes and their utilization as metal-chelate affinity adsorbents for lysozyme adsorption(Vsp Bv, 2002) Garipcan, B.; Say, R.; Patir, S.; Arica, Y.; Denizli, A.Different adsorbents have been reported in the literature for protein purification. The authors have developed a novel and new approach to obtain high protein adsorption capacity utilizing a 2-methacrylamidoalanine-containing membrane. Amino acid ligand 2-methacrylamidoalanine (MAAL) monomer was synthesized using methacryloyl chloride and alanine. Poly(2-hydroxyethylmethacrylate-co-2-methacrylamidoalanine) [p(HEMA-co-MAAL)] membranes were then prepared by UV-initiated photopolymerization of HEMA and MAAL in the presence of an initiator (azobisisobutyronitrile, AIBN). The synthesized MAAL monomer was characterized by NMR. p(HEMA-co-MAAL) membranes were characterized by swelling studies, porosimeter, SEM, FTIR, and elemental analysis. These membranes have macropores in the size range of 5-10 mum. Cu(II) ions (25.9 mmol/m(2)) were chelated on these membranes. p(HEMA-co-MAAL) membranes were used to study the adsorption of lysozyme from aqueous media containing different amounts of lysozyme (0.1-3.0 mg/l) and at different pH values (4.0-8.0). The non-specific adsorption of lysozyme on the pHEMA membranes was negligible (0.9 mug/cm(2)). Incorporation of MAAL increased the lysozyme adsorption significantly up to 2.96 mg/cm(2). The lysozyme adsorption capacity of the Cu(II) incorporated membranes (9.98 mg/cm(2)) was greater than that of the p(HEMA-co-MAAL) membranes. More than 90% of the adsorbed lysozyme was desorbed in I h in the desorption medium containing 1.0 M NaCl and 0.025 M EDTA. The metal-chelate affinity membranes are suitable for repeated use for more than ten cycles without a noticeable loss of capacity.
