INVESTIGADORES
WOLMAN Federico Javier
artículos
Título:
Improved hollow-fibre membranes for dye-affinity
Autor/es:
FEDERICO J. WOLMAN, EDUARDO E. SMOLKO, OSVALDO CASCONE, MARIANO GRASSELLI
Revista:
JOURNAL OF SEPARATION SCIENCE - (Online)
Editorial:
WILEY-VCH Verlag GmbH & Co.
Referencias:
Lugar: Weinheim; Año: 2005 vol. 28 p. 45 - 45
ISSN:
1615-9314
Resumen:
Hollow-fibre membranes with different degrees of surface hydrophilicity were obtained by grafting mixtures of glycidyl methacrylate (GMA) and dimethyl acrylamide (DMAA) in various proportions, and Cibacron Blue F3G-A was attached to them through ammonia or glucamine spacers. Membrane hydrophilicity increased with the amount of dimethyl acrylamide in the grafted polymer. As the hydrophilicity increased the permeability decreased from 352 mL/cm2 min MPa for membranes grafted with GMA with ammonia spacer to 12.7 mL/cm2 min MPa for membranes grafted with GMA/DMAA 1/3 with glucamine spacer. Membranes grafted with GMA/DMAA 1/3 with ammonia spacer showed the best performance for BSA and lysozyme adsorption: maximum capacity was 15.3 l 2.2 mg BSA/mL membrane and 58.3 l 6.6 mg lysozyme/mL membrane while dissociation constants were 0.27 l 0.16 and 0.13 l 0.12 mg/mL, respectively. Over 80% of adsorbed proteins could be eluted with 2 M NaCl + 20% isopropanol in 20 mM sodium phosphate buffer, pH 7.0.2 min MPa for membranes grafted with GMA with ammonia spacer to 12.7 mL/cm2 min MPa for membranes grafted with GMA/DMAA 1/3 with glucamine spacer. Membranes grafted with GMA/DMAA 1/3 with ammonia spacer showed the best performance for BSA and lysozyme adsorption: maximum capacity was 15.3 l 2.2 mg BSA/mL membrane and 58.3 l 6.6 mg lysozyme/mL membrane while dissociation constants were 0.27 l 0.16 and 0.13 l 0.12 mg/mL, respectively. Over 80% of adsorbed proteins could be eluted with 2 M NaCl + 20% isopropanol in 20 mM sodium phosphate buffer, pH 7.0.2 min MPa for membranes grafted with GMA/DMAA 1/3 with glucamine spacer. Membranes grafted with GMA/DMAA 1/3 with ammonia spacer showed the best performance for BSA and lysozyme adsorption: maximum capacity was 15.3 l 2.2 mg BSA/mL membrane and 58.3 l 6.6 mg lysozyme/mL membrane while dissociation constants were 0.27 l 0.16 and 0.13 l 0.12 mg/mL, respectively. Over 80% of adsorbed proteins could be eluted with 2 M NaCl + 20% isopropanol in 20 mM sodium phosphate buffer, pH 7.0.l 2.2 mg BSA/mL membrane and 58.3 l 6.6 mg lysozyme/mL membrane while dissociation constants were 0.27 l 0.16 and 0.13 l 0.12 mg/mL, respectively. Over 80% of adsorbed proteins could be eluted with 2 M NaCl + 20% isopropanol in 20 mM sodium phosphate buffer, pH 7.0.l 0.16 and 0.13 l 0.12 mg/mL, respectively. Over 80% of adsorbed proteins could be eluted with 2 M NaCl + 20% isopropanol in 20 mM sodium phosphate buffer, pH 7.0.l 0.12 mg/mL, respectively. Over 80% of adsorbed proteins could be eluted with 2 M NaCl + 20% isopropanol in 20 mM sodium phosphate buffer, pH 7.0. Key Words: Hollow-fibre membranes; Dye ligands; Affinity chromatography;Hollow-fibre membranes; Dye ligands; Affinity chromatography;