Adsorption of immunoglobulin Y in supermacroporous continuous cryogel with immobilized Cu(2+) ions
Willer Ferreira da Silva Júnior1, Rodrigo Cano1, Antonio Helvécio Totola1
1Department of Chemistry, Biotechnology and Bioprocess Engineering, Federal University of São João Del Rei, Ouro Branco, MG 36420-000, Brazil.
The influence of temperature, pH and ionic strength on the adsorption of Immunoglobulin Y (IgY) in IDA-Cu(2+) cryogel system was studied by batch equilibrium measurements. The adsorptive equilibrium data were obtained at 17 and 27°C, pH 5.0 and 6.5, and at ionic strength of 50 and 200mmolL(-1) NaCl. Langmuir, Freundlich and Langmuir-Freundlich models were fitted to equilibrium data, while the enthalpy of adsorption of IgY in IDA-Cu(2+) cryogel system was calculated through Van't Hoff analysis. The binding of IgY on cryogel was stronger at 27°C and lowest pH and ionic strength values, with apparent maximum adsorption capacity of 27mgg(-1). The adsorption of protein in the resin was spontaneous in all analyzed cases. The results provide valuable information to enable the improvement of IgY purification processes.
The influence of temperature, pH and ionic strength on the adsorption of Immunoglobulin Y (IgY) in IDA-Cu(2+) cryogel system was studied by batch equilibrium measurements. The adsorptive equilibrium data were obtained at 17 and 27°C, pH 5.0 and 6.5, and at ionic strength of 50 and 200mmolL(-1) NaCl. Langmuir, Freundlich and Langmuir-Freundlich models were fitted to equilibrium data, while the enthalpy of adsorption of IgY in IDA-Cu(2+) cryogel system was calculated through Van't Hoff analysis. The binding of IgY on cryogel was stronger at 27°C and lowest pH and ionic strength values, with apparent maximum adsorption capacity of 27mgg(-1). The adsorption of protein in the resin was spontaneous in all analyzed cases. The results provide valuable information to enable the improvement of IgY purification processes.
