1Department of Chemistry, Biotechnology and Bioprocess Engineering, Federal University of São João Del Rei, Ouro Branco, MG 36420-000, Brazil. 2Department of Veterinary, Federal University of Viçosa, Viçosa, MG 36570-000, Brazil. 3Department of Bioprocess and Biotechnology, São Paulo State University, Araraquara, SP, 14801-902, Brazil. 4Department of Food Technology, Federal University of Viçosa, Viçosa, MG 36570-000, Brazil. 5Department of Animal Science, Federal University of Bahia, Salvador, BA 40110-909, Brazil. 6Institute of Agricultural Sciences, Federal University of Minas Gerais, Montes Claros, MG 39400-401, Brazil. Electronic address: email@example.com.
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.