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Adsorption of immunoglobulin Y in supermacroporous continuous cryogel with immobilized Cu(2+) ions.

Posted by on in 2015
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Júnior WF1Cano R1Totola AH1Carvalho LM2Cerri MO3Coimbra JS4Carvalho GG5Carvalho BM6. 2015. J Chromatogr A. 1395:16-22. doi: 10.1016/j.chroma.2015.03.052. Epub 2015 Mar 27.

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: brunamara.carvalho@gmail.com.

Abstract

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.

Copyright © 2015 Elsevier B.V. All rights reserved.

KEYWORDS:

Adsorption isotherms; Cryogel; IMAC; Immunoglobulin Y; Thermodynamic parameters

PMID:
 
25857540
 
[PubMed - in process]
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