alexa Interaction of Whey Lactoferrin with Copper Immobilized
ISSN: 2155-9821

Journal of Bioprocessing & Biotechniques
Open Access

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Research Article

Interaction of Whey Lactoferrin with Copper Immobilized in Polyacrylamide Cryogel

Carvalho BMA1*, Carvalho LM2, Silva Jr WF1, Minim LA3and Carvalho GGP4
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 Food Technology, Federal University of Viçosa, Viçosa, MG 36570-000, Brazil
4Department of Animal Science, Federal University of Bahia, Salvador, BA 40110-909, Brazil
Corresponding Author : Carvalho BMA
Department of Chemistry
Biotechnology and Bioprocess Engineering
Federal University of São João Del Rei
Ouro Branco, MG 36420-000, Brazil
Tel: +55-021- 31-374-139-62
E-mail: [email protected]
Received October 31, 2014; Accepted November 27, 2014; Published December 01, 2014
Citation: Carvalho BMA, Carvalho LM, Silva Jr WF, Minim LA, Carvalho GGP (2014) Interaction of Whey Lactoferrin with Copper Immobilized in Polyacrylamide Cryogel. J Bioprocess Biotech 4:189. doi: 10.4172/2155-9821.1000189
Copyright: © 2014 Carvalho BMA, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
 

Abstract

Design and optimization of Immobilized Metal Affinity Chromatography (IMAC) processes require deep knowledge of driving factors responsible for interaction between immobilized metal and biomolecules. Based on this requirement, interactions between lactoferrin from cheese whey and IDA-Cu2+-cryogel system was investigated. Data from adsorption of lactoferrin in the system at pH 6, 7 and 8, as well as NaCl concentration from 200 to 1000 mmol L−1 were adjusted Langmuir, Freundlich, Temkin and Langmuir-Freundlich isotherm models. Although all models were able to explain the interaction lactoferrin-cryogel system, the Langmuir-Freundlich model was the most accurate one. In addition, it could explain quantitatively the cooperativity and heterogeneity of the bounds between protein and matrix. The methods used in this project are useful for both better understanding of the protein-immobilized metal interactions and developing preparative scale IMAC.

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