Microcalorimetric study of the adsorption of lactoferrin in supermacroporous continuous cryogel with immobilized Cu2+ ions

被引：17

作者：

Carvalho, B. M. A. ^{[1
]}

Da Silva, L. H. M. ^{[2
]}

Carvalho, L. M. ^{[3
]}

Soares, A. M. ^{[4
,5
]}

Minim, L. A. ^{[2
]}

Da Silva, S. L. ^{[1
]}

机构：

[1] Univ Fed Sao Joao del Rei, Chem Biotechnol & Bioproc Dept, BR-36420000 Ouro Branco, MG, Brazil

[2] Fed Univ Fed Vicosa, Dept Food Technol, BR-36270000 Vicosa, MG, Brazil

[3] Univ Fed Vicosa, BR-36270000 Vicosa, MG, Brazil

[4] Fundacao Oswald Cruz Fdn Fiocruz, Ctr Study Biomol Appl Hlth CEBio, BR-76812245 Porto Velho, RO, Brazil

[5] Fed Univ Rondonia, Dept Med, BR-76812245 Porto Velho, RO, Brazil

来源：

JOURNAL OF CHROMATOGRAPHY A | 2013年 / 1312卷

关键词：

Analytical biochemistry; Immobilized metal ion affinity; chromatography; Lactoferrin; Adsorption; Microcalorimetry; AFFINITY-CHROMATOGRAPHY; PH VALUE; LYSOZYME; BINDING; PURIFICATION; PROTEINS; SORPTION; IMAC;

D O I：

10.1016/j.chroma.2013.08.042

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The adsorption affinity of lactoferrin from whey in monolithic supermacroporous cryogel was analyzed using equilibrium data adsorptive isothermal titration microcalorimetry to measure thermodynamic information governing the process. Isotherm data was obtained at temperatures of 20, 30 and 40 degrees C, pH 6,7 and 8, and ionic strength of 200, 600 and 1000 mmol L-1 NaCl. The Langmuir model was fitted to equilibrium data. The binding was tighter at higher temperatures. The adsorption of protein was observed as spontaneous in all cases analyzed. The microcalorimetric study indicated that, in most cases examined, the adsorption of the protein in the matrix was entropy and enthalpy favored and entropy driven. Results provide data to enable the improvement of technical processes for the affinity separation of proteins. (C) 2013 Elsevier B.V. All rights reserved.

引用

页码：1 / 9

页数：9

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