期刊
JOURNAL OF CHROMATOGRAPHY A
卷 1312, 期 -, 页码 1-9出版社
ELSEVIER
DOI: 10.1016/j.chroma.2013.08.042
关键词
Analytical biochemistry; Immobilized metal ion affinity; chromatography; Lactoferrin; Adsorption; Microcalorimetry
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.
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