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

• Published in: Journal of Chromatography A Vol. 1312; pp. 1 - 9
• Main Authors: Carvalho, B.M.A., Da Silva, L.H.M., Carvalho, L.M., Soares, A.M., Minim, L.A., Da Silva, S.L.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 01-10-2013; Elsevier
• Subjects: Adsorption; Affinity; Analytical biochemistry; Analytical, structural and metabolic biochemistry; Binding; Biological and medical sciences; chromatography; copper; enthalpy; Entropy; Fundamental and applied biological sciences. Psychology; Immobilized metal ion affinity chromatography; ionic strength; ions; Isotherms; Lactoferrin; Metalloproteins; Microcalorimetry; Other metalloproteins; Proteins; sodium chloride; sorption isotherms; temperature; Titration; Whey; Lactoferrin; Microcalorimetry; Adsorption; Analytical biochemistry; Immobilized metal ion affinity chromatography; Immobilized metal ion affinity; Ferroprotein; Adsorption energy; Adsorption isotherm; Immobilization; Immobilized metal affinity chromatography; Porous material; Protein; Affinity adsorbent; Separation method; Affinity chromatography; Acrylamide copolymer; chromatography; Thermal analysis; Isothermal titration calorimetry; Thermodynamic properties; Copper II Ions; Tridentate ligand; Macroporosity; Stationary phase
• ISSN: 0021-9673
• DOI: 10.1016/j.chroma.2013.08.042

•Lactoferrin was purified with high efficiency by the system cryogel-IDA-Cu2+.•The adsorption isotherms showed that the system is stable.•The entropy of the process was positive for all cases analyzed.•The process of adsorption and separation of lactoferrin was spontaneous.
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°C, pH 6, 7 and 8, and ionic strength of 200, 600 and 1000mmolL−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.