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Thermodynamic aspects of the bovine serum albumin adsorption onto N , N ′‐ diethylaminoethyl dextran microbeads
Author(s) -
Can Hatice Kaplan,
Güner Ali
Publication year - 2005
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.21950
Subject(s) - adsorption , bovine serum albumin , enthalpy , gibbs free energy , dextran , chemistry , standard molar entropy , chromatography , thermodynamics , freundlich equation , serum albumin , albumin , standard enthalpy of formation , biochemistry , physics
Abstract Adsorption of proteins on solid surfaces is widely studied because of its importance in various biotechnological, medical, and technical applications, e.g., biosensor cardiovascular implants and chromatography. Adsorption thermodynamics has been studied on the microbeads of N , N ′‐diethylaminoethyl (DEAE) dextran anion exchanger for bovine serum albumin at 25, 30, 35 40, and 45°C. As a result some thermodynamic parameters like Freundlich constants, thermodynamic equilibrium constant ( K D ), standard free energy changes (Δ G assoc ), standard entropy changes (Δ S assoc ), and standard enthalpy change (Δ H assoc ) have been evaluated. Using the linear Van't Hoff plot, the Δ H assoc value of the system for the interaction of BSA adsorbed crosslinked DEAE dextran microbeads was determined as 12.5 kJ/mol. © 2005 Wiley Periodicals, Inc. J Appl Polym Sci, 2006