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Article
Study of hydrophobic interaction adsorption of bovine serum albumin under overloaded conditions using flow microcalorimetry.
Journal of Chromatography A (1999)
  • Maria A. Esquibel-King
  • Ana Christina Dias-Cabral
  • Joao A. Quieroz
  • Neville G. Pinto, University of Louisville
Abstract
The adsorption behavior of bovine serum albumin (BSA) on a Sepharose based hydrophobic interaction support has been studied. Flow microcalorimetry has been used to determine the heat of adsorption under overloaded chromatographic conditions. These data have been complemented with capacity factor and isotherm measurements to provide insight on the mechanisms of adsorption. The heat of adsorption data have confirmed that the hydrophobic interaction adsorption of BSA under linear isotherm conditions is driven by entropy changes. Under overloaded (non-linear) conditions, however, it has been shown that the changes in enthalpy can drive adsorption; this behavior is not evident from analyses of capacity factor data. It is postulated that for BSA adsorption on the Sepharose derivative of interest, attractive force interactions between adsorbed protein molecules drive the adsorption process under overloaded conditions in a high (NH4)2SO4 environment. It is further postulated that these interactions are due to a change in confirmation of the adsorbed protein under these conditions.
Keywords
  • Hydrophobic interaction chromatography,
  • Flow microcalorimetry,
  • Thermodynamic parameters,
  • Albumin,
  • Proteins
Disciplines
Publication Date
December, 1999
DOI
10.1016/S0021-9673(99)01118-8
Citation Information
Maria A. Esquibel-King, Ana Christina Dias-Cabral, Joao A. Quieroz and Neville G. Pinto. "Study of hydrophobic interaction adsorption of bovine serum albumin under overloaded conditions using flow microcalorimetry." Journal of Chromatography A Vol. 865 Iss. 1-2 (1999) p. 111 - 122 ISSN: 0021-9673
Available at: http://works.bepress.com/neville-pinto/34/