Use este identificador para citar ou linkar para este item: https://locus.ufv.br//handle/123456789/22401
Tipo: Artigo
Título: Hydrophobic interaction adsorption of whey proteins: effect of temperature and salt concentration and thermodynamic analysis
Autor(es): Minim, Luis A.
Bonomo, Renata C. F.
Coimbra, Jane S. R.
Fontan, Rafael C. I.
Silva, Luis H. Mendes da
Minim, Valéria P. R.
Abstract: The adsorptive behavior of bovine serum albumin (BSA) and β-lactoglobulin (β-lg) on hydrophobic adsorbent was studied at four temperatures and different salt concentrations. The Langmuir model was fitted by experimental equilibrium data showing that an increase in temperature and salt concentration results in an increase on the capacity factor of both proteins. A thermodynamic analysis coupled with isotherm measurements showed that salt concentration and temperature affected the enthalpic and entropic behavior of the adsorption process of both proteins, mainly to the β-lg. The fast variation in the Z value for temperature over than 303.1 K suggest a great conformational change occurring in the β-lg structure, which almost duplicated the maximum adsorption capacity of this protein.
Palavras-chave: Bovine serum albumin
β- Lactoglobulin
Thermodynamic parameters
Isotherm
Hydrophobic interaction
Editor: Journal of Chromatography B
Tipo de Acesso: Elsevier B.V.
URI: https://doi.org/10.1016/j.jchromb.2006.06.021
http://www.locus.ufv.br/handle/123456789/22401
Data do documento: 21-Nov-2006
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