title: Hydrophobic interaction adsorption of hen egg white proteins albumin, conalbumin, and lysozyme.
abstract: Hydrophobic adsorption equilibrium data of the hen egg white proteins albumin, conalbumin, and lysozyme were obtained in batch systems, at 25 degrees C, using the Streamline Phenyl resin as adsorbent. The influence of three types of salt, NaCl, Na(2)SO(4), or (NH(4))(2)SO(4), and their concentration on the equilibrium data were evaluated. The salt Na(2)SO(4) showed the higher interaction with the studied proteins, thus favoring the adsorption of proteins by the adsorbent, even though each type of salt interacted in a distinct manner with each protein. The isotherm models of Langmuir, Langmuir exponential, and Chen and Sun were well fitted to the equilibrium data, with no significant difference being observed at the 5% level of significance. The mass transfer model applied simulated correctly adsorption kinetics of the proteins under the studied conditions.
authors.affiliation: Laboratório de Processos de Separação, LPS, Departamento de Tecnologia de Alimentos, Universidade Federal de Viçosa, UFV, 36571-000-Viçosa, MG, Brazil.
authors.forename: Edwin E Garcia
authors.initials: EE
authors.lastname: Rojas
authors.forename: Jane S
authors.initials: JS
authors.lastname: dos Reis Coimbra
authors.forename: Luis A
authors.initials: LA
authors.lastname: Minim
authors.forename: Sérgio H
authors.initials: SH
authors.lastname: Saraiva
authors.forename: César A Sodré
authors.initials: CA
authors.lastname: da Silva
mesh_terms: D000327:Adsorption; D000418:Albumins / Q000737:chemistry*; D003207:Conalbumin / Q000737:chemistry*; D007700:Kinetics; D009113:Muramidase / Q000737:chemistry*
chemical_list: D000418:Albumins; D003207:Conalbumin; D009113:Muramidase