Hydrophobic interaction adsorption of hen egg white proteins albumin, conalbumin, and lysozyme.
作者： Edwin E Garcia Rojas , Jane S dos Reis Coimbra , Luis A Minim , Sérgio H Saraiva , César A Sodré da Silva
DOI: 10.1016/J.JCHROMB.2006.04.033
关键词: Lysozyme 、 Mass transfer 、 Hydrophobic effect 、 Adsorption 、 Chemistry 、 Conalbumin 、 Albumin 、 Langmuir 、 Chromatography 、 Salt (chemistry)
摘要: Abstract Hydrophobic adsorption equilibrium data of the hen egg white proteins albumin, conalbumin, and lysozyme were obtained in batch systems, at 25 °C, using Streamline Phenyl ® resin as adsorbent. The influence three types salt, NaCl, Na 2 SO 4 , or (NH ) their concentration on evaluated. salt showed higher interaction with studied proteins, thus favoring by adsorbent, even though each type interacted a distinct manner protein. isotherm models Langmuir, Langmuir exponential, Chen Sun well fitted to data, no significant difference being observed 5% level significance. mass transfer model applied simulated correctly kinetics under conditions.
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