This study evaluated the adsorption process in agitated tanks with the proteins ovalbumin, conalbumin, and lysozyme by employing anion and cation exchange resins at different temperatures (5, 15, 25, and 35 °C). The equilibrium data showed that the different temperatures and adsorbents (cationic and anionic) preferentially influenced adsorption of the studied proteins. The employed isotherm model (Langmuir) adjusted well to the equilibrium data of these proteins. For the adsorption kinetics, two models were employed: pore diffusivity and a second-order kinetic model, in which the second presented the best fit to the experimental data. The calculated thermodynamic parameters indicated a spontaneous, viable, and endothermic process and also showed that entropy has a greater effect on the process than enthalpy. © 2011 Springer-Verlag.