Adsorption kinetics of bovine serum albumin (BSA) to mixed-mode adsorbent with benzylamine ligand was studied via stirred-batch uptakeexperiments. The effects of liquid-phase conditions, such as salt concentration and pH, on the uptake rates of BSA were evaluated by effectivepore diffusivity (De) derived from the pore diffusion model (PDM). The results indicated that when electrostatic attractive interactions existbetween protein and ligand, De increases firstly with increasing salt concentration and then turns to decreasing after reaching the maximum.When there are electrostatic repulsion protein/ligand interactions, it seems that the adsorption process is patch controlled, and the specificsalt concentration to result in a minimum adsorption capacity could be found. The value of De showed a similar tendency to the change ofadsorption capacities. With the increase of salt concentration, the increase in De value was considered due to the decrease of electrostaticrepulsion interactions and increase of hydrophobic interactions between BSA and ligand. Since BSA has the most compact structure at theisoelectric point, which leads to lower hydrodynamic forces, it is reasonable that the maximum of effective diffusion coefficient could be foundaround the isoelectric point.