Adsorption and desorption behavior of Bovine Serum Albumin (BSA) on surface-modified magnetic nanoparticles covered with thermosensitive polymer (PNIPAM) was investigated as a function of temperature, pH, and ionic strength. Functionalization of surface-modified magnetic particles was performed by seed polymerization using N-isopropylacrylamide (PNIPAM) as the main monomer. Characterization of these particles was carried out using transmission electron micrography (TEM), and vibrating sample magnetometry (VSM). The adsorption results exhibited both pH and temperature sensitivity. The results showed that the temperature effect on adsorption/desorption behavior was mainly dependent on the properties of the particles' surface. The effect of pH was also investigated and it was observed that a smaller amount of protein was adsorbed at higher pH because of the electrostatic repulsive force between protein molecules and latex particles. The maximum amount of protein was adsorbed near the isoelectric point of BSA. Desorption results showed that more protein was desorbed when adsorption was done at lower temperatures and desorption efficiency was found to be higher than 80%.