The hydrophobic affinity ligand L-tryptophan immobilized magnetic poly(glycidyl methacrylate) [m-poly(GMA)] beads in monosize form (1.6μm in diameter) were used for the affinity depletion of human serum albumin [HSA]. The m-poly(GMA) beads were prepared by dispersion polymerization in the presence of Fe3O4 nano-powder. The epoxy groups of the m-poly(GMA) beads were converted into amino groups by using 1,6 diaminohexane (i.e., spacer arm). L-tryptophan was then covalently immobilized on spacer arm attached m-poly(GMA) beads. Elemental analysis of immobilised L-tryptophan for nitrogen was estimated as 42.5 μmol/g polymer. Adsorption studies were performed under different conditions in a batch system (i.e., medium pH, protein concentration and temperature). Maximum lysozyme adsorption amount of m-poly(GMA) and L-tryptophan immobilized m-poly(GMA) [m-poly(GMA)-L-tryptophan] beads were 1.78 and 172.9 mg/g, respectively. The applicability of two kinetic models including pseudo-first order and pseudo-second order model was estimated. It was also observed that after 5 adsorption–elution cycle, m-poly(GMA)-L-tryptophan beads can be used without significant loss in HSA adsorption capacity. The elution results demonstrated that the adsorption of HSA to the adsorbent was reversible.