Designing an immobilised metal ion affinity process on large-scale demands that a thorough understanding be developed regarding the adsorption behaviour of proteins on metal-loaded gels and the characteristic adsorption parameters to be evaluated. In view of this requirement, interaction of alpha-amylase as a model protein with newly synthesised magnetic-poly(divinylbenzene-1-vinylimidazole) [m-poly(DVB-VIM)] microbeads (average diameter, 53-212 mu m) was investigated. The m-poly(DVB-VIM) microbeads were prepared by copolymerising of divinylbenzene (DVB) with 1-vinylimidazole (VIM). The m-poly(DVB-VIM) microbeads were characterised by N-2 adsorption/desorption isotherms, electron spin resonance, elemental analysis, scanning electron microscope and swelling studies. Cu2+ ions were chelated on the m-poly(DVB-VIM) beads and used in adsorption of alpha-amylase in a batch system. The maximum alpha-amylase adsorption capacity of the m-poly(DVB-VIM)-Cu2+ beads was determined as 10.84 mg/g at pH 6.0, 25 A degrees C. The adsorption data were analyzed using three isotherm models, which are the Langmuir, Freundlich and Dubinin-Radushkevich isotherm models. The pseudo-first-order, pseudo-second-order, modified Ritchie's-second-order and intraparticle diffusion models were used to test dynamic experimental data. The study of temperature effect was quantified by calculating various thermodynamic parameters such as Gibbs free energy, enthalpy and entropy changes.