Concanavalin A (Con A) immobilized monosize and magnetic poly(glycidyl methacrylate)[m-poly(GMA)] beads were investigated for specific adsorption of yeast invertase from aqueous solutions. m-Poly(GMA) beads (1.6 m in diameter) were prepared by dispersion polymerization in the presence of Fe3O4 nanopowder. The epoxy groups of m-poly(GMA) beads were opened by base catalyses. Then, Con A was immobilized by covalent binding onto the beads. Con A immobilization amount was 12.5 mg/g. The invertase adsorption capacity of the m-poly(GMA)/Con A beads was 111 mg/g. The maximum invertase adsorption on the m-poly(GMA)/Con A beads was observed at pH 5.5. The optimum activity for both free and adsorbed invertase was observed at 50C. Vmax values were determined as 330 U/mg and 292 U/mg enzyme, for free and adsorbed invertase, respectively. KM values were found to be the same for free and adsorbed invertase (20 mM). Adsorption of invertase via Con A improved the pH stability of invertase. Thermal stability also increased with adsorption. The adsorbed enzyme activity was found to be quite stable in repeated experiments.