The aim of this work was to evaluate the possibilities of immobilization of lactoperoxidase (LPO) on concanavalin A-Sepharose 4B support. Significant biospecific interaction of this heme-containing glycoenzyme with Con A was established by using \alpha-D-mannopyranoside and \alpha-D glucopyranoside, which are involved in the linking of the carbohydrate moieties of the enzyme with lectin. The preparation obtained indicated improved kinetic parameters (K_m and V_{\max}) compared with the soluble form. No significant differences were observed between the optimal pH and temperature of the anchored and free enzymes. The thermal stability of the biospecifically immobilized preparation was substantially higher than that of the unbound enzyme. In addition, seven cycles of enzymatic conversion and washing of the column showed the remarkable operational stability of immobilized LPO.