Stability of enzymes is significant factor for their industrial feasibility. α–amylase is an important enzyme for some industries i.e., textile, food, paper and pharmaceutics.. Pumice particles (PPa) are non-toxic, natural, low-cost alternative adsorbents with high adsorption capacity. In this study, Cu2+ ions were attached onto pumice particles (Cu2+-APPa). Then, Cu2+-APPa embedded composite cryogel was synthesized (Cu2+-APPaC) via polymerization of gel-forming agents at minus temperatures. Characterization studies of the Cu2+-APPaC cryogel column was performed by X-ray fluorescence spectrometer (XRF), scanning electron microscopy (SEM), and Brunauer, Emmett, Teller (BET) apparatus. The experiments were carried out in a continuous column system. α–amylase was adsorbed onto Cu2+-APPaC cryogel with maximum amount of 858.7 mg/g particles at pH 4.0. Effects of pH and temperature on the activity profiles of the free and the immobilized α–amylase were investigated, and results indicate that immobilization did not alter the optimum pH and temperature values. kcat value of the immobilized α–amylase is higher than that of the free α–amylase while KM value increases by immobilization. Storage and operational stabilities of the free and the immobilized α–amylase were determined for 35 days and for 20 runs, respectively.