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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, Cu 2+ ions were attached onto pumice particles (Cu 2+ -APPa). Then, Cu 2+ -APPa embedded composite cryogel was synthesized (Cu 2+ -APPaC) via polymerization of gelforming agents at minus temperatures. Characterization studies of the Cu 2+ -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 Cu 2+ -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 αamylase were determined for 35 days and for 20 runs, respectively.

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