For years, crystallization has been used as a recovery technology for industrial enzymes. In this work, the crystallization of an alpha-amylase originating from Bacillus Licheniformis was investigated in accordance with the solubility data previously obtained for the material. In the experiments, the material was crystallized by the addition of seed crystals to amylase solutions that had been made supersaturated by ultrafiltration. The initial supersaturation of the solutions was kept below the metastable zone threshold so that crystal growth occurs with minimal nucleation. The growth rate of alpha-amylase has a second-order dependence upon the supersaturation at the conditions examined. These conditions covered solution temperature, pH and the addition of either ammonium sulfate or sodium sulfate as the inorganic precipitant. The kinetic and solubility data obtained are useful in predicting the operating time and the yield of an industrial crystallization process.