An affinity chromatographic method with a novel eluant from Bacillus licheniformis is described. alpha-amylase was bound to starch, starch-celite, starch-Sepharose columns and the bound alpha-amylase was rapidly eluted with 2% (w/v) white dextrin. The binding capacity of a-amylase to starch column is 380 mu mol/g of starch. The purified enzyme showed a single polypeptide on SDS-polyacrylamide gel electrophoresis with a molecular weight of 58 kD. The specificity of purified enzyme was confirmed by immunodiffusion, immunoelectrophoresis. Single radial immunodiffusion and western blotting studies analyzed the synthesis of enzyme at different time points. (c) 2005 Elsevier Inc. All rights reserved.