Affinity chromatography of α-amylase from Bacillus licheniformis |
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| Authors: | Damodara Rao Mendu BVV Ratnam A Purnima C Ayyanna |
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| Institution: | aDepartment of Pediatrics, Division of Infectious Diseases, Johns Hopkins University School of Medicine, 720 Rutland Avenue, Ross 1135B, Baltimore, MD 21093, USA;bSan Diego Supercomputer Center, University of California San Diego, La Jolla, CA 92093-0537, USA;cCenter for Biotechnology, Department of Chemical Engineering, Andhra University, Visakhapatnam 530 003, India |
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| Abstract: | An affinity chromatographic method with a novel eluant from Bacillus licheniformis is described. α-amylase was bound to starch, starch-celite, starch-Sepharose columns and the bound α-amylase was rapidly eluted with 2% (w/v) white dextrin. The binding capacity of α-amylase to starch column is 380 μmol/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. |
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| Keywords: | α -Amylase Affinity chromatography Bacillus licheniformis Immunological characterization |
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