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Affinity chromatography of α-amylase from Bacillus licheniformis by Damodara Rao Mendu; B.V.V. Ratnam; A. Purnima; C. Ayyanna is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Affinity chromatography of α-amylase from Bacillus licheniformis about?

An affinity chromatographic method with a novel eluant from Bacillus licheniformis is described. ␣-amylase was bound to starch, starchcelite, starch-Sepharose columns and the bound ␣-amylase was rapidly eluted with 2% (w/v) white dextrin. The binding capacity of ␣-amylase to starch column is 380 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.

Who reads Affinity chromatography of α-amylase from Bacillus licheniformis?

Author

Damodara Rao Mendu; B.V.V. Ratnam; A. Purnima; C. Ayyanna

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0141-0229)

Published

2005

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)