Affinity chromatography of α-amylase from Bacillus licheniformis

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

Research output: Contribution to journalArticlepeer-review

27 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)712-717
Number of pages6
JournalEnzyme and Microbial Technology
Issue number7
StatePublished - Dec 1 2005
Externally publishedYes


  • Affinity chromatography
  • Bacillus licheniformis
  • Immunological characterization
  • α-Amylase

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology


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