Rapid method for the affinity purification of thermostable α-amylase from Bacillus licheniformis

M. Damodara Rao, B. V.V. Ratnam, Dasari VenkataRamesh, C. Ayyanna

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


A rapid and efficient method the exploiting affinity of α-amylase for its substrate starch is described. α-amylase from Bacillus licheniformis was purified to homogeneity by ammonium sulphate precipitation and affinity chromatography with 230-fold purification. The α-amylase adsorption to various starches was examined in order to screen its ability for highest binding to starch. The α-amylase was bound to starch more tenaciously, hence various eluants like maltose, soluble starch and high salts could not elute the bound α-amylase. However, the bound α-amylase was instantly eluted using 2% (w/v) dextrin. The purified enzyme showed a single polypeptide on SDS-PAGE, with a molecular weight of 58 kD. Western blot analysis confirmed the specificity of antibody raised against purified α-amylase.

Original languageEnglish (US)
Pages (from-to)371-375
Number of pages5
JournalWorld Journal of Microbiology and Biotechnology
Issue number3
StatePublished - Apr 2005
Externally publishedYes


  • Affinity adsorption
  • Bacillus licheniformis
  • α-amylase

ASJC Scopus subject areas

  • Biotechnology
  • Physiology
  • Applied Microbiology and Biotechnology


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