Purification of α-amylase from Bacillus licheniformis by chromatofocusing and gel filtration chromatography

M. Damodara Rao, A. Purnima, D. V. Ramesh, C. Ayyanna

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

A combination of chromatofocusing and gel filtration chromatography resulted in a simple purification of α-amylase from Bacillus licheniformis. The purification was approximately 77-fold. Identification of the purity was established by SDS-PAGE. Molecular weight and isoelectric point of the purified enzyme were 58 kDa and 7.18 respectively. Western blot analysis confirms the specificity of antibody raised against purified α-amylase.

Original languageEnglish (US)
Pages (from-to)547-550
Number of pages4
JournalWorld Journal of Microbiology and Biotechnology
Volume18
Issue number6
DOIs
StatePublished - 2002
Externally publishedYes

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Amylases
Gel Chromatography
Antibody Specificity
Isoelectric Point
Polyacrylamide Gel Electrophoresis
Molecular Weight
Western Blotting
Enzymes
Bacillus licheniformis

Keywords

  • α-Amylase
  • Chromatofocusing
  • Gel filtration chromatography

ASJC Scopus subject areas

  • Biotechnology
  • Physiology
  • Applied Microbiology and Biotechnology

Cite this

Purification of α-amylase from Bacillus licheniformis by chromatofocusing and gel filtration chromatography. / Damodara Rao, M.; Purnima, A.; Ramesh, D. V.; Ayyanna, C.

In: World Journal of Microbiology and Biotechnology, Vol. 18, No. 6, 2002, p. 547-550.

Research output: Contribution to journalArticle

Damodara Rao, M. ; Purnima, A. ; Ramesh, D. V. ; Ayyanna, C. / Purification of α-amylase from Bacillus licheniformis by chromatofocusing and gel filtration chromatography. In: World Journal of Microbiology and Biotechnology. 2002 ; Vol. 18, No. 6. pp. 547-550.
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