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

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

doi:10.1023/A:1016374228444

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

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

Pathology

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13 Scopus citations

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 language	English (US)
Pages (from-to)	547-550
Number of pages	4
Journal	World Journal of Microbiology and Biotechnology
Volume	18
Issue number	6
DOIs	https://doi.org/10.1023/A:1016374228444
State	Published - Aug 23 2002

Keywords

Chromatofocusing
Gel filtration chromatography
α-Amylase

ASJC Scopus subject areas

Biotechnology
Physiology
Applied Microbiology and Biotechnology

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10.1023/A:1016374228444

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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.",

keywords = "Chromatofocusing, Gel filtration chromatography, α-Amylase",

author = "{Damodara Rao}, M. and A. Purnima and Ramesh, {D. V.} and C. Ayyanna",

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AU - Damodara Rao, M.

AU - Purnima, A.

AU - Ramesh, D. V.

AU - Ayyanna, C.

PY - 2002/8/23

Y1 - 2002/8/23

N2 - 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.

AB - 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.

KW - Chromatofocusing

KW - Gel filtration chromatography

KW - α-Amylase

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JF - Mircen Journal of Applied Microbiology and Biotechnology

IS - 6

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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