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

A combination of chromatofocusing and gel filtration chromatography resulted in a simple purification of alpha -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 pur...

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Bibliographic Details
Published in:World journal of microbiology & biotechnology 2002-08, Vol.18 (6), p.547-550
Main Authors: DAMODARA RAO, M, PURNIMA, A, RAMESH, D. V, AYYANNA, C
Format: Article
Language:English
Subjects:
Biological and medical sciences
Biotechnology
Enzyme engineering
Fundamental and applied biological sciences. Psychology
Improved methods for extraction and purification of enzymes
Methods. Procedures. Technologies
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Summary:A combination of chromatofocusing and gel filtration chromatography resulted in a simple purification of alpha -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 alpha -amylase.
ISSN:0959-3993
1573-0972
DOI:10.1023/A:1016374228444