Partial purification and comparative characterization of alpha-amylase secreted by Lactobacillus amylovorus

An alpha-amylase (E.C. 3.2.1.1.) secreted by Lactobacillus amylovorus was partially purified and characterized. This high-molecular-weight enzyme [Imam SH, Burgess-Cassler A, Cote GL, Gordon SH, Baker FL (1991) Cuff Microbiol 22:365-370] was quantified with a clinical alpha-amylase assay adapted to...

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Bibliographic Details
Published in:Current microbiology 1991-10, Vol.23 (4), p.207-213
Main Authors: Burgess-Cassler, A, Imam, S
Format: Article
Language:English
Subjects:
alpha -amylase
Bacteriology
Biological and medical sciences
Biotechnology
characterization
denaturation
enzyme activity
Fundamental and applied biological sciences. Psychology
heat tolerance
Lactobacillus
Metabolism. Enzymes
Microbiology
molecular weight
physicochemical properties
protein secretion
purification
renaturation
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Summary:An alpha-amylase (E.C. 3.2.1.1.) secreted by Lactobacillus amylovorus was partially purified and characterized. This high-molecular-weight enzyme [Imam SH, Burgess-Cassler A, Cote GL, Gordon SH, Baker FL (1991) Cuff Microbiol 22:365-370] was quantified with a clinical alpha-amylase assay adapted to a microplate format. It was isolated from concentrated cell-free culture medium by ammonium sulfate precipitation, ion exchange, and hydrophobic interaction chromatographies. The enzyme was not particularly thermostable, but like three other microbial alpha-amylases tested for comparison, was renaturable following treatment with SDS and heat. The pH optimum and pI were 5.5 +/- 0.5 and 5.0, respectively; its temperature optimum was 60-65 degrees C, and the molecular weight on SDS gels was 140 +/- 10 kDa.
ISSN:0343-8651
1432-0991
DOI:10.1007/BF02092280