Purification and characterization of a thermostable alpha-amylase from Bacillus stearothermophilus
Language English Country United States Media print
Document type Journal Article
PubMed
11271801
DOI
10.1007/bf02908945
Knihovny.cz E-resources
- MeSH
- alpha-Amylases chemistry isolation & purification metabolism MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Geobacillus stearothermophilus enzymology isolation & purification MeSH
- Hydrogen-Ion Concentration MeSH
- Soil Microbiology MeSH
- Temperature MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- alpha-Amylases MeSH
A soil isolate of Bacillus stearothermophilus was found to synthesize thermostable alpha-amylase. The enzyme was purified to homogeneity by ammonium sulfate fractionation and IECC on DEAE-cellulose column. The purified enzyme was considered to be a monomeric protein with a molar mass of 64 kDa, as determined by SDS-PAGE. The enzyme showed a wide range of pH tolerance and maximum activity at pH 7.0. The temperature tolerance was up to 100 degrees C with more than 90% catalytic activity; the maximum activity was observed at 50 degrees C. Divalent metal ions exhibited inhibitory effect on the enzyme activity. However, proteinase inhibitor did not react positively.
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