Purification and characterization of a thermostable alpha-amylase from Bacillus stearothermophilus
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články
PubMed
11271801
DOI
10.1007/bf02908945
Knihovny.cz E-zdroje
- MeSH
- alfa-amylasy chemie izolace a purifikace metabolismus MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- Geobacillus stearothermophilus enzymologie izolace a purifikace MeSH
- koncentrace vodíkových iontů MeSH
- půdní mikrobiologie MeSH
- teplota MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- alfa-amylasy 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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