, Volume 45, Issue 3, pp 207-210

Purification and characterization of a thermostable α-amylase fromBacillus stearothermophilus

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A soil isolate ofBacillus stearothermophilus was found to synthesize thermostable α-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 °C with more than 90% catalytic activity: the maximum activity was observed at 50 °C. Divalent metal ions exhibited inhibitory effect on the enzyme activity. However, proteinase inhibitor did not react positively.