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Purification and characterization of a thermostable alpha-amylase from Bacillus stearothermophilus
K Chakraborty1, B K Bhattacharyya, S K Sen
1Microbiology Laboratory, Department of Botany, School of Life Sciences, Visva-Bharati, Santiniketan 731 235, India.
Abstract:
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.