Purification and characterization of a thermostable alpha-amylase from Bacillus stearothermophilus.
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.
Chakraborty
K
K
Microbiology Laboratory, Department of Botany, School of Life Sciences, Visva-Bharati, Santiniketan 731 235, India.
Bhattacharyya
B K
BK
Sen
S K
SK
D004591:Electrophoresis, Polyacrylamide Gel; D001411:Geobacillus stearothermophilus / Q000201:enzymology* / Q000302:isolation & purification; D006863:Hydrogen-Ion Concentration; D012988:Soil Microbiology; D013696:Temperature; D000516:alpha-Amylases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism
D000516:alpha-Amylases