Folia Microbiologica

, Volume 45, Issue 3, pp 207–210

Purification and characterization of a thermostable α-amylase fromBacillus stearothermophilus

  • K. Chakraborty
  • B. K. Bhattacharyya
  • S. K. Sen
Papers

DOI: 10.1007/BF02908945

Cite this article as:
Chakraborty, K., Bhattacharyya, B.K. & Sen, S.K. Folia Microbiol (2000) 45: 207. doi:10.1007/BF02908945

Abstract

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.

Copyright information

© Institute of Microbiology, Academy of Sciences of the Czech Republic 2000

Authors and Affiliations

  • K. Chakraborty
    • 1
  • B. K. Bhattacharyya
    • 1
  • S. K. Sen
    • 1
  1. 1.Microbiology Laboratory, Department of BotanySchool of Life SciencesSantiniketanIndia