Purification and properties of heat stable α-amylase from Bacillus brevis

@article{Tsvetkov1989PurificationAP,
  title={Purification and properties of heat stable α-amylase from Bacillus brevis},
  author={Valeri T. Tsvetkov and Elka I. Emanuilova},
  journal={Applied Microbiology and Biotechnology},
  year={1989},
  volume={31},
  pages={246-248}
}
SummaryAn extracellular α-amylase has been isolated from a continuous culture of a thermophilic strain of Bacillus brevis. This enzyme was purified eightfold and obtained in electrophoretically homogenous form. The enzyme had a molecular weight of about 58000, a pH optimum from 5.0 to 9.0 and a temperature optimum at 80°C. The half-life of the purified enzyme in the presence of 5 mM CaCl2 at 90° C and pH 8.0 was 20 min. The Km value for soluble starch was calculated to be 0.8 mg/ml. 

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