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

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Summary

An 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 K m value for soluble starch was calculated to be 0.8 mg/ml.

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Authors and Affiliations

  1. Institute of Microbiology, 1113, Sofia, Bulgaria

    Valeri T. Tsvetkov & Elka I. Emanuilova

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  1. Valeri T. Tsvetkov
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  2. Elka I. Emanuilova
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Tsvetkov, V.T., Emanuilova, E.I. Purification and properties of heat stable α-amylase from Bacillus brevis . Appl Microbiol Biotechnol 31, 246–248 (1989). https://doi.org/10.1007/BF00258403

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  • DOI: https://doi.org/10.1007/BF00258403

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