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Purification and properties of the raw starch-degrading α- amylase of Bacillus sp. IMD 434

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Abstract

The raw starch-degrading a-amylase of Bacillus sp. IMD 434 was purified to homogeneity by acetone precipitation, ion- exchange chromatography and hydrophobic interaction chromatography. The enzyme had a relative molecular mass of 69,200, displayed maximum activity at pH 6.0 and 65 °C and released large amounts of glucose and maltose on hydrolysis of starch.

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Authors and Affiliations

  1. Department of Industrial Microbiology, National University of Ireland, Dublin, Belfield, Dublin 4, Ireland

    Lynn M. Hamilton, Catherine T. Kelly & William M. Fogarty

Authors
  1. Lynn M. Hamilton
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  2. Catherine T. Kelly
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  3. William M. Fogarty
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Hamilton, L.M., Kelly, C.T. & Fogarty, W.M. Purification and properties of the raw starch-degrading α- amylase of Bacillus sp. IMD 434. Biotechnology Letters 21, 111–115 (1999). https://doi.org/10.1023/A:1005413816101

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  • DOI: https://doi.org/10.1023/A:1005413816101

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