| Abstract: | The purified α-amylase from Bacillus licheniformis M27, produced under solid state fermentation technique, showed novel characteristics as compared to those reported by other workers for the purified α-amylases from B. licheniformis obtained by submerged fermentation process. Some of the novel features of the characteristics of the enzyme from B. licheniformis M27 include two peaks for pH optima at 6.5–7.0 and 8.5–9.0, gradual loss of activity to about 86% between pH 7.0–7.5 followed by rise to full activity between 7.5–8.5, temperature optimum at 85–90°C at pH 7.0 and 9.0, sharp fall in stability at acidic pH values and the thermostability response which is more similar to the enzyme from other species of Bacillus. The moleculuar weight of the enzyme was found to be 19,500 ± 500 and 56,000 ± 2,000 when determined by gel filtration and SDS PAGE, respectively. The activation energy is 20.4 times lower than that reported for the enzyme from another strain of B. licheniformis. It also showed differences in the contents of amino acids such as serine, proline and methionine. |
