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<p>The alkaline protease produced by <i>Bacillus cereus</i> FT 11 was partially purified by ammonium sulphate precipitation and immobilised in 3.5% alginate beads. The characterisation studies of immobilised enzyme showed that it has maximum activity at a temperature of 65 °C (450 U/ml), pH of 10.5 (295 U/ml) and protein substrate (casein) concentration of 3.5% (305 U/ml). The Vmax of immobilised enzyme was found to be 303 U/ml and Km value, 2.51&#xa0;mg/ml, which indicates a high affinity of enzyme towards its substrate. The immobilized enzyme also showed stability at wide ranges of temperatures from 5 °C to 65 °C with 96% residual activity and wide ranges of pH from 8.0 to 10.5 with 95% residual activity. The enzyme was further purified by ion exchange chromatography method with DEAE cellulose as the matrix and the activity was analysed through zymogram with gelatine. The specific activity of purified enzyme was calculated to be 421 U/mg.</p>

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Immobilisation, characterisation and zymogram analysis of alkaline protease produced by Bacillus cereus FT11

  • 期刊论文

  • 发表日期：

    2025年1月31日

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  • B. Asha,
  • N. K. Shainy,
  • M. Palaniswamy

摘要

The alkaline protease produced by Bacillus cereus FT 11 was partially purified by ammonium sulphate precipitation and immobilised in 3.5% alginate beads. The characterisation studies of immobilised enzyme showed that it has maximum activity at a temperature of 65 °C (450 U/ml), pH of 10.5 (295 U/ml) and protein substrate (casein) concentration of 3.5% (305 U/ml). The Vmax of immobilised enzyme was found to be 303 U/ml and Km value, 2.51 mg/ml, which indicates a high affinity of enzyme towards its substrate. The immobilized enzyme also showed stability at wide ranges of temperatures from 5 °C to 65 °C with 96% residual activity and wide ranges of pH from 8.0 to 10.5 with 95% residual activity. The enzyme was further purified by ion exchange chromatography method with DEAE cellulose as the matrix and the activity was analysed through zymogram with gelatine. The specific activity of purified enzyme was calculated to be 421 U/mg.