Thermodynamic and kinetic characteristics of an a-amylase from Bacillus licheniformis SKB4


  • Saptadip Samanta
  • Arpan Das
  • Suman Kumar Haider
  • Arijit Jana
  • Sanjay Kar
  • Pradeep Kumar Das Mohapatra
  • Bikash Ranjan Pad
  • Keshab Chandra Mondal


An amylolytic bacterial strain, Bacillus licheniformis SKB4 produced maximum amylase at pH 6.5 at 42 °C, and at late stationary phase (24 h) of growth. Starch and peptone were found the best supporting carbon and nitrogen source with C:N ratio of 1:2 for amylase production. The purified enzyme was non-responsive to most of the metal ions except K+ and Mg++ (1.0 mM). The enzyme was stable and active at pH 6.5. The enzyme showed optimum temperature at 90 °C with 10 min of half life (t½) at 100 °C. The Q10 of the enzyme was 1.0. The thermodynamic principles like activation energy, free energy for substrate binding and transition state of the enzyme were found 31.53, 5.53 and -17.4 KJ/Mol of starch, respectively. The kinetic constant like Vmax, Km, K catand catalytic efficiency (Kcat/Km)for starch were found to be 1.04 μmol mg-1 min-1, 6.2 mg ml-1,2 × 103 S-1 and 3.22 × 102 ml mg-1 S-1,respectively. All these findings suggested that this amylase has unique characteristics for starch hydrolysis in respect to thermostability and kinetic properties.


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How to Cite

Samanta, S., Das, A., Haider, S. K., Jana, A., Kar, S., Mohapatra, P. K. D., Pad, B. R. and Mondal, K. C. (2014) “Thermodynamic and kinetic characteristics of an a-amylase from Bacillus licheniformis SKB4”, Acta Biologica Szegediensis, 58(2), pp. 147–156. Available at: (Accessed: 20 May 2024).




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