The bacterial strain Penibacillus sp was shown to produce extracellular a-amylases activity. The enzyme was purified to homogeneity with an overall recovery of 24 % and specific activity of 57.1 U/mg. The native protein showed a molecular mass of 160 kDa composed of a homodimmer of 82 kDa polypeptide by SDS-PAGE. The optimum pH and temperature of the amylase were 5.5 and 45ºC, respectively. The purified enzyme was stable from pH 7.5 to 9.0 and able to prolong its thermal stability up to 50ºC. The purified amylase shows interesting properties useful for industrial applications.
El-Shebawi, K. (2014). PURIFICATION OF -AMYLASE FROM PENIBACILLUS SP. Al-Azhar Journal of Pharmaceutical Sciences, 49(1), 269-276. doi: 10.21608/ajps.2014.6973
MLA
Khalid El-Shebawi. "PURIFICATION OF -AMYLASE FROM PENIBACILLUS SP", Al-Azhar Journal of Pharmaceutical Sciences, 49, 1, 2014, 269-276. doi: 10.21608/ajps.2014.6973
HARVARD
El-Shebawi, K. (2014). 'PURIFICATION OF -AMYLASE FROM PENIBACILLUS SP', Al-Azhar Journal of Pharmaceutical Sciences, 49(1), pp. 269-276. doi: 10.21608/ajps.2014.6973
VANCOUVER
El-Shebawi, K. PURIFICATION OF -AMYLASE FROM PENIBACILLUS SP. Al-Azhar Journal of Pharmaceutical Sciences, 2014; 49(1): 269-276. doi: 10.21608/ajps.2014.6973
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