PURIFICATION OF -AMYLASE FROM PENIBACILLUS SP | ||||
| Al-Azhar Journal of Pharmaceutical Sciences | ||||
| Article 20, Volume 49, Issue 1 - Serial Number 49, March 2014, Page 269-276 PDF (498.38 K) | ||||
| Document Type: Original Article | ||||
| DOI: 10.21608/ajps.2014.6973 | ||||
 View on SCiNiTO | ||||
| Author | ||||
| Khalid El-Shebawi | ||||
| Department of Microbial Biotechnology, National Research Center, Dokki, Cairo, Egypt | ||||
| Abstract | ||||
| 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. | ||||
| Keywords | ||||
| amylase; Purification; Penibacillus sp | ||||
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