Purification and characterization of an extracellular alkaline protease produced from an isolated bacillus subtilis.
Loading...
Date
2013-04
Authors
Journal Title
Journal ISSN
Volume Title
Publisher
Abstract
This paper describes the studies on the purification and partial characterization of serine alkaline
protease produced through submerged fermentation process from a locally isolated Bacillus subtilis. This strain,
grown in a highly alkaline medium (pH 10), produces an extracellular proteolytic enzyme. The alkaline protease was
purified in a simple two-step procedure involving ammonium sulphate precipitation and gel filtration. Sodium
dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analysis of the purified alkaline protease indicated
an estimated molecular mass of 30KDa. It was more active in the range of 20-60ºC and had an optimum activity at
55ºC with optimum pH of 10.5. Characterization of the protease showed that it required certain cations such as Mg++,
Mn++ and Ca++ for maximal activity. The serine nature of the alkaline protease was confirmed by PMSF inhibition.
The temperature and pH stability of this Alkaline Protease from Bacillus Subtilismakes it potentially useful
forindustrial applications.
Description
Keywords
Bacillus subtilis, Alkaline protease, SmF, Purification, Characterization
Citation
Bundela Vijaya, Mandal S K. Purification and characterization of an extracellular alkaline protease produced from an isolated bacillus subtilis. International Journal of Applied Biology and Pharmaceutical Technology. 2013 Apr-June; 4(2): 112-120.