Isolation, purification, characterization and applications of serine protease from Bacillus megaterium
Journal Title: Journal of Applied and Natural Science - Year 2010, Vol 2, Issue 2
Abstract
Bacillus megaterium isolated from poultry farm soil was identified by standard biochemical tests and screened for the production of serine protease. Production of serine protease was done using 5 different medias by varying the type of amino acid added. The purification was done by salt precipitation, dialysis and DEAE-cellulose ion exchange chromatography. The proline containing media obtained the highest fold purification out of the five different medias (leucine , lysine, proline, tryptophan and methionine cotaining media). The enzyme showed an optimal activity at the temperature 37°C and the pH 6 which are known as its optimum temperature and pH respectively. The enzyme was proved as a Mn2+ dependent serine protease as it was activated by Mn2+ ions and inhibited by PMSF. The molecular weight of the enzyme was determined by SDS-PAGE technique as around 30kDa. It showed an excellent detergent activity on the blood stains and a very good stability in presence of locally available detrgents. The enzyme acted on the keratin protein of the chicken feather and showed a degrading capa City on the protein. So it was proved that the recently studied serine protease has a keratinase activity also. From these datas I conclude that the protease isolated from Bacillus megaterium is a Mn 2+ dependent serine protease which has both keratinase and detergent activity.
Authors and Affiliations
T. Rajesh, Deepa , Divya , M. Mahesh, Somshekar
Keywords
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- EP ID EP152126
- DOI 10.31018/jans.v2i2.141
- Views 80
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