scholarly journals Expression and Characterization ofCoprothermobacter proteolyticusAlkaline Serine Protease

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Tanveer Majeed ◽  
Romana Tabassum ◽  
William J. Orts ◽  
Charles C. Lee
Keyword(s):  
Bacillus Subtilis ◽  
Serine Protease ◽  
Biochemical Characterization ◽  
Thermophilic Bacterium ◽  
Protease Gene ◽  
Optimum Temperature ◽  
Optimal Activity ◽  
Potential Applications ◽  
Alkaline Conditions ◽  
Putative Protease

A putative protease gene (aprE) from the thermophilic bacteriumCoprothermobacter proteolyticuswas cloned and expressed inBacillus subtilis. The enzyme was determined to be a serine protease based on inhibition by PMSF. Biochemical characterization demonstrated that the enzyme had optimal activity under alkaline conditions (pH 8–10). In addition, the enzyme had an elevated optimum temperature (60°C). The protease was also stable in the presence of many surfactants and oxidant. Thus, theC. proteolyticusprotease has potential applications in industries such as the detergent market.

scholarly journals Isolation, purification, characterization and applications of serine protease from Bacillus megaterium

2010 ◽  
Vol 2 (2) ◽  
pp. 313-317 ◽  
Author(s):  
T. S. Rajesh ◽  
Deepa Deepa ◽  
Divya Divya ◽  
M. Mahesh ◽  
Somshekar Somshekar
Keyword(s):  
Serine Protease ◽  
Bacillus Megaterium ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Protease Production ◽  
Optimum Temperature ◽  
Salt Precipitation ◽  
Biochemical Tests ◽  
Optimal Activity ◽  
Sds Page

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 DEAEcellulose 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 showedan 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 capacity 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 Mn2+ dependent serine protease which has both keratinase and detergent activity.

scholarly journals Expression and activity-dependent changes of a novel limbic-serine protease gene in the hippocampus

1995 ◽  
Vol 15 (7) ◽  
pp. 5088-5097 ◽  
Author(s):  
ZL Chen ◽  
S Yoshida ◽  
K Kato ◽  
Y Momota ◽  
J Suzuki ◽  
...  
Keyword(s):  
Serine Protease ◽  
Protease Gene ◽  
Activity Dependent ◽  
Serine Protease Gene ◽  
Expression And Activity
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