|MAJEED, TANVEER - National Institute Of Biotechnology And Genetic Engineering (NIBGE)|
|TABASSUM, ROMANA - National Institute Of Biotechnology And Genetic Engineering (NIBGE)|
|Orts, William - Bill|
Submitted to: The Scientific World
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 10/8/2013
Publication Date: 10/8/2013
Citation: Majeed, T., Tabassum, R., Orts, W.J., Lee, C.C. 2013. Expression and characterization of Coprothermobacter proteolyticus alkaline serine protease. The Scientific World. doi: 10.1155/2013/396156.
Interpretive Summary: INTERPRETIVE SUMMARY Proteases are hydrolytic enzymes that break down proteins into smaller fragments. These enzymes have wide industrial applications spanning detergents, food, leather, pharmaceuticals, and bioremediation. The detergent industry is the single largest consumer of proteases which are used to remove proteinaceous stains. These enzymes are required to function in the presence of diverse environmental conditions such as denaturants, metal ions, oxidants, surfactants, and elevated temperatures and pH. We report the first expression and characterization of a recombinant protease from Coprothermobacter proteolyticus, a thermophilic microorganism. The enzyme was demonstrated to function at alkaline pH at elevated temperatures. Thus, this protease has properties that make it a promising candidate for industrial usage.
Technical Abstract: TECHNICAL ABSTRACT A putative protease gene (aprE) from the thermophilic bacterium Coprothermobacter proteolyticus was cloned and expressed in Bacillus subtilis. The enzyme was determined to be a serine protease based on inhibition by PMSF. Biochemical characterization demonstrated 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, the C. proteolyticus protease has potential applications in industries such as the detergent market.