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Updated: May 3, 2026

The Multifaceted Benefits of Protein Co-expression in Escherichia coli
Published on: February 5, 2015
Expression and characterization of Coprothermobacter proteolyticus alkaline serine protease
Tanveer Majeed1, Romana Tabassum1, William J Orts2
1National Institute for Biotechnology and Genetic Engineering (NIBGE), P.O. Box 577, Jhang Road, Faisalabad 38000, Pakistan ; Pakistan Institute of Engineering and Applied Science (PIEAS), Islamabad 44000, Pakistan.
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 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, the C. proteolyticus protease has potential applications in industries such as the detergent market.

