Purification and Characterization of an Alkaline Protease from Bacillus Alcalophilus

摘要

The purification and characterization of an alkaline protease produced by Bacillus alcalophilus were investigated. The enzyme was purified in two steps: concentrating the crude enzyme using ammonium sulfate precipitation, followed by cation-exchange chromatography. The purified protease had a molecular mass of approximately 28 kDa, was highly active over an alkaline pH range of 10.0 to 11.0, and remained stable over a pH range of 7.0 to 12.0. The optimum temperature for the enzyme activity was found to be 40～60°C, while the thermotolerance of the enzyme was poor. Therefore, these characteristics of the protease indicate its potential for a wide range of commercial applications.