Cost effective characterization process and molecular dynamic simulation of detergent compatible alkaline protease from Bacillus pumilus strain MP27

摘要

A psychrothermotolerant alkaline protease isolated from Bacillus pumilus MP27 with a molecular mass similar to 53 kDa was isolated from Southern ocean water samples. It was partially purified by single step TPP with purity fold of 16.65. The enzyme was found to be widely stable within a range of temperature and pH, maintaining 52.25% of its activity at 50 degrees C and 92% at pH 12. The enzyme exhibited an exceptional activity along with tested detergents, showing 98% stability with SDS (10 mg/ml) and- 99% stability with Tide detergent (7 mg/ml). Further, the alkaline protease gene of 1152 bp was successfully cloned in pGEM-T Easy vector in E. coli DH5 alpha. The gene sequence was further translated, modeled and molecular dynamic simulation was performed. The modeled protein was highly unstable during the first 5 ns and therefore could not able to form bonds with the ligand after 1 ns of simulation.