Characterization of a thermostable protease from Bacillus subtilis BSP strain.

ABSTRACT: This study used conservative one variable-at-a-time study and statistical surface response methods to increase the yields of an extracellular thermostable protease secreted by a newly identified thermophilic Bacillus subtilis BSP strain. Using conventional optimization techniques, physical parameters in submerged fermentation were adjusted at the shake flask level to reach 184 U/mL. These physicochemical parameters were further optimized by statistical surface response methodology using Box Behnken design, and the protease yield increased to 295 U/mL. The protease was purified and characterized biochemically. Both Ca²⁺ and Fe²⁺ increased the activity of the 36 kDa protease enzyme. Based on its strong inhibition by ethylenediaminetetracetate (EDTA), the enzyme was conf

SUBMITTER: Majeed T 

PROVIDER: S-EPMC11247832 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature