Characterization of a thermostable protease from Bacillus subtilis BSP strain
2024
Tanveer Majeed | Charles C. Lee | William J. Orts | Romana Tabassum | Tawaf Ali Shah | Yousef A. Bin Jardan | Turki M. Dawoud | Mohammed Bourhia
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 confirmed to be a metalloprotease. The protease was also resistant to various organic solvents (benzene, ethanol, methanol), surfactants (Triton X-100), sodium dodecyl sulfate (SDS), Tween 20, Tween-80 and oxidants hydrogen per oxide (H2O2). Characteristics, such as tolerance to high SDS and H2O2 concentrations, indicate that this protease has potential applications in the pharmaceutical and detergent industries.
Afficher plus [+] Moins [-]Informations bibliographiques
Cette notice bibliographique a été fournie par Directory of Open Access Journals
Découvrez la collection de ce fournisseur de données dans AGRIS
