| Autor: |
Tanveer Majeed, Charles C. Lee, William J. Orts, Romana Tabassum, Tawaf Ali Shah, Yousef A. Bin Jardan, Turki M. Dawoud, Mohammed Bourhia |
| Jazyk: |
angličtina |
| Rok vydání: |
2024 |
| Předmět: |
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| Zdroj: |
BMC Biotechnology, Vol 24, Iss 1, Pp 1-12 (2024) |
| Druh dokumentu: |
article |
| ISSN: |
1472-6750 |
| DOI: |
10.1186/s12896-024-00870-5 |
| Popis: |
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. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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