{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["24(1)"],"submitter":["Majeed T"],"pubmed_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 Ca<sup>2+</sup> and Fe<sup>2+</sup> increased the activity of the 36 kDa protease enzyme. Based on its strong inhibition by ethylenediaminetetracetate (EDTA), the enzyme was conf"],"journal":["BMC biotechnology"],"pagination":["49"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11247832"],"repository":["biostudies-literature"],"pubmed_title":["Characterization of a thermostable protease from Bacillus subtilis BSP strain."],"pmcid":["PMC11247832"],"pubmed_authors":["Bourhia M","Jardan YAB","Shah TA","Majeed T","Dawoud TM","Lee CC","Tabassum R","Orts WJ"],"additional_accession":[]},"is_claimable":false,"name":"Characterization of a thermostable protease from Bacillus subtilis BSP strain.","description":"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 Ca<sup>2+</sup> and Fe<sup>2+</sup> increased the activity of the 36 kDa protease enzyme. Based on its strong inhibition by ethylenediaminetetracetate (EDTA), the enzyme was conf","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-06-01T19:33:32.269Z","creation":"2025-04-06T11:29:49.053Z"},"accession":"S-EPMC11247832","cross_references":{"pubmed":["39010004"],"doi":["10.1186/s12896-024-00870-5"]}}