Production, Optimization and Partial Characterization of Alkaline Protease from Bacillus subtilis spp. subtilis NRRL B-3384 and B-3387

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dc.contributor.authorAkkale, Cengız
dc.date.accessioned2025-01-06T17:22:39Z
dc.date.available2025-01-06T17:22:39Z
dc.date.issued2023
dc.departmentAdana Alparslan Türkeş Bilim ve Teknoloji Üniversitesi
dc.description.abstractBacillus subtilis has been a reliable platform for the expression of extracellular proteases for several decades. Although a majority of Bacillus subtilis subspecies express proteases, the amount of secreted enzyme varies depending on the strain and environmental conditions used. Here, two Bacillus subtilis spp. subtilis strains, NRRL B-3384 and NRRL B-3387, from the ARS Culture collection (NRRL), were compared for secreted protease activity. The highest activity was found in strain NRRL B-3384, and proteolysis occurred at temperatures as high as 80°C and across a broad range of pH, with maximum activity at pH 9.0 and 60°C indicating the presence of a thermostable alkaline protease. To our knowledge, this is the first study to evaluate protease production in Bacillus subtilis spp. subtilis strains NRRL B-3384 and B3387 and suggests that NRRL B-3384 may have utility in the production of enzymes for industrial use.
dc.identifier.doi10.17350/HJSE19030000300
dc.identifier.endpage144
dc.identifier.issn2149-2123
dc.identifier.issn2148-4171
dc.identifier.issue2
dc.identifier.startpage135
dc.identifier.trdizinid1190580
dc.identifier.urihttps://doi.org/10.17350/HJSE19030000300
dc.identifier.urihttps://search.trdizin.gov.tr/tr/yayin/detay/1190580
dc.identifier.urihttps://hdl.handle.net/20.500.14669/434
dc.identifier.volume10
dc.indekslendigikaynakTR-Dizin
dc.language.isoen
dc.relation.ispartofHittite Journal of Science and Engineering
dc.relation.publicationcategoryMakale - Ulusal Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/openAccess
dc.snmzKA_20241211
dc.subjectBacillus subtilis
dc.subjectactivity
dc.subjectenzyme
dc.subjectprotease
dc.titleProduction, Optimization and Partial Characterization of Alkaline Protease from Bacillus subtilis spp. subtilis NRRL B-3384 and B-3387
dc.typeArticle

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