Purification and characterization of alkaline protease from alkalophilic Bacillus sp.

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dc.contributor.authorMuderriszade A.
dc.contributor.authorEnsari N.Y.
dc.contributor.authorAguloglu S.
dc.contributor.authorOtludil B.
dc.date.accessioned2024-04-24T18:43:56Z
dc.date.available2024-04-24T18:43:56Z
dc.date.issued2001
dc.departmentDicle Üniversitesien_US
dc.description.abstractAlkaline protease was purified from Bacillus sp. isolated from soil. The pH optimum was 11.5 at 37°C. Calcium divalent cation was effective to stabilize the enzyme especially at higher temperatures. The proteolytic activity was inhibited by active site inhibitors of PMSF (Phenylmethylsulfonyl fluoride), and ions of Mg, Mn, Pb, Li, Zn, Ag, Hg. The enzyme was stable in the presence of some detergents, such as Triton-X-100, Tween-80, SDS (sodium dodecyl sulfate) and EDTA (ethylendiaminetetraacetic acid), pH 11.5 and 37°C for 30 min. The optimum pH was 11.5 at 37°C and the optimum temperature was 62°C at pH 11.5.en_US
dc.identifier.issn0555-1099
dc.identifier.issue6en_US
dc.identifier.scopus2-s2.0-0042831144
dc.identifier.scopusqualityN/A
dc.identifier.startpage677en_US
dc.identifier.urihttps://hdl.handle.net/11468/24475
dc.identifier.volume37en_US
dc.indekslendigikaynakScopus
dc.language.isoruen_US
dc.relation.ispartofPrikladnaya Biokhimiya i Mikrobiologiya
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.titlePurification and characterization of alkaline protease from alkalophilic Bacillus sp.en_US
dc.titlePurification and characterization of alkaline protease from alkalophilic Bacillus sp.
dc.typeArticleen_US

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