Purification and characteristics of alkaline proteinase from alkalophylic Bacillus sp.

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dc.contributor.authorMuderrizade A.
dc.contributor.authorEnsari N.Y.
dc.contributor.authorAguloglu S.
dc.contributor.authorOtludil B.
dc.date.accessioned2024-04-24T17:58:45Z
dc.date.available2024-04-24T17:58:45Z
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 degrees 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 degrees C for 30 min. The optimum pH was 11.5 at 37 degrees C and the optimum temperature was 62 degrees C at pH 11.5.en_US
dc.identifier.endpage677en_US
dc.identifier.issn0555-1099
dc.identifier.issue6en_US
dc.identifier.pmid11771320en_US
dc.identifier.scopus2-s2.0-0035515015en_US
dc.identifier.scopusqualityN/Aen_US
dc.identifier.startpage674en_US
dc.identifier.urihttps://hdl.handle.net/11468/24085
dc.identifier.volume37en_US
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoruen_US
dc.relation.ispartofPrikladnaia biokhimiia i mikrobiologiiaen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.titlePurification and characteristics of alkaline proteinase from alkalophylic Bacillus sp.en_US
dc.title.alternativeOchistka i kharakteristika shchelochnoi proteinazy alkalofil'nogo shtamma Bacillus sp..en_US
dc.typeArticleen_US

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