Production, purification, and characterization of metalloprotease from Candida kefyr 41 PSB

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dc.authoridYenidunya, Ali Fazil -- 0000-0002-9886-977Xen_US
dc.contributor.authorYavuz, Sevgi
dc.contributor.authorKocabay, Samet
dc.contributor.authorCetinkaya, Serap
dc.contributor.authorAkkaya, Birnur
dc.contributor.authorAkkaya, Recep
dc.contributor.authorYenidunya, Ali Fazil
dc.contributor.authorBakici, Mustafa Zahir
dc.date.accessioned2019-07-27T12:10:23Z
dc.date.accessioned2019-07-28T09:44:25Z
dc.date.available2019-07-27T12:10:23Z
dc.date.available2019-07-28T09:44:25Z
dc.date.issued2017
dc.department[Yavuz, Sevgi] Cumhuriyet Univ, Fac Engn, Dept Bioengn, TR-58140 Sivas, Turkey -- [Kocabay, Samet] Inonu Univ, Fac Sci, Dept Mol Biol & Genet, TR-44280 Malatya, Turkey -- [Cetinkaya, Serap -- Akkaya, Birnur -- Yenidunya, Ali Fazil] Cumhuriyet Univ, Fac Sci, Dept Mol Biol & Genet, TR-58140 Sivas, Turkey -- [Akkaya, Recep] Cumhuriyet Univ, Vocat Sch Hlth Serv, TR-58140 Sivas, Turkey -- [Bakici, Mustafa Zahir] Cumhuriyet Univ, Dept Microbiol, Fac Med, TR-58140 Sivas, Turkeyen_US
dc.description.abstractA thermostable metalloprotease, produced from an environmental strain of Candida kefyr 41 PSB, was purified 16 fold with a 60% yield by cold ethanol precipitation and affinity chromatography (bentoniteacrylamide-cysteine microcomposite). The purified enzyme appeared as a single protein band at 43 kDa. Its optimum pH and temperature points were found to be 7.0 and 105 degrees C, respectively. K-m and V-max values of the enzyme were determined to be 3.5 mg/mL and 4.4 mu mol mL(-1) min(-1), 1.65 mg/mL and 6.1 mu mol mL(-1) min(-1), using casein and gelatine as the substrates, respectively. The activity was inhibited by using ethylenediamine tetraacetic acid (EDTA), indicating that the enzyme was a metalloprotease. Stability of the enzyme was investigated by using thermodynamic and kinetic parameters. The thermal inactivation profile of the enzyme conformed to the first order kinetics. The half life of the enzyme at 95, 105, 115, 125 and 135 degrees C was 1310, 610, 220, 150, and 86 min, respectively. (C) 2016 Elsevier B.V. All rights reserved.en_US
dc.description.sponsorshipCumhuriyet University (CUBAP) [F-368]en_US
dc.description.sponsorshipThis work was supported by The Research Fund of Cumhuriyet University (CUBAP, Project no: F-368).en_US
dc.identifier.doi10.1016/j.ijbiomac.2016.10.006en_US
dc.identifier.endpage113en_US
dc.identifier.issn0141-8130
dc.identifier.issn1879-0003
dc.identifier.pmid27717786en_US
dc.identifier.scopus2-s2.0-84991010640en_US
dc.identifier.scopusqualityQ1
dc.identifier.startpage106en_US
dc.identifier.urihttps://dx.doi.org/10.1016/j.ijbiomac.2016.10.006
dc.identifier.urihttps://hdl.handle.net/20.500.12418/7058
dc.identifier.volume94en_US
dc.identifier.wosWOS:000390621900011en_US
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherELSEVIER SCIENCE BVen_US
dc.relation.ispartofINTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULESen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectCandida kefyren_US
dc.subjectco-Catalytic activeen_US
dc.subjectMetalloproteaseen_US
dc.subjectOrganic solvent stableen_US
dc.subjectThermostableen_US
dc.titleProduction, purification, and characterization of metalloprotease from Candida kefyr 41 PSBen_US
dc.typeArticleen_US

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