A highly inducible ?-galactosidase from enterobacter sp

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dc.authorid0000-0001-8253-9568en_US
dc.authorid0000-0002-5314-0475en_US
dc.contributor.authorShaikhan, Bestoon Ahmed
dc.contributor.authorGüven, Kemal
dc.contributor.authorBekler, Fatma Matpan
dc.contributor.authorAcer, Ömer
dc.contributor.authorGüven, Reyhan Gül
dc.date.accessioned2021-08-09T07:55:00Z
dc.date.available2021-08-09T07:55:00Z
dc.date.issued2020en_US
dc.departmentDicle Üniversitesi, Fen Bilimleri Enstitüsü, Biyoloji Ana Bilim Dalıen_US
dc.description.abstractEnterobacter sp. 3TP2A isolated from a petroleum station was found to produce a novel, highly inducible mesophilic intracellular β-galactosidase in the presence of lactose up to 76.5 U mg-1. The enzyme was purified to 17.3-fold after gel permeation chromatography with a yield of approximately 11 %. The optimum pH and temperature values of the purified enzyme were found to be 8.0-9.0 and 35 °C, respectively. The molecular weight of the enzyme was approx. 60 kDa with a single band by both SDS-PAGE and native-PAGE, and estimated by gel filtration chromatography. The enzyme was inhibited by Zn2+ and EDTA, while Cu2+ had strong inhibitory effect even at low concentrations. Activation by Mg2+ and inhibition by EDTA show that the enzyme is metal-dependent or a metalloenzyme. The enzyme was slightly activated by 2-mercaptoethanol, while slightly inhibited by iodoacetamide. On the other hand, PCMB inhibited the enzymatic activity to a great extent, whereas it was completely inhibited by N-ethylmaleimide. The Vmax and Km values were calculated as 0.701 μmol min-1 and 0.104 mM, respectively. The results indicated that the β-galactosidase Enterobacter sp. 3TP2A might well be a good candidate for use in biotechnology, particularly in the area of environment and health.en_US
dc.identifier.citationShaikhan, B. A., Güven, K., Bekler, F. M., Acer, Ö. ve Güven, R. G. (2020). A highly inducible β-galactosidase from enterobacter sp. Journal of the Serbian Chemical Society, 85(5), 609-622.en_US
dc.identifier.doi10.2298/JSC190711141S
dc.identifier.endpage622en_US
dc.identifier.issue5en_US
dc.identifier.scopus2-s2.0-85090678820
dc.identifier.scopusqualityQ3
dc.identifier.startpage609en_US
dc.identifier.urihttp://www.doiserbia.nb.rs/Article.aspx?ID=0352-51391900141S#.YQ0Ss4gzaUk
dc.identifier.urihttps://hdl.handle.net/11468/7269
dc.identifier.volume85en_US
dc.identifier.wosWOS:000535935100003
dc.identifier.wosqualityQ4
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.institutionauthorShaikhan, Bestoon Ahmed
dc.institutionauthorGüven, Kemal
dc.institutionauthorBekler, Fatma Matpan
dc.institutionauthorAcer, Ömer
dc.institutionauthorGüven, Reyhan Gül
dc.language.isoenen_US
dc.publisherSerbian Chemical Societyen_US
dc.relation.ispartofJournal of the Serbian Chemical Society
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectB-galactosidaseen_US
dc.subjectCharacterizationen_US
dc.subjectEnterobacteren_US
dc.subjectInhibitionen_US
dc.subjectPurificationen_US
dc.titleA highly inducible ?-galactosidase from enterobacter spen_US
dc.titleA highly inducible ?-galactosidase from enterobacter sp
dc.typeArticleen_US

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