A highly inducible ?-galactosidase from enterobacter sp
dc.authorid | 0000-0001-8253-9568 | en_US |
dc.authorid | 0000-0002-5314-0475 | en_US |
dc.contributor.author | Shaikhan, Bestoon Ahmed | |
dc.contributor.author | Güven, Kemal | |
dc.contributor.author | Bekler, Fatma Matpan | |
dc.contributor.author | Acer, Ömer | |
dc.contributor.author | Güven, Reyhan Gül | |
dc.date.accessioned | 2021-08-09T07:55:00Z | |
dc.date.available | 2021-08-09T07:55:00Z | |
dc.date.issued | 2020 | en_US |
dc.department | Dicle Üniversitesi, Fen Bilimleri Enstitüsü, Biyoloji Ana Bilim Dalı | en_US |
dc.description.abstract | Enterobacter 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.citation | Shaikhan, 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.doi | 10.2298/JSC190711141S | |
dc.identifier.endpage | 622 | en_US |
dc.identifier.issue | 5 | en_US |
dc.identifier.scopus | 2-s2.0-85090678820 | |
dc.identifier.scopusquality | Q3 | |
dc.identifier.startpage | 609 | en_US |
dc.identifier.uri | http://www.doiserbia.nb.rs/Article.aspx?ID=0352-51391900141S#.YQ0Ss4gzaUk | |
dc.identifier.uri | https://hdl.handle.net/11468/7269 | |
dc.identifier.volume | 85 | en_US |
dc.identifier.wos | WOS:000535935100003 | |
dc.identifier.wosquality | Q4 | |
dc.indekslendigikaynak | Web of Science | |
dc.indekslendigikaynak | Scopus | |
dc.institutionauthor | Shaikhan, Bestoon Ahmed | |
dc.institutionauthor | Güven, Kemal | |
dc.institutionauthor | Bekler, Fatma Matpan | |
dc.institutionauthor | Acer, Ömer | |
dc.institutionauthor | Güven, Reyhan Gül | |
dc.language.iso | en | en_US |
dc.publisher | Serbian Chemical Society | en_US |
dc.relation.ispartof | Journal of the Serbian Chemical Society | |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.rights | info:eu-repo/semantics/openAccess | en_US |
dc.subject | B-galactosidase | en_US |
dc.subject | Characterization | en_US |
dc.subject | Enterobacter | en_US |
dc.subject | Inhibition | en_US |
dc.subject | Purification | en_US |
dc.title | A highly inducible ?-galactosidase from enterobacter sp | en_US |
dc.title | A highly inducible ?-galactosidase from enterobacter sp | |
dc.type | Article | en_US |
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