Shaikhan, Bestoon AhmedGüven, KemalBekler, Fatma MatpanAcer, ÖmerGüven, Reyhan Gül2021-08-092021-08-092020Shaikhan, 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.http://www.doiserbia.nb.rs/Article.aspx?ID=0352-51391900141S#.YQ0Ss4gzaUkhttps://hdl.handle.net/11468/7269Enterobacter 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.eninfo:eu-repo/semantics/openAccessB-galactosidaseCharacterizationEnterobacterInhibitionPurificationArticle855609622WOS:0005359351000032-s2.0-8509067882010.2298/JSC190711141SQ3Q4