Response of Fungal L-glutaminase to some Anhydrides and Chelating Agents | ||||
| Journal of Basic and Environmental Sciences | ||||
| Volume 11, Issue 4, October 2024, Page 307-314 PDF (1.2 MB) | ||||
| Document Type: Original Article | ||||
| DOI: 10.21608/jbes.2024.390984 | ||||
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| Authors | ||||
| Esraa A. Sobieh1; Mervat G. Hassan* 1; Mohamed O. Abdel-Monem1; Sabah A. Abo-ElMaaty1; Hamed M El-Shora2 | ||||
| 1Botany and Microbiology Department, Faculty of Science, Benha University | ||||
| 2Botany and Microbiology Department, Faculty of Science, Mansoura University | ||||
| Abstract | ||||
| Specific activity of L-glutaminase (E.C 3.5.1.2) was determined by isolating and partially purifying it from Penicillium chrysogenum using ammonium sulfate (85%). Upon addition of maleic anhydride (MA) and succinic anhydride (SA) to the reaction media at different concentrations (0.2, 0.4, 0.6, 0.8, and 1.0 mM), the enzyme was shown to be inhibited. The activity of the enzyme was reduced at a concentration of 10 mM by the four chelating agents ethylene glycol tetraacetate (EGTA), ethylenediaminetetraacetate (EDTA), phenannthroline, and dipyridyl, suggesting that the enzyme is a metalloenzyme. Metal cations such as CoCl2, CuCl2, FeCl3, and MgCl2 in the reaction media at a concentration of 10 mM shown to be inhibitory to the enzyme. Nevertheless, calcium chloride enhanced the enzyme activity at an equivalent concentration. | ||||
| Keywords | ||||
| L-glutaminase; Fungi; Anhydrides; Chelating agents; Metal Cations | ||||
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