Purification and characterization of urease from leaves of Trigonella foenum-graecum | ||
| Mansoura Journal of Chemistry | ||
| Volume 62, Issue 4, August 2023, Pages 70-75 PDF (943.37 K) | ||
| Document Type: Original Article | ||
| DOI: 10.21608/mjcc.2023.412061 | ||
| Authors | ||
| Amany A. Ibrahim* 1; Abdel-Aziz F. Abdel-Aziz2; Rehab A. El-Mougy2; Hamed M. El-Shora3 | ||
| 11Chemistry Department, Faculty of Science, Mansoura University, Mansoura, Egypt. | ||
| 2Chemistry Department, Faculty of Science, Mansoura University, Mansoura, Egypt. | ||
| 3Botany Department, Faculty of Science, Mansoura University, Mansoura, Egypt. | ||
| Abstract | ||
| Urease is amidohydrolase enzyme (EC: 3.5.1.5) splits urea into carbon dioxide and ammonia. The enzyme was purified from fenugreek (Trigonella foenum-graecum) leaves using ammonium sulphate precipitation (80%), phenyl sepharose, hydroxyapatite and sephadex G-200. The specific activity of the purified urease from sephadex G-200 was 210 U per mg protein with 6.6 % yield. The final fold of purification was 677. The optimal pH of the purified urease was 8.0 whereas the optimal temperature was 40°C. The purified urease exhibited appreciable thermal stability at 60 °C particularly in presence of bovine serum albumin (BSA). Also, the enzyme exhibited appreciable storage stability at 25°C. | ||
| Keywords | ||
| Urease; Trigonella foenum; graecum; Specific activity; Storage stability; Purification | ||
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