Purification and characterization of urease from leaves of Trigonella foenum-graecum

Ibrahim, Amany A.; Abdel-Aziz, Abdel-Aziz  F.; El-Mougy, Rehab A.; El-Shora, Hamed M.

doi:10.21608/mjcc.2023.412061

Purification and characterization of urease from leaves of Trigonella foenum-graecum

Document Type : Original Article

Authors

¹ 1Chemistry Department, Faculty of Science, Mansoura University, Mansoura, Egypt.

² Chemistry Department, Faculty of Science, Mansoura University, Mansoura, Egypt.

³ Botany Department, Faculty of Science, Mansoura University, Mansoura, Egypt.

10.21608/mjcc.2023.412061

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 mgprotein 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.

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