Purification and kinetics of uricase from fenugreek
Mohamed, H., Youssef, M., El-Moogy, R., El-Shora, H. (2023). Purification and kinetics of uricase from fenugreek. EKB Journal Management System, 62(4), 56-61. doi: 10.21608/mjcc.2023.411562
Howida E. Mohamed; Magdy M. Youssef; Rehab A. El-Moogy; Hamed M. El-Shora. "Purification and kinetics of uricase from fenugreek". EKB Journal Management System, 62, 4, 2023, 56-61. doi: 10.21608/mjcc.2023.411562
Mohamed, H., Youssef, M., El-Moogy, R., El-Shora, H. (2023). 'Purification and kinetics of uricase from fenugreek', EKB Journal Management System, 62(4), pp. 56-61. doi: 10.21608/mjcc.2023.411562
Mohamed, H., Youssef, M., El-Moogy, R., El-Shora, H. Purification and kinetics of uricase from fenugreek. EKB Journal Management System, 2023; 62(4): 56-61. doi: 10.21608/mjcc.2023.411562

Purification and kinetics of uricase from fenugreek

Mansoura Journal of Chemistry
Volume 62, Issue 4, August 2023, Page 56-61  XML PDF (1.32 MB)
Document Type: Original Article
DOI: 10.21608/mjcc.2023.411562
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Authors
Howida E. Mohamed* 1; Magdy M. Youssef1; Rehab A. El-Moogy1; Hamed M. El-Shora2
1Chemistry Department, Faculty of Science, Mansoura University, Mansoura, Egypt
2Botany Department, Faculty of Science, Mansoura University, Mansoura, Egypt
Abstract
Uricase (EC 1.7.3.3) is an enzyme involved in the purine breakdown pathway. The enzyme was isolated from fenugreek (Trigonella foenum-graecum) leaves and purified by 80% ammonium sulfate, DEAE-cellulose and Sephadex G-200. The final specific activity was 230.76 Umg-1 protein and the final yield of purification was 2.87 % with 133.38-fold. The optimal pH and the optimal temperature were 8.0 and 40°C. The enzyme was inactivated by the chelating agent as α-α-dipyridyl and the  IC50 value of α-α-dipyridyl was 9.03 mM.
Keywords
Uricase; Fenugreek (Trigonella foenum-graecum L.); Purification; Characterization
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