Purification and kinetics of uricase from fenugreek | ||
Mansoura Journal of Chemistry | ||
Volume 62, Issue 4, August 2023, Pages 56-61 PDF (1.32 M) | ||
Document Type: Original Article | ||
DOI: 10.21608/mjcc.2023.411562 | ||
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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