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S. Daneshjoo, E.s. Dashtban Moghadam, M.r. Jafari, S.m. Rezayat Sorkhabadi, Kh. Khajeh,
Volume 10, Issue 2 (Spring 2019)
Abstract
Some diseases such as gout, the formation of kidney stones, Lesch-Nyhan syndrome, Heart disease, diabetes type II and metabolic syndrome are caused due to the high concentration of uric acid. Within drugs, uricase significantly decreases the level of uric acid in plasma. The production, formulation and preservation proteins need special conditions so that there was no alteration in their structure and highest activity and response, at the same time the lowest immunogenicity can be achieved.In this study, uricase from Aspergillus flavus was cloned and expressed in Escherichia coli BL21. The protein was then purified using affinity chromatography. The enzyme activity and stability were compared with the common industrial Rasburicase. Results showed higher activity and stability at different temperatures (50, 37, 25, 4, and-20°C). Since uricase has an important role in the prevention and cure of mentioned diseases, therefore, the stable form of this enzyme could be a potential candidate for drug development.
