Purification and some properties of uricase from aspergillus flavus S-79

ABSTRACT

The work in this paper is concerned with the purification and properties of uricase from local Aspergillus flavus, S-79 isolated from an Egyptian soil. Purification by gel-filtration through a series of Sephadex G 200-120 and G 200 columns was tested by agarose gel electrophoresis. A specific activity of 0.144 units/mg protein was obtained [288-fold increase]. The purified uricase was found most active at PH 9.2, in 0.1 m borate buffer and at 37 C. The activity of this uricase was completely inhibited by sulphate of Zn2+ [50 mu g/ml] but sulphates of Mg2+, Cu2+, Fe2+ and Co2+ were stimulatory at 50 mu g/ml. Cobalt sulphate was the best activator, at 50 mu g/ml. Cobalt sulphate was the best activator, at 50 mu g/ml but not at 100 mu g/ml. However, 10 mu g/ml was stimulatory than 50 mu g/ml