Abstract
Uricase from bovine kidney, purified to homogeneity level, had a molecular weight of 70 kDa. The apparent Km and Vmax values for uric acid hydrolysis were 0.125 mM and 102 IU mg-1 protein respectively. The activation energy requirement for uric acid hydrolysis by uricase and inactivation of enzyme were 11.6 and 14.5 kJ/M respectively. Both enthalpy (Δ H*) and entropy of activation (Δ S*) for uricase activity were lower than those reported for some thermostable enzymes.
Keywords: Bovine uricase, enthalpy, entropy, kinetics and thermodynamics, temperature inactivation
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