Purification and characterization of uricase enzyme produced fromPseudomonas aeruginosa 7
karbala journal of pharmaceutical sciences,
Volume 3, Issue 3, Pages 64-76
Abstracturicase enzyme was partially purified from culture filtrate of P. aeruginosa 7 by two steps :
Precipitation with ammonium sulfate 70 % saturation and ion exchange chromatography on DEAE – Cellulose . uricase was purified by 7.2 fold with yield 43.79 % .
Uricase showed optimum pH (8.5 – 9) and pH stability was in the range of (8 – 9.5) . the temperature optimum of uricase enzyme was 35 Co .and the thermostable for uricase enzyme to observe that the enzyme was retain reserved by perfect activity at (25 – 40) Co and for 20 min.
The kinetic of uricase enzyme that representation by Km and Vmax was investigation and to be whole estimation by followed by three method , the rang value of Km was reached to 0.0091 mg / ml . However the Vmax was reached to 6.68 µM / ml . min. , by using the uric acid as a substrate.
The effective of some metal ion was studied and the result showed that the NiCl , AgCl2 and HgClare inhibiters , inaddition to that using 1 mM from FeCl2 cause to lose 88.93 % from enzyme activity. Whereas NaCl enhance the enzyme activity that reached to 216.448 % at 1 mMconcentration , Mgcl2 ,CaCl2 were consider enhancer to the enzyme activity at concentration of 5mM and the residue activity was reached to(170.35 and129.62)% respectively .
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