Isolation, Partial Purification, Characterization and Inhibition of Urease (E.C. 3.5.1.5) Enzyme from the Cajanus cajan Seeds

Urease (urea amidohydrolase, E.C. 3.5.1.5), a nickel dependent metalloenzyme, catalyzes the hydrolysis of urea and one molecule of urea results in the release of two molecules of ammonia and one molecule of carbon dioxide. The objective of present study was to characterize urease enzyme from Cajanus cajan. The partial purification of urease enzyme was done by acetone fractionation method. The optimum temperature for urease enzyme in the present study was found to be 60°C and the optimum pH was 7.5. Partial purification of Cajanus cajan showed the fold purification to be 5.17 and the per cent recovery was found to be 56.6. Further, the effect of various inhibitors including CuSO₄, AgNO₃, SnCl₂ and HgCl₂ on the activity of urease enzyme was determined.