ORIGINAL ARTICLE |
Data source : Google Scholar QueryDate : 2016-12-24 Cites : 5 |
Enzyme activity is
influenced by a large number of factors. Environmental conditions such
as pH, temperature, salt concentration, substrate concentration,
activators, and inhibitors may change the three dimensional shape of an
enzyme, altering its rate of activity and/or its ability to bind
substrate. The effects of such environmental factors were evaluated.
The optimum pH and temperature of the purified urease were 7.2 and
48°C, respectively, using urea as substrate. The optimum substrate
(urea) concentration for urease was 25 mM. The enzyme showed the
highest activity when incubated for 30 min at 480C. EDTA, a metal
chelator, decreased the enzyme activity significantly. This may be due
to the removal of metal ions located on or near the active site.
Divalent cations like Ba2+ and Mg2+ slightly stimulated the enzyme at
a concentration of 1-3 mM whereas Na+ and K+ produced little or no
effect on the activity. Ca2+ enhanced urease activity by 120.47%, while Pb2+, Cu2+, Zn2+ and Hg2+ almost
completely inhibited the urease activity.