Authors : S.B.Patharde and A.M.Chilke
Page Nos : 8-14
The aim of present study was to investigate the kinetic properties of acid phosphatase extracted from liver of Clarias gariepinus. The activity of acid phosphatase was determined biochemically by using p-Notrophenol as standard and p-nitrophenyl phosphate as substrate. The effect of pH, temperature, time and substrate concentration was studied by exposing the enzyme to the range of pH from 3.37 to 6.5, temperature ranging from 300C to 600C, time ranging from 10 to 80 min, and substrate ranging from 0.8 mM to 4.0 mM, however the range of enzyme concentration from 20 µl to 120 µl was used for studying the effect of enzyme concentration on reaction velocity. The enzyme was found to have maximum velocity at temperature 400C and pH 5.0, however its activity increased with increase in time and enzyme concentration. The increased in substrate concentration increases enzyme activity and found to stabilize at certain extent and it was considered to be Vmax. The Vmax and Km values were found to be 131.57 µg/g wt. and 8.64 mM of kidney from resulted graph.