DILIP B. PATIL AND ANAND A. KSHIRSAGAR
Abstract
The inhibition of the glycinemax urease calatysed hydrolysis of urea by Benzoic acid, o-benzoic acid, p-benzoic acid and 2, 4 â Dichlorobenzoic acid has been carried out on the basis of kinetic measurement of urea hydrolysis. The concentration of urea was varied in the range of 0.40 x 10-2M to 2.50 x 10-2M and that of inhibitor was maintained 3.0 x 1QM. The Michaelis constant, Km, apperent Michaelis constant, Kmapp⢠and dissociation constant of enzyme â inhibitor complex, kâ were determined at pH 6.80 and temperature 37.0°C. All the Chlorobenzoic acids shows competitive type of inhibition.