β-Glucuronidase is a lysosomal enzyme. It plays an important role in carbohydrate metabolism. The renal β-glucuronidase at optimum pH-5 was observed to produce ∆G, -2.074 kcal/mole at 453 K. Reduction in ∆G was recorded above and below these pH optima. With the increase in temperature, the ∆G was decreased from -2.3 kcal/mole at 358 K to -10.2 kcal/mole at 834 K at constant pH-4.5. However, with the increase in enzyme and substrate concentration ∆G was seen to increase at constant temperature 435 K and pH-4.5 for 1 h incubation. For all the above experimental parameters, the equilibrium constant (Keq, 0.641) was kept constant. It was concluded that the enzyme is greatly affected by the pH and the temperature in the course of time. These factors might have distorted the physical structure of the enzyme and hence the efficiency to catalyze the reaction hampered and resulted in the decrease in ∆G. However, the increase in enzyme and substrate concentration favors the reaction by enhancing the subsequent increase in ∆G in the renal β-glucuronidase of Labeo rohita.
