Investigating the Impact of Various Parameters On the Activity of Acid Phosphatases from Seedlings of Coronopus didymus

The thermal stability of purified acid phosphatase from the germinating seedlings of Coronopus didymus (Jangli halon) was investigated by studying the impact of various thermodynamic parameters [t_1/2, E_d, ΔH° (enthalpy change), ΔG° (free energy change), and ΔS° (entropy change)] of heat treatment in the temperature range of 55-75 °C. The thermal denaturation of acid phosphatase, assessed by loss in activity, was evidently followed by first-order kinetics, which varies with time and yield during the process of denaturation. The half-life of the enzyme was 693 min at 55 °C. The E_d (activation energy of denaturation) was calculated by the Arrhenius plot (30 kcal mol^-1), and the Z-value was 17.3 °C. The various thermodynamic parameters studied were as follows: ΔH°, the change in enthalpy of inactivation, was 121.93 kJ mol^-1 at 55 °C; ΔG°, the change in free energy of inactivation, was 110.65 kJ mol^-1 at 55 °C; and ΔS°, the change in entropy of inactivation, was 34.39 J mol^-1 k^-1 at 55 °C. This suggests that acid phosphatase activity is thermostable to long heat treatment up to 60 °C.

Keywords: Coronopus didymus; acid phosphatase; biocatalyst; inactivation; thermodynamic; thermostability.