Abstract
Herein acid phosphatase isoenzyme was extracted from the C. murale seedlings. The purification was accomplished by chromatographic techniques and passing through DEAE-cellulose and Sephadex G-100 column. The specific activity of acid phosphatase 5.75 U/mg of protein was obtained with 66 purification fold 15.8% yield andmolecular masswas 29 kDawith very faint bands corresponding to 18 kDa and 14 kDa. The maximal activity at pH 5.0 and 50 degrees C best illustrated by first order kinetics. When temperature was raised (55 degrees C to 75 degrees C), the deactivation rate constant was increased from 0.001 to 0.014 min(-1), while half-life was decreased from 693 to 49 min(-1). The results of activity collected at different temperature were then used to estimate, activation energy of hydrolysis reaction (Ea= 47.59 kJmol(-1)). A high Z-value (18.86 degrees C min(-1)) was obtained indicating a less sensitivity towards temperatures. The residual activity examinations were carried out from 55 degrees C to 75 degrees C and assessing the Deactivation Energy (Ed 116.39 kJmol(-1)), Enthalpy change (Delta H degrees 113.55kJmol(-1)), Entropy change (.S degrees 110.33kJmol(-1)) and change in Gibbs free energy (Delta G degrees 10.02 kJmol(-1)). Taken together, thermodynamic parameters confirm the high stability of enzyme and show potential commercial applicability. (C) 2020 Elsevier B.V. All rights reserved.