Modeling of the Thermal Behaviour of Acid Phosphatase from Breadfruit (Artocarpus communis) Seeds: Equilibrium Model Approach

Abstract

Stabilization of enzymes is crucial to improve their durability and efficiency in various industrial applications. Thus, the search for new thermostable enzymes is a booming field. The seeds of Artocarpus communis are rich in acid phosphatases. Study of these enzymes could also be of interest in different biotechnological applications. Acid phosphatases are the enzymes that catalyze transphosphorylation reactions and promotes the hydrolysis of numerous orthophosphate esters in acidic media, as a crucial element for the metabolism of phosphate in tissues. The catalytic activity of Acid phosphatase from Artocarpus communis (ACP) seeds has been investigated using p-nitrophenylphosphate (pNPP) as substrate. Using the Equilibrium Model (EQM), the thermal inactivation data were analyzed. ΔG*act, ΔG*inact, ΔHeq and Teq were found to be (83.37 ± 0.02 kJ mol-1), (101.9 ± 0.2 kJ mol-1), (185 ± 2 kJ mol-1) and (326.90 ± 0.16 K) respectively. These results indicate that the enzyme is relatively stable in its native state, with the inactivation energy exceeding the catalytic energy.