Modeling of the Thermal Behaviour of Acid Phosphatase from Breadfruit (Artocarpus communis) Seeds: Equilibrium Model Approach
Kambiré Sobamfou Marius
General Chemistry Laboratory (GCL), University of Péléforo Gon Coulibaly, BP 1328 Korhogo, Côte d’Ivoire.
Gnanwa Mankambou Jacques
Agrovalorisation Laboratory, University of Jean Lorougnon Guédé, BP 150 Daloa, Côte d’Ivoire.
Niaré Adama *
Fundamental and Applied Physics Laboratory (FAPL), University of Nangui Abrogoua, Abidjan 02, Côte d’Ivoire.
Karamoko Bonito Aristide
European Membrane Institute (EMI), UMR 5635, University of Montpellier, 34090, Montpellier, France.
Dembélé Georges Stéphane
Laboratory of Thermodynamics and Physico-chemistry of the Environment, UFR SFA, Nangui University, 02 BP 801 Abidjan 02, Côte-d’Ivoire.
*Author to whom correspondence should be addressed.
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.
Keywords: Acid phosphatase, Artocarpus Communis, thermodynamic parameters, equilibrium model