1 General Chemistry Laboratory (LCG), University of Péléforo Gon Coulibaly, BP 1328 Korhogo, Côte d’Ivoire.
2 Fundamental and Applied Physics Laboratory (LPFA), University of Nangui Abrogoua, Abidjan 02, Côte d’Ivoire.
3 Thermodynamics and Environmental Physics Laboratory, University of Nangui Abrogoua, Abidjan 02, Côte d’Ivoire.
4 Agrovalorisation Laboratory, Jean Lorougnon Guédé University, Daloa, BP 150 Daloa, Cote d’Ivoire.
5 Ivorian Research Group in Disease Modeling (GIR2M), Abidjan, Côte-d’Ivoire.
Research Article
World Journal of Advanced Research and Reviews, 2024, 24(02), 671-681
Received on 24 September 2024; revised on 01 November 2024; accepted on 04 November 2024
This article focuses on modeling the kinetics of thermal inactivation of acid phosphatases extracted from breadfruit (Artocarpus communis L). By examining the stability of these enzymes at different temperatures, the study highlights their importance in the plant kingdom for fruit preservation, and in the animal kingdom for medical diagnostics. The study demonstrated that the kinetics of thermal inactivation of acid phosphatases P1A, P1B and P2 are influenced by temperature and the substrate used. Analyses revealed that more complex kinetic models, such as two-step models, offer a better representation of inactivation for certain substrates, notably PPNa and pNPP at specific temperatures. This indicates the formation of partially active enzymes in some cases. Understanding these inactivation mechanisms is crucial for optimizing the use of phosphatases in plant applications, such as fruit preservation, and in medical diagnostic contexts. The results obtained provide a solid basis for future research aimed at improving the stability and efficacy of phosphatases in various fields.
Acid phosphatases; Kinetic modeling; Artocarpus communis; Thermodynamics; Thermal inactivation
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Sobamfou Marius Kambiré, Adama Niaré, Georges Stéphane Dembélé, Akassa Marius Bernard Djako, Jacques Mankambou Gnanwa and Mamadou Guy-Richard Koné. Contribution to modeling the kinetics of phosphatase thermal inactivation. World Journal of Advanced Research and Reviews, 2024, 24(2), 671-681. Article DOI: https://doi.org/10.30574/wjarr.2024.24.2.3361