Understanding the chemistry of amino acids as the pillar of the proteins framework is vital when elucidating their mechanisms. The oxidation of aspartic acid (ASP) with molybdenum-oxime-ligand framework (MOL) is executed with the ultraviolet–visible spectroscopy technique, and the Menger- Portnoy model is generated in order to give more explanation to the empirical kinetic data. The aspartic acid’s oxidation is inert salt (NaCl) and counter-ion effects dependent. Deprotonation of the ASP countered the accelerating effect of the proton supplied by the acid (HCl). The mole ratio shared between the ASP and molybdenum-oxime-ligand framework is singlet with the generation of aldehyde malonic radical and carbon dioxide evolution. The kinetic order in [ASP] and [MOL] is singlet, and the thermodynamic activation parameter (ΔS‡ = −134.34 Jmol−1K−1) accounts for the solvation orderliness within the activated ASP-MOL specie at the transition state and the maintenance of MOL structural integrity. The interfacial active specie (sodium dodecyl sulphate, SDS) proves useful in catalysing ASP oxidation, and it is reinforced by Menger-Portnoy kinetic parameters.