Solubility and thermodynamic interactions of L-aspartic acid in aqueous organic solvent systems

This study examines the complex behavior of L-aspartic acid in water-organic solvent systems, namely its solubility and thermodynamic interactions across a range of temperatures. L-aspartic acid, a vital component in protein synthesis and cellular processes, exhibits various solubility patterns influenced by solvent properties and structural features. Experimental methods involving gravimetric analysis were employed to measure solubility, revealing temperature-dependent trends. Results indicate that L-aspartic acid solubility increases with rise in temperature, with the highest solubility observed in pure water and lower solubility observed in organic media. Notably, L-aspartic acid shows significant solubility in water–dimethylformamide (DMF) systems owing to favorable dipole–dipole interactions. However, solubility diminishes in water–acetonitrile (ACN) systems, attributed to ACN’s hydrophobic nature. Thermodynamic analysis reveals complex interactions, including hydrogen bonding and dipole-dipole forces, impacting solvation. Furthermore, the role of L-aspartic acid is evaluated in solvent–solvent interactions, elucidating the changes in entropy and solvent structure. The introduction of L-aspartic acid disrupts intermolecular hydrogen bonds in water, leading to increased disorder. Conversely, the water-organic solvent systems exhibit structured arrays, influenced by acid–base interactions and solvent self-association. Overall, this investigation provides insights into the thermodynamic behavior of L-aspartic acid in mixed solvent systems, shedding light on its applications in biological and industrial realms. Further researches will elucidate the complex interactions.