4.7 Article

Solubility and solvation energetics of L-histidine in aqueous NaCl/KCl electrolyte media

Journal

JOURNAL OF MOLECULAR LIQUIDS
Volume 391, Issue -, Pages -

Publisher

ELSEVIER
DOI: 10.1016/j.molliq.2023.123240

Keywords

L -histidine; Solubility; Salting-out effect; Solvation energetics; Entropy

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This article describes the solubility etiquette of L-histidine, an important amino acid, in chloro aqueous solutions of alkali metals (Na, K) under equilibrium saturated conditions. The study discusses the interaction modes occurring during solvation and the influence of solvent molecules on L-histidine. The experimental results show that L-histidine has higher solubility in an aqueous KCl solution compared to a NaCl solution, and the solubility decreases with increasing electrolyte concentrations due to the salting-out effect. Additionally, the solubility of the amino acid increases with rising temperature in both electrolyte solutions.
This article describes the solubility etiquette of an important amino acid L-histidine in chloro aqueous solutions of alkali metals (Na, K) under equilibrium saturated conditions through an analytical gravimetric technique at equidistant temperatures. Different thermodynamic parameters along with transfer Gibbs energies under standard conditions were estimated using theoretical methods and experimental solubilities. The way of surrounding by solvent molecules of solute L-histidine in the used media is discussed based on different modes of interactions occurring during solvation. The experimental section describes that the L-histidine solubility enhances in an aqueous KCl solution rather than in NaCl solution. The drop down in L-histidine solubility with moving up electrolyte concentrations at a certain temperature is caused by the salting-out effect. For the studied amino acid, the salting out effect is more pronounced in NaCl electrolyte at any temperature. Amino acid shows higher solubility with rising temperature in both electrolytes' solutions. The current study suggests that the physical properties of NaCl and KCl and the size of the L-histidine molecules are two crucial factors for the chemical stability of the protein building unit.

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