Molecular interaction studies of l -alanine and l -phenylalanine in water and in aqueous citric acid at different temperatures using volumetric, viscosity and ultrasonic methods

The behavior of L-histidine (His) in an aqueous buffer solution (pH 7.4) is studied via densimetry and differential scanning calorimetry. The densities and specific heat capacities of solutions of the amino acid are determined in the 288.15-313.15 K range of temperatures at His concentrations of 0.00215 to 0.03648 mol kg −1 . The apparent and partial molar parameters of L-histidine in the buffer solution are found, and features of the temperature and concentration dependences are identified. It is shown that the partial molar properties of transferring the amino acid from water to the buffer solution (both volume and heat capacity) have positive values in the investigated range of temperatures. Different types of molecular interaction between the solute and the solvent are considered using the Gurney model.

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“…with temperature, which agrees with the data on other amino acids in aqueous solutions [1,2,15,[20][21][22].…”

Section: Volumetric Properties Of Solutionssupporting

confidence: 90%

“…Most biochemical processes occur in aqueous solutions. It is therefore of interest to study the physicochemical properties of biologically active substances in liquid phases [1][2][3][4][5][6]. Of special importance is the use of buffer systems that produce solutions similar to physiological media [7,8].…”

Section: Introductionmentioning

confidence: 99%

Molecular Interactions of L-Histidine in an Aqueous Buffer Solution in the Temperature Range of 288–313 K

Tyunina

Badelin

Kuritsyna

2020

Russ. J. Phys. Chem.

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“…The η data for both L-phenylalanine in water are compared with the literature values. [20][21][22][23]42 The experimental viscosities for both solutes studied in water show some deviation from the literature data 20,22 (Figure S2A,B). Das and Dash 22 have reported the viscosities for (0.0100−0.0811) mol•kg −1 L-phenylalanine in water, and their values of viscosities are slightly higher than the present values at (298.15 and 308.15) K (Figure S2A,B).…”

Section: Hydration Numbermentioning

confidence: 55%

Understanding Interactions between Amino Acids and Food Additives via Physicochemical and Spectroscopic Approaches

Kaur

Arti

Kaur³

et al. 2022

J. Chem. Eng. Data

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The effects of preservatives (E281 and E282) on the physicochemical and structural properties of amino acids in processed foods and other commodities have been studied using thermophysical (density and viscosity) and spectroscopic techniques in aqueous solutions. The explication of the derived properties shows that the addition of a cosolute intensifies the densities and viscosities of l-phenylalanine and l-tyrosine aqueous solutions and changes in the taste and hydration numbers of solute molecules. Preservatives have been designed to be physically and spectroscopically dehydrating; they thereby enhance solute–cosolute interactions over the hydration effect.

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“…Due to their importance in many industrial applications such as food and pharmaceutical sectors, many researchers are interested on the solubility enhancement 7,8 as well as the thermodynamic properties of amino acids 9 . Therefore, in this work, L-alanine was selected as the model compound, in which it is classified as a nonessential aliphatic amino acid which contains a methyl group 10 . Meanwhile an additive compound from different amino acid types including L-leucine and Glycine were used in an attempt to study their effect on L-alanine solubility behaviour.…”

Section: Introductionmentioning

confidence: 99%

Influence of amino acid additives on solution behaviour of L-alanine

Othman

Anuar

Bakar

et al. 2018

Chem. Eng. Res. Bull.

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Abstract:The solubility experiment of L-alanine solution was performed in a 250ml jacketed glass crystallizer without and with amino acid additives at temperature from 15 o C to 75 o C by means of gravimetric method. On the whole, L-leucine additive significantly altered the solubility of L-alanine and Glycine additive caused an erratic pattern on the solubility data of L-alanine. The hydrophobic methyl side chain of L-leucine additives is believed to contribute to the formation of water clathrate in the solution which affected the interaction of L-alanine molecules in water solvent and thus modified the solubility of L-alanine. Finally, thermodynamic data analysis of L-alanine solution was extensively assessed. The negative deviation of L-alanine from the ideal solution is as a result of high solute-solvent interaction, which is due to the hydrophobicity and clathrate phenomenon of the water molecules in the solution.

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Molecular interaction studies of l -alanine and l -phenylalanine in water and in aqueous citric acid at different temperatures using volumetric, viscosity and ultrasonic methods

Cited by 37 publications

References 46 publications

Molecular Interactions of L-Histidine in an Aqueous Buffer Solution in the Temperature Range of 288–313 K

Molecular Interactions of L-Histidine in an Aqueous Buffer Solution in the Temperature Range of 288–313 K

Understanding Interactions between Amino Acids and Food Additives via Physicochemical and Spectroscopic Approaches

Influence of amino acid additives on solution behaviour of L-alanine

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