Volumetric and Viscosity Properties of Monosaccharides in Aqueous Amino Acid Solutions at 298.15 K

Abstract

Apparent molar volumes V Φ,S and viscosity B-coefficients for D-(+)-glucose, D-(+)-galactose, D-(+)-xylose, and D-(-)-ribose in aqueous amino acid (glycine or L-alanine) solutions have been determined respectively from density and viscosity measurements at 298.15 K. Infinite-dilution apparent molar volumes for the saccharides V Φ,S 0 in aqueous glycine or L-alanine solutions have been evaluated, together with the standard transfer volumes ∆ t V Φ,S 0 of the saccharides from water to aqueous amino acid solutions. It is shown that values of transfer volumes and viscosity B-coefficients are positive and increase with increasing amino acid contents. Volumetric parameters indicating the interactions of saccharides with amino acids in water have been obtained from the transfer volumes of the saccharides. The interactions between saccharides and amino acids are discussed in terms of the structural interaction model and the stereo structure of monosaccharide molecules.

Density and Optical Properties of {Ciprofloxacin Hydrochloride + Aqueous-Ethanol} Mixtures at 30°C

“…Molecular interactions are studied through the measurements of refractive indices of solution [1][2][3]. and are useful for getting the valuable information about polarizability of solution [4][5][6][7][8].…”

Thermo-Acoustical Studies on Interionic Interactions of Some -amino Acids in Aqueous Sucrose Solution at Varying Mass Percentages

“…one useful approach is to investigate interactions of the model compounds of proteins, i.e., amino acids in aqueous and mixed-aqueous solution [1][2][3][4][5] . The physicochemical properties of amino acids in aqueous solutions provide valuable information on solute-solute and solute-solvent interactions that are important in understanding the stability of proteins, and are implicated in several biochemical and physiological processes in a living cell 6 .…”

“…Because of direct solute-solvent interactions and/ or alteration of the water structure, these solutes can change many properties of globular proteins, such as their hydration, solubility and the activity of enzymes 1, 4, 5, 11and 12 . These interactions are important in understanding the stability of proteins, and are implicated in several biochemical and physiological processes in a living cell [13][14][15][16] . The protein-carbohydrate interactions are important for immunology, biosynthesis, pharmacology, medicine, and cosmetic industry [17][18] .…”

“…Thus, the properties of amino acids in aqueous-carbohydrate solutions are essential for understanding the chemistry of biological systems [19][20][21][22] . Direct study of solute/solvent interactions is difficult due to complex conformation of biological macromolecules 5 . Therefore, the convenient approach is to study simpler model compounds i.e.…”

“…Therefore, the convenient approach is to study simpler model compounds i.e. amino acids and peptides, which are the basic components of proteins 5,6 . When dissolved in water amino acids convert into zwitterionic forms due to the ionization of their carboxyl ("COOH) and amino groups (NH 2 ).…”