%0 Journal Article
%T Study of Bovine Serum Albumin Solubility in Aqueous Solutions by Intrinsic Viscosity Measurements
%A Martin Alberto Masuelli
%J Advances in Physical Chemistry
%D 2013
%I Hindawi Publishing Corporation
%R 10.1155/2013/360239
%X The behavior of bovine serum albumin (BSA) in water is scarcely studied, and the thermodynamic properties arising from the experimental measurements have not been reported. Intrinsic viscosity measurements are very useful in assessing the interaction between the solute and solvent. This work discussed in a simple determination of the enthalpy of BSA in aqueous solution when the concentration ranges from 0.2 to 36.71%£¿wt. and the temperature from 35 to C. The relationship between the concentration and intrinsic viscosity is determined according to the method of Huggins. The temperature increase reduces the ratio between inherent viscosity and concentration ( ). This is reflected in the Van't Hoff curve. Furthermore, this work proposes hydrodynamic cohesion value as an indicator of the degree of affinity of protein with water and thermodynamic implications in conformational changes. 1. Introduction Solubility is the ability of a substance to dissolve into another; it is given by the solubility constant which is in equilibrium with the solute excess or ions excess. Basic studies on proteins have focused on protein concentration, pH, ionic strength, polymeric additives, the dielectric properties of solvent and solvent mixtures, and effect temperature. In the case of proteins and polysaccharides, solubility studies are closely related to studies of gelation that try to determine the temperature and the concentration of gelation ( and ) (Djabourov) [1]. The conformational stability of a protein is determined by intramolecular factors and solvent interactions (hydration). Solubility is determined primarily by intermolecular effects (protein/protein), but, as proteins are solvated, the hydration effects are also involved in changes in solubility. Conformational changes (changes in functional activity) can be induced by changes in temperature, pressure, and the solvent medium. The technological performance of proteins depends critically on conformation, hydration (water-holding capacity), and solubility. Like other polymers, proteins can be characterized by their chain conformations. However, methods of polymer statistics cannot be applied to most proteins because they adopt specific (native) conformations under different physiological conditions. Since proteins are polyelectrolytes, their solubility behavior is governed largely by electrostatic (ionic) interactions. In determining charge/charge interactions, and values of individual amino acids play an important role (Franks) [2]. Barton [3] worked with solubility parameters, trying to explain their nature and
%U http://www.hindawi.com/journals/apc/2013/360239/