Study of Bovine Serum Albumin Solubility in Aqueous Solutions by Intrinsic Viscosity Measurements

M.A. MASUELLI

Advances in Physical Chemistry

Hindawi

Lugar: New York; Año: 2013 vol. 2013 p. 1 - 8

1687-7993

The behavior of bovine serum albumin (BSA) in water is scarcely studied, and the thermodynamic properties arising from theexperimental measurements have not been reported. Intrinsic viscosity measurements are very useful in assessing the interactionbetween the solute and solvent. This work discussed in a simple determination of the enthalpy of BSA in aqueous solution when theconcentration ranges from 0.2 to 36.71% wt. and the temperature from 35 to 40∘C. The relationship between the concentration andintrinsic viscosity is determined according to the method of Huggins. The temperature increase reduces the ratio between inherentviscosity and concentration (𝜂𝑖/𝑐).This is reflected in theVan?tHoff curve. Furthermore, this work proposes hydrodynamic cohesionvalue as an indicator of the degree of affinity of protein with water and thermodynamic implications in conformational changes.