Interactions, desorption and mixing thermodynamics in mixed monolayers of β-lactoglobulin and bovine serum albumin

J Sanchez-Gonzalez, MA Cabrerizo-Vı́lchez… - Colloids and Surfaces B …, 2001 - Elsevier
Colloids and Surfaces B: biointerfaces, 2001Elsevier
The interactions between milk proteins, β-Lactoglobulin (β-Lg) and bovine serum albumin
(BSA), at the air–water interface have been evaluated. The surface pressure (π), molecular
area (a) isotherms were obtained by compression of the monolayers at different pH and
temperature. In the method used to calculate the interactions, the desorbed segments of the
proteins into the aqueous subphase have been considered. Earlier, the desorbed segments
have been estimated from the compressibility factor, z, as a function of the surface pressure …
The interactions between milk proteins, β-Lactoglobulin (β-Lg) and bovine serum albumin (BSA), at the air–water interface have been evaluated. The surface pressure (π), molecular area (a) isotherms were obtained by compression of the monolayers at different pH and temperature. In the method used to calculate the interactions, the desorbed segments of the proteins into the aqueous subphase have been considered. Earlier, the desorbed segments have been estimated from the compressibility factor, z, as a function of the surface pressure (virial state equation). The main conclusion from this study is that for biopolymers it is not possible to apply only the mixing thermodynamics to evaluate the intermolecular forces. It is necessary to include the desorption phenomenon. From these results, we can conclude that the main interaction between both proteins is of electrostatic character.
Elsevier
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