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Liquid-liquid phase separations in aqueous solutions of globular proteins

✍ Scribed by V. Vlachy; H. W. Blanch; J. M. Prausnitz

Publisher
American Institute of Chemical Engineers
Year
1993
Tongue
English
Weight
836 KB
Volume
39
Category
Article
ISSN
0001-1541

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✦ Synopsis

Abstract

A simple statistical‐mechanical theory, known as the random‐phase approximation, is applied to study liquid‐liquid phase separations in solutions of globular proteins. Phase separation may be induced by addition of nonionic polymer or/and ordinary electrolytes. In this analysis, the osmotic‐attraction mechanism, whereby the depletion of “solvent” particles between two proteins causes an attractive force, is primarily responsible for phase separation. For one‐component models of protein solutions, the theory yields simple algebraic expressions for the equation of state and for the chemical potential of the protein. This analytical theory describes the observed solubility behavior of proteins, including the effect of protein and polymer size, protein charge and concentration, and concentration of simple electrolytes.

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