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Liquid−Liquid Extraction of Proteins with Reversed Micelles
Author(s) -
Pires M. J.,
AiresBarros M. R.,
Cabral J. M. S.
Publication year - 1996
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp950050l
Subject(s) - micelle , extraction (chemistry) , chromatography , solubilization , chemistry , protein purification , cutinase , aqueous solution , kinetics , aqueous two phase system , liquid–liquid extraction , biochemistry , enzyme , organic chemistry , physics , quantum mechanics
The recovery of proteins using reversed micelles is a liquid−liquid extraction process that has received increasing attention since proteins were shown to be solubilized in organic solvents with surfactants, maintaining their functional properties, and to be transferred between an aqueous solution and a reversed micellar organic phase. This article reviews the application of reversed micellar systems as a bioseparation technique for isolation and purification of proteins. The parameters that affect protein solubilization into the reversed micelles and the equilibrium and kinetics aspects that are involved in the extraction and back‐extraction of proteins are discussed. Several examples are also described including the application of this technique for purification of recombinant proteins: cytochrome b 5 and a cutinase from Fusarium solani pisi .