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Characteristics of protein partitioning in an aqueous micellar‐gel system
Author(s) -
van den Broeke L.J.P.,
van Roosmalen D.,
DohmenSpeelmans M.P.J.,
Dietz C.H.J.T.,
van der Wielen L.A.M.,
Keurentjes J.T.F.
Publication year - 2005
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.20710
Subject(s) - myoglobin , micelle , chemistry , bovine serum albumin , chromatography , phase (matter) , partition coefficient , ovalbumin , volume fraction , aqueous solution , partition (number theory) , micellar solutions , analytical chemistry (journal) , biochemistry , organic chemistry , immune system , mathematics , combinatorics , immunology , biology
Partitioning of proteins has been studied experimentally in a system combining a gel‐bead phase and a nonionic micellar phase. The micellar phase consists of cylindrically shaped micelles, which are completely excluded from the gel‐bead phase. Partitioning of single‐component protein solutions (myoglobin, ovalbumin, and BSA) is determined by excluded‐volume interactions in the micellar phase, and as a result the proteins prefer the gel‐bead phase to the micellar phase. The protein concentration inside the gel beads increases with an increase in volume fraction of the micelles and increases with an increase in the size of the proteins. The protein partition coefficients obtained for a binary mixture of myoglobin and bovine serum albumin (BSA) show the same protein concentration dependence as the single‐component protein partition coefficients. © 2005 Wiley Periodicals, Inc.