A large
fraction of unused clinical transfusion plasma is nowadays
discarded. Nevertheless, some proteins, including serum albumin, immunoglobulins,
and clot factors, are still viable for use in diagnosis or research.
However,
lasma is a complex matrix, requiring multiple steps and time-consuming
methods for the isolation of proteins. In this work, aqueous micellar
two-phase systems (AMTPS) composed of nonionic surfactants (Triton
X-114 or Tergitol 15-S-7) were investigated to simultaneously separate
immunoglobulin G (IgG) and human serum albumin (HSA) from human expired
plasma. A factorial planning was applied to the nonionic surfactant
and plasma concentrations to enhance the systems separation performance.
After identifying the best conditions with AMTPS formed by nonionic
surfactants, mixed AMTPS formed by Tergitol 15-S-7 and various surface-active
ionic liquids (SAILs) acting as cosurfactants were additionally investigated
to tailor the proteins partition between the two phases. The mixed
AMTPS composed of Tergitol 15-S-7 as the nonionic surfactant and tributyltetradecylphosphonium
chloride as the cosurfactant at pH 8.0 improved the simultaneous separation
of both proteins to the opposite phases. IgG purification of 1.14-fold
in the surfactant-poor phase and HSA purification of 1.36-fold in
the surfactant-rich phase were obtained. Method reproducibility was
investigated using additional samples of human serum and plasma and
serum mixtures. Although improvements in the purification factor of
each protein are still a future goal, mixed AMTPS comprising nonionic
surfactants and SAILs as cosurfactants may be considered as novel
platforms to be used in the simultaneous separation of value-added
compounds from complex and natural matrices.
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