[ASC-list] Brisbane CHANGE of VENUE: AIBN Special Seminar: Assistant Professor Cristiana Boi, DICMA, Alma Mater Studiorum, Universita di Bologna.
jayne.keane at qm.qld.gov.au
Thu Sep 13 02:44:47 UTC 2012
AIBN SPECIAL SEMINAR: CHANGE OF VENUE
Assistant Professor Cristiana Boi, DICMA, Alma Mater Studiorum,
Universita di Bologna.
Purification of biomolecules using convective chromatography
Thursday, 13 September 2012
Q.B.P. Seminar Room, Level 3, Room 3.142
Abstract: Affinity chromatography represents one of the most important
and widely used unit operations in the biotechnology industry. However,
traditional packed bead columns suffer from several limitations such as
high pressure drop, slow mass transfer through the diffusive pores and
strong dependence of the binding capacity on flow rate. One possible
alternative to overcome these drawbacks is represented by convective
media columns packed with affinity membrane or monoliths.
This work presents the purification of immunoglobulin G in columns
packed with convective media, and discusses the enhanced performance
versus packed bead columns. The stationary phases studied derive from
the functionalization of membranes and monoliths with natural and
synthetic affinity ligands that show high specificity towards IgG.
The affinity materials are completely characterized through adsorption,
washing and elution cycles. The separation performance of the affinity
supports has been determined by feeding both pure IgG solutions and a
cell culture supernatant. Relevant process parameters, such as maximum
adsorption capacity, affinity equilibrium constant and selectivity, are
evaluated and carefully compared among the different affinity supports.
The scale-up of the improved affinity materials for industrial
applications is also addressed.
The experimental data collected have been used for the validation of a
proposed simulation model. Such chromatographic model is based on
species mass balance equation over the convective medium, coupled with a
suitable kinetic equation which represents the interaction between the
IgG target molecule and the ligand immobilized on the porous support.
Model simulations are in good agreement with all of the experimental
affinity cycles, demonstrating the accuracy of the model to describe the
transport phenomena in the column and the adsorption binding mechanism.
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