Abstract
Flexible, well-dispersed and continuous 100-nm diameter cellulose fibers were prepared from an ionic liquid solvent by a novel dry-jet wet-electro spinning process. The ribbon fibers formed were chemically activated and an affinity dye, cibacron blue (CB) was immobilized at 0.22 g CB/g dry fibers loading to the surface of these fibers. The resulting affinity matrix was packed into a chromatography column and the adsorption, desorption and specificity of this matrix for bovine serum albumin (BSA) was studied. These electrospun fibers had a BSA binding capacity of 230 mg/g, nearly twice that of CB-immobilized 100-?m beads and over ten-fold higher capacity that CB-immobilized cellulose fibers prepared by a conventional electrospinning process. The results of this work suggest that chromatography supports of flexible, well-dispersed, continuous nanofibers may offer advantages over conventional supports in affinity separations.
Highlights
The rapid development of biotechnology and biomedicine requires more reliable and efficient separation technologies for the isolation and purification of biopolymers such as therapeutic proteins, antibodies, enzymes and nucleic acids
Unmodified cellulose can be directly regenerated into nanoscale fibers through dry-jet wet electrospinning using ionic liquid (IL)
cibacron blue (CB) immobilized fibers, used as an affinity chromatography packing, showed good adsorption behavior for 0.2 mg/mL bovine serum albumin (BSA) solution as compared with a column packed with CB immobilized beads
Summary
The rapid development of biotechnology and biomedicine requires more reliable and efficient separation technologies for the isolation and purification of biopolymers such as therapeutic proteins, antibodies, enzymes and nucleic acids. The retention of solutes is based on specific, reversible interactions found in biological systems, such as the binding of an enzyme with an inhibitor or an antibody with an antigen. These interactions are exploited in affinity chromatography by immobilizing an affinity ligand onto a support, and using this as a stationary phase. Traditional affinity chromatography relies on a column packed with gel beads. This approach has certain limitations including a high-pressure drop and low flow rates that lead to low productivities and difficulties in efficient scale-up
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