Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9690487 | China Particuology | 2005 | 6 Pages |
Abstract
Protein expression in E. coli often results in the formation of a kind of protein aggregate called inclusion body. Conversion of the inactive protein aggregate into biologically active protein is a key step in production of recombinant products. Conventional dilution refolding technique suffers from disadvantages of low recovery and low concentration. Various chromatographic refolding techniques have been developed over the last few years. These include size-exclusion chromatography, ion exchange chromatography, hydrophobic interaction chromatography and different affinity chromatography. A successful strategy is the use of gradient elution in column control which provides a gentle and gradual change of the solution environment for the macromolecule to refold at nano-scale. The gradient refolding at column scale could minimize misfolding and aggregation which are induced by sudden change of the solution in conventional refolding operation.
Keywords
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Fluid Flow and Transfer Processes
Authors
Fangwei Wang, Yongdong Liu, Jing Chen, Zhiguo Su,