Chromatographic refolding of proteins: molecular action and column control--颗粒学报PARTICUOLOGY

Wang, F., Liu, Y., Chen, J., & Su, Z. (2005). Chromatographic refolding of proteins: molecular action and column control. China Particuology, 3(6), 337-342. https://doi.org/10.1016/S1672-2515(07)60212-7

Chromatographic refolding of proteins: molecular action and column control

Fangwei Wang ^{a b}, Yongdong Liu ^b, Jing Chen ^b, Zhiguo Su ^b *

a Bioscience and Biotechnology Department, Dalian University of Technology, Dalian 116024, P. R. China
b National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100080, P. R. China

10.1016/S1672-2515(07)60212-7

Volume 3, Issue 6, December 2005, Pages 337-342

Received 10 November 2005, Accepted 26 November 2005, Available online 27 November 2007.

E-mail: zgsu@home.ipe.ac.cn

Highlights

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.

Graphical abstract

Keywords

protein refolding; size-exclusion chromatography; ion exchange chromatography; hydrophobic interaction chromatography; affinity chromatography

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