Refolding of detergent‐denatured lysozyme using  β ‐cyclodextrin‐assisted ion exchange chromatography | Zendy

Zhang Li | Zendy; Zhang Qinming | Zendy; Wang Chaozhan | Zendy

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Refolding of detergent‐denatured lysozyme using β ‐cyclodextrin‐assisted ion exchange chromatography

Author(s) -

Zhang Li,

Zhang Qinming,

Wang Chaozhan

Publication year - 2013

Publication title -

biomedical chromatography

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.4

H-Index - 65

eISSN - 1099-0801

pISSN - 0269-3879

DOI - 10.1002/bmc.2800

Subject(s) - chemistry , lysozyme , chromatography , cyclodextrin , ion chromatography , dithiothreitol , solubilization , urea , ion exchange , enzyme , biochemistry , ion , organic chemistry

Chromatography‐based protein refolding is widely used. Detergent is increasingly used for protein solubilization from inclusion bodies. Therefore, it is necessary to develop a refolding method for detergent‐denatured/solubilized proteins based on liquid chromatography. In the present work, sarkosyl‐denatured/dithiothreitol‐reduced lysozyme was used as a model, and a refolding method based on ion exchange chromatography, assisted by β ‐cyclodextrin, was developed for refolding detergent‐denatured proteins. Many factors affecting the refolding, such as concentration of urea, concentration of β ‐cyclodextrin, pH and flow rate of mobile phases, were investigated to optimize the refolding conditions for sarkosyl‐denatured lysozymes. The results showed that the sarkosyl‐denatured lysozyme could be successfully refolded using β ‐cyclodextrin‐assisted ion exchange chromatography. Copyright © 2012 John Wiley & Sons, Ltd.

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