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Refolding of superoxide dismutase by ion-exchange chromatography

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Abstract

A new ion-exchange chromatography process was developed for refolding of iron superoxide dismutase (Fe-SOD) produced in Escherichia coli as an inclusion body. After adsorption on an ion-exchange matrix, the denatured protein was eluted by gradient decrease of urea concentration and pH of the elution buffer. The dual gradient allowed the denatured protein to refold to its correct native conformation with return of biological activity. Compared with the traditional dilution, refolding process, the new process increased the refolding yield five-fold. The process could also be carried out at high protein concentration to decrease the solution volume after refolding.

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Authors and Affiliations

  1. State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, P. R. China

    Ming Li & Zhi-Guo Su

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  1. Ming Li
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  2. Zhi-Guo Su
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Li, M., Su, ZG. Refolding of superoxide dismutase by ion-exchange chromatography. Biotechnology Letters 24, 919–923 (2002). https://doi.org/10.1023/A:1015596211026

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  • DOI: https://doi.org/10.1023/A:1015596211026

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