Optimization of DsbA Purification from Recombinant Escherichia coli Broth Using Box-Behnken Design Methodology

罗曼; 关怡新; 姚善泾

doi:10.1016/S1004-9541(13)60457-7

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Optimization of DsbA Purification from Recombinant Escherichia coli Broth Using Box-Behnken Design Methodology

生物技术与生物工程 | Updated：2026-01-06

- Optimization of DsbA Purification from Recombinant Escherichia coli Broth Using Box-Behnken Design Methodology
- Optimization of DsbA Purification from Recombinant Escherichia coli Broth Using Box-Behnken Design Methodology
- 中国化学工程学报（英文版） 2013年21卷第2期页码：185-1911004-954160457-7
- Affiliations：
  
  Department of Chemical and Biological Engineering, Zhejiang University,Hangzhou,China,310027
- Author bio：
- Funds：
- DOI：10.1016/S1004-9541(13)60457-7
  中图分类号：
- 纸质出版：2013
- Accepted：
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罗曼, 关怡新, 姚善泾. Optimization of DsbA Purification from Recombinant Escherichia coli Broth Using Box-Behnken Design Methodology[J]. 中国化学工程学报（英文版）, 2013,21(2):185-1911004-954160457-7.

Broth Using Box-Behnken Design Methodology[J]. Chinese Journal of Chemical Engineering, 2013, 21(2): 185-191.
罗曼, 关怡新, 姚善泾. Optimization of DsbA Purification from Recombinant Escherichia coli Broth Using Box-Behnken Design Methodology[J]. 中国化学工程学报（英文版）, 2013,21(2):185-1911004-954160457-7. DOI： 10.1016/S1004-9541(13)60457-7.

Broth Using Box-Behnken Design Methodology[J]. Chinese Journal of Chemical Engineering, 2013, 21(2): 185-191. DOI： 10.1016/S1004-9541(13)60457-7.

摘要

Abstract

Disulfide bond formation protein A (DsbA) is one of the important helper proteins for folding in protein synthesis in vivo. In this study

purification of recombinant DsbA was investigated by examining four important factors with Box-Behnken design method

a statistic-based design of experiments. The optimal operation conditions were obtained by adopting the effectiveness coefficient method on the multi-objective problem

which takes the protein recovery

purification efficiency and throughput of ion-exchange chromatography into account. After the optimization

protein recovery of 96.8% and purity higher than 95% DsbA was achieved

and the productivity was (377.9?1.7) mg soluble DsbA per liter broth. The purified protein was identified by peptide mass fingerprinting matching the record of gi|2624856

a mutant of DsbA. The DsbA was preliminarily applied to the refolding of denatured lysozyme in vitro.

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