Highly efficient folding of multi‐disulfide proteins in superoxidizing Escherichia coli cytoplasm. Issue 12 (5th August 2014)

• Record Type: Journal Article
• Authors: Zhang, Wenyao; Zheng, Wenyun; Mao, Miaowei; Yang, Yi
• Is Part Of: Biotechnology and bioengineering. Volume 111:Issue 12(2014:Dec.)
• Page Start: 2520
• Page End: 2527
• Publication Date: 2014-08-05
• Subjects: Biotechnology -- Periodicals; Bioengineering -- Periodicals; 660.6
• DOI: 10.1002/bit.25309
• Languages: English
• ISSNs: 0006-3592

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>ABSTRACT</title> <sec id="bit25309-sec-0001" sec-type="section"> <p>In this study, we monitored the thiol–disulfide redox potential of different <italic>Escherichia coli</italic> strains using redox‐sensitive variants of green fluorescent protein. The cells with extreme oxidizing cytoplasm were generated by introducing a highly efficient disulfide relay system. The developed cells have exceptionally efficient de novo disulfide bond formation and significantly improve the oxidative folding of the client multi‐disulfide proteins. Superoxidizing <italic>E. coli</italic> strain provides an effective method for the high‐level production of recombinant disulfide‐containing proteins. Biotechnol. Bioeng. 2014;111: 2520–2527. © 2014 Wiley Periodicals, Inc.</p> </sec> </abstract>