Literature DB >> 35089552

Protein Expression Optimization Strategies in E. coli: A Tailored Approach in Strain Selection and Parallelizing Expression Conditions.

Shyn Ric Tang1, Balaji Somasundaram1, Linda H L Lua2.   

Abstract

Escherichia coli remains a traditional and widely used host organism for recombinant protein production. Its well-studied genome, availability of vectors and strains, cheap and relatively straight-forward cultivation methods paired with reported high protein yields are reasons why E. coli is often the first-choice host expression system for recombinant protein production. The chapter enclosed here details protocols and design strategies in strain selection and methods on how to parallelize expression conditions to optimize for soluble target protein expression in E. coli. The methods described have been validated in a protein production research facility.
© 2022. Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Culture media; Culture parameters; E. coli; Expression Optimization; Protein Expression; Protein Solubility; Strains; pET system

Mesh:

Substances:

Year:  2022        PMID: 35089552     DOI: 10.1007/978-1-0716-1859-2_5

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  23 in total

Review 1.  Codon bias and heterologous protein expression.

Authors:  Claes Gustafsson; Sridhar Govindarajan; Jeremy Minshull
Journal:  Trends Biotechnol       Date:  2004-07       Impact factor: 19.536

2.  Refolding of cytochrome c using reversed micelles.

Authors:  M Sakono; M Goto; S Furusaki
Journal:  J Biosci Bioeng       Date:  2000       Impact factor: 2.894

3.  Direct refolding of recombinant human growth differentiation factor 5 for large-scale production process.

Authors:  J Honda; H Andou; T Mannen; S Sugimoto
Journal:  J Biosci Bioeng       Date:  2000       Impact factor: 2.894

Review 4.  Choose a Suitable Expression Host: A Survey of Available Protein Production Platforms.

Authors:  Francisco J Fernández; M Cristina Vega
Journal:  Adv Exp Med Biol       Date:  2016       Impact factor: 2.622

Review 5.  Codon Bias as a Means to Fine-Tune Gene Expression.

Authors:  Tessa E F Quax; Nico J Claassens; Dieter Söll; John van der Oost
Journal:  Mol Cell       Date:  2015-07-16       Impact factor: 17.970

6.  Highly efficient production of soluble proteins from insoluble inclusion bodies by a two-step-denaturing and refolding method.

Authors:  Zhong Yang; Linlin Zhang; Yan Zhang; Ting Zhang; Yanye Feng; Xiuxiu Lu; Wenxian Lan; Jufang Wang; Houming Wu; Chunyang Cao; Xiaoning Wang
Journal:  PLoS One       Date:  2011-07-29       Impact factor: 3.240

Review 7.  Solubilization and refolding of bacterial inclusion body proteins.

Authors:  Surinder Mohan Singh; Amulya Kumar Panda
Journal:  J Biosci Bioeng       Date:  2005-04       Impact factor: 2.894

8.  Overcoming the solubility limit with solubility-enhancement tags: successful applications in biomolecular NMR studies.

Authors:  Pei Zhou; Gerhard Wagner
Journal:  J Biomol NMR       Date:  2010-01       Impact factor: 2.835

9.  Escherichia coli physiology in Luria-Bertani broth.

Authors:  Guennadi Sezonov; Danièle Joseleau-Petit; Richard D'Ari
Journal:  J Bacteriol       Date:  2007-09-28       Impact factor: 3.490

Review 10.  Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system.

Authors:  Sofia Costa; André Almeida; António Castro; Lucília Domingues
Journal:  Front Microbiol       Date:  2014-02-19       Impact factor: 5.640

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