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PMID: 15629064 Published · epublish English Journal Article

Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli.

Microbial cell factories ·Vol. 4 ·No. 1 ·2005-01-04 ·Pages 1

Sørensen HP, Mortensen KK

Abstract

Pure, soluble and functional proteins are of high demand in modern biotechnology. Natural protein sources rarely meet the requirements for quantity, ease of isolation or price and hence recombinant technology is often the method of choice. Recombinant cell factories are constantly employed for the production of protein preparations bound for downstream purification and processing. Eschericia coli is a frequently used host, since it facilitates protein expression by its relative simplicity, its inexpensive and fast high density cultivation, the well known genetics and the large number of compatible molecular tools available. In spite of all these qualities, expression of recombinant proteins with E. coli as the host often results in insoluble and/or nonfunctional proteins. Here we review new approaches to overcome these obstacles by strategies that focus on either controlled expression of target protein in an unmodified form or by applying modifications using expressivity and solubility tags.

Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Sørensen Hans Peter
Laboratory of BioDesign, Department of Molecular Biology, Aarhus University, Gustav Wieds Vej 10C, 8000 Aarhus C, Denmark. kkm@mb.au.dk.
Mortensen Kim Kusk
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Article Info
Journal
Microbial cell factories
Abbr.
Microb Cell Fact
ISSN
1475-2859
Published
2005-01-04
Epub
2005-00-04
Pages
1
Language
English
Region
England
NLM ID
101139812
PMCID
PMC544838
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