Secretory and extracellular production of recombinant proteins using Escherichia coli

Appl Microbiol Biotechnol. 2004 Jun;64(5):625-35. doi: 10.1007/s00253-004-1559-9. Epub 2004 Feb 14.


Escherichia coli is one of the most widely used hosts for the production of recombinant proteins. However, there are often problems in recovering substantial yields of correctly folded proteins. One approach to solve these problems is to have recombinant proteins secreted into the periplasmic space or culture medium. The secretory production of recombinant proteins has several advantages, such as simplicity of purification, avoidance of protease attack and N-terminal Met extension, and a better chance of correct protein folding. In addition to the well-established Sec system, the twin-arginine translocation (TAT) system has recently been employed for the efficient secretion of folded proteins. Various strategies for the extracellular production of recombinant proteins have also been developed. For the secretory production of complex proteins, periplasmic chaperones and protease can be manipulated to improve the yields of secreted proteins. This review discusses recent advances in secretory and extracellular production of recombinant proteins using E. coli.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Bacterial Proteins / metabolism
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / metabolism
  • Membrane Transport Proteins / metabolism
  • Molecular Chaperones / metabolism
  • Periplasm / metabolism*
  • Protein Folding
  • Protein Sorting Signals / physiology
  • Recombinant Proteins / biosynthesis*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • SEC Translocation Channels
  • SecA Proteins


  • Bacterial Proteins
  • Escherichia coli Proteins
  • Membrane Transport Proteins
  • Molecular Chaperones
  • Protein Sorting Signals
  • Recombinant Proteins
  • SEC Translocation Channels
  • twin-arginine translocase complex, E coli
  • Adenosine Triphosphatases
  • SecA Proteins