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2000
Volume 5, Issue 1
  • ISSN: 2211-3347
  • E-ISSN: 1874-4788

Abstract

Extracellular production of recombinant proteins using bacterial systems such as Escherichia coli has many advantages, including preferred protein properties, e.g. N-terminal authenticity, correct disulfide linkages, high product bioactivity and stability, and simplified downstream processing. This approach offers an impressive choice to the expression of naturally secretory proteins of which posttranslational modifications are non-essential for biological functions. In this communication, we review recent advances and patents obtained in excretory production of recombinant proteins in E. coli, making use of human epidermal growth factor (hEGF) as a model protein to illustrate how this approach has facilitated efficient production of hEGF. This enables affordable supply for an elaborate assessment of the biological functions of hEGF and subsequently its application to the development of a wide range of skincare and medically-oriented products for commercial applications.

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/content/journals/cheng/10.2174/2211334711205010045
2012-04-01
2025-10-02
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