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Expression of intein-tagged fusion protein and its applications in downstream processing

  1. Lishi Wang1,†,
  2. Jung Hye Kang1,
  3. Ki Hyung Kim1,
  4. E. K. Lee2,*

Article first published online: 16 OCT 2009

DOI: 10.1002/jctb.2277

Issue

Journal of Chemical Technology and Biotechnology

Journal of Chemical Technology and Biotechnology

Volume 85, Issue 1, pages 11–18, January 2010

Additional Information

How to Cite

Wang, L., Kang, J. H., Kim, K. H. and Lee, E. K. (2010), Expression of intein-tagged fusion protein and its applications in downstream processing. J. Chem. Technol. Biotechnol., 85: 11–18. doi: 10.1002/jctb.2277

Author Information

  1. 1

    Bioprocessing Research Laboratory, Dept. of Chemical Engineering, Hanyang University Ansan, Korea 426-791

  2. 2

    College of Bionanotechnology, KyungWon University, Sungnam, Korea 461-701

  1. †

    Inner Mongolia Medical College, Huhhot City, Inner Mongolia, People's Republic of China.

*College of Bionanotechnology, KyungWon University, Sungnam, Korea 461-701.

Publication History

  1. Issue published online: 1 DEC 2009
  2. Article first published online: 16 OCT 2009
  3. Manuscript Accepted: 10 SEP 2009
  4. Manuscript Revised: 23 AUG 2009
  5. Manuscript Received: 19 JUN 2009

Funded by

  • Ministry of Knowledge Economy (MKE)
  • Korea Industrial Technology Foundation (KOTEF)
  • Korea Science and Engineering Foundation (KOSEF)
  • Korean government (MEST). Grant Number: R11-2008-044-01001-0

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Keywords:

  • intein;
  • protein splicing element;
  • protein purification;
  • intervening proteins;
  • self-cleaving proteins;
  • affinity tag

Abstract

The conventional methods of downstream purification of a recombinant protein are not only complicated and delicate but time consuming, and need to be improved. Since the intein, the protein splicing element, was discovered, this self-cleaving element has been exploited and applied to the purification of recombinant proteins which could significantly simplify the purification procedure. Intein has the unique property that when it is combined with an affinity tag, it enables a target protein to be purified in a single chromatographic step. This review elucidates the properties of intein (the mechanism that unravels the intein-based protein splicing), the advantages of an intein affinity expression system, the progress of intein-based protein purification procedures, and recent advances in the applications of intein. Further development of the intein-based purification system may lead to the applications of this system to industrial-scale production of recombinant proteins. Copyright © 2009 Society of Chemical Industry

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