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Bioprocess Engineering

, Volume 17, Issue 1, pp 35–38 | Cite as

Laboratory-scale permeabilization of Escherichia coli cells for recovery of a small recombinant protein – Staphylokinase

  • I. Gehmlich
  • H.-D. Pohl
  • W. A. Knorre

Abstract

The recovery of recombinant proteins includes a purification process that has to be compressed to a minimum of steps in order to get high yields with a low cost expenditure. A selective liberation of recombinant proteins by cell permeabilization leads to both a high product purity just in the beginning of the recovery process and to a simplification of the cell residue separation compared to the mechanical cell disruption. In case of the purification of the bacterial plasminogen activator Staphylokinase from E. coli cells, yields of 82% with a purity of 46% were attained by utilization of permeabilization by biomass freezing, resuspension in a Tris/EDTA-buffer and following micro-diafiltration. A recovery process without interruption (freezing) is possible due to the addition of guanidine-HCl and Triton X100 to the buffer. These methods were developed on a laboratory-scale.

Keywords

Biomass Triton X100 Recombinant Protein Plasminogen Plasminogen Activator 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1997

Authors and Affiliations

  • I. Gehmlich
    • 1
  • H.-D. Pohl
    • 1
  • W. A. Knorre
    • 1
  1. 1.Hans-Knöll-Institut für Naturstoff-Forschung, Bereich Bioverfahrensentwicklung, Beutenbergstr. 11, 07745 Jena, GermanyDE

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