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Secreted production of an elastin-like polypeptide by Pichia pastoris


Elastin-like polypeptides (ELPs) are biocompatible designer polypeptides with inverse temperature transition behavior in solution. They have a wide variety of possible applications and a potential medical importance. Currently, production of ELPs is done at lab scale in Escherichia coli shake flask cultures. With a view to future large scale production, we demonstrate secreted production of ELPs in methanol-induced fed-batch cultures of Pichia pastoris and purification directly from the culture medium. The production of ELPs by P. pastoris proved to be pH dependent within the experimental pH range of pH 3 to 7, as an increasing yield was found in cultures grown at higher pH. Because ELP produced at pH 7 was partly degraded, a pH optimum for production of ELP was found at pH 6 with a yield of 255 mg of purified intact ELP per liter of cell-free medium.

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The authors are grateful to Aernout Martens who provided the pMTL23-AIII cloning vector that was used for oligomerization and Antoine Moers for his assistance in the practical work. This project is financially supported by the Netherlands Ministry of Economic Affairs and the B-Basic partner organizations ( through B-Basic, a public–private NWO-ACTS program (ACTS = Advanced Chemical Technologies for Sustainability).

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Correspondence to Frits A. de Wolf.

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Open Access This is an open access article distributed under the terms of the Creative Commons Attribution Noncommercial License (, which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited.

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Schipperus, R., Teeuwen, R.L.M., Werten, M.W.T. et al. Secreted production of an elastin-like polypeptide by Pichia pastoris . Appl Microbiol Biotechnol 85, 293–301 (2009).

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  • Elastin-like polypeptides
  • Pichia pastoris
  • Secreted expression
  • Inverse transition cycling
  • Heterologous protein expression