A simple cost-effective methodology for large-scale purification of recombinant non-animal collagens

Yong Y. Peng, Violet Stoichevska, Soren Madsen, Linda Howell, Geoff J. Dumsday, Jerome A. Werkmeister, John A.M. Ramshaw

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28 Citations (Scopus)


Recently, a different class of collagen-like molecules has been identified in numerous bacteria. Initial studies have shown that these collagens are readily produced in Escherichia coli and they have been isolated and purified by various small-scale chromatography approaches. These collagens are non-cytotoxic, are non-immunogenic, and can be produced in much higher yields than mammalian collagens, making them potential new collagens for biomedical materials. One of the major drawbacks with large-scale fermentation of collagens has been appropriate scalable down-stream processing technologies. Like other collagens, the triple helical domains of bacterial collagens are particularly resistant to proteolysis. The present study describes the development and optimization of a simple, scalable procedure using a combination of acid precipitation of the E. coli host proteins, followed by proteolysis of residual host proteins to produce purified collagens in large scale without the use of chromatographic methods.

Original languageEnglish
Pages (from-to)1807-1815
Number of pages9
JournalApplied Microbiology and Biotechnology
Issue number4
Publication statusPublished - Feb 2014
Externally publishedYes


  • Non-animal collagen
  • Precipitation
  • Proteolysis
  • Purification
  • Triple helix

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