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

Content Provider	Springer Nature Link
Author	Peng, Yong Y. Stoichevska, Violet Madsen, Soren Howell, Linda Dumsday, Geoff J. Werkmeister, Jerome A. Ramshaw, John A. M.
Copyright Year	2014
Abstract	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.
Starting Page	1807
Ending Page	1815
Page Count	9
File Format	PDF
ISSN	01757598
Journal	Applied Microbiology and Biotechnology
Volume Number	98
Issue Number	4
e-ISSN	14320614
Language	English
Publisher	Springer Berlin Heidelberg
Publisher Date	2014-01-09
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	Non-animal collagen Precipitation Proteolysis Purification Triple helix Microbiology Microbial Genetics and Genomics Biotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Applied Microbiology and Biotechnology Biotechnology

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