ArticleApplied microbiology and biotechnology2014
A simple cost-effective methodology for large-scale purification of recombinant non-animal collagens.
Article in Applied microbiology and biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed, 44 citations in OpenAlex.
- Innovations and challenges in collagen and gelatin production through precision fermentation.World journal of microbiology & biotechnology · 2025Review
- Development and functional evaluation of recombinant type III collagen intrauterine implant gel.Regenerative biomaterials · 2025Article
- Article
- Expression and Purification of Collagen-Like Proteins of Group A Streptococcus.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Temporally degradable collagen-mimetic hydrogels tuned to chondrogenesis of human mesenchymal stem cells.Biomaterials · 2016Article
- Harnessing the Versatility of Bacterial Collagen to Improve the Chondrogenic Potential of Porous Collagen Scaffolds.Advanced healthcare materials · 2016Article
- Application of Collagen Scaffold in Tissue Engineering: Recent Advances and New Perspectives.Polymers · 2016Review
- Preparation and characterization of monomers to tetramers of a collagen-like domain from Streptococcus pyogenes.Bioengineered · 2014Article
- Engineered recombinant bacterial collagen as an alternative collagen-based biomaterial for tissue engineering.Frontiers in chemistry · 2014Article
- Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.