• Howell, Linda
• Werkmeister, Jerome
• Peng, Yong
• Stoichevska, Violet
• Ramshaw, John

Abstract

ecently, a different class of collagen-like molecules has been identified in numerous bacteria.Initial studies have shown that these collagens are readily produced in E. coli and they have been isolated and purified by various small scale chromatography approaches. These collagens are non-cytotoxic, non immunogenic and can be produced in much higher yields than mammalian collagens, making them potential new collagens forbiomedical materials.One of the major drawbacks with large scale fermentation of collagens has been appropriate scalable down-steam processing technologies.Like other collagens, the triple helical-domains of bacterial collagens are particularly resistant to proteolysis.The present study describes the development and optimisation 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.

Topics

• precipitation
• chromatography
• fermentation