Recombinant protein production in E. coli

Many therapeutic proteins, for example recombinant human insulin, are made in the bacterium Escherichia coli. Bacterial fermentation is a preferred production route for many proteins as it is a relatively cheap and simple process when compared to production in eukaryotic hosts. However, bacterial production of recombinant proteins is not perfect, as many proteins are difficult to manufacture in a functional, correctly-folded form. Research in my lab focuses on ways in which these protein production processes can be improved, through a combination of whole process design, optimisation and monitoring. We are interested in high cell density cultivation using fed-batch methods, single cell analysis using flow cytometry, coupling of fermentation to cell harvest and product release, and stress minimisation methods for optimisation of protein folding and bacterial viability. A PhD project in this area will include many of these aspects with the objective of improving process yield.

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