Recipient organisationUniversity of KentSource-published name: University of Kent
Funding£2K
PeriodJul 2025 — Jul 2026
In plain English
AI plain-English summary
Bacteria are being turned into tiny factories that package valuable molecules inside membrane bubbles and spit them out into the surrounding liquid. The University of Kent team has found a cheap way to tag proteins so that cells stuff them into these natural envelopes—called vesicles—and release them ready for collection. Currently, extracting useful proteins from bacteria is slow and expensive, requiring cell destruction and complex purification. This method lets researchers simply scoop the filled vesicles from the growth broth, and the packages stay stable in a fridge for months. By merging this approach with Leiden University’s expertise in membrane transport and nanoreactor engineering, the project aims to build self-contained chemical factories inside these vesicles. Success would mean bacteria producing nanoreactors that can run multi-step chemical reactions without needing to purify individual enzymes. This could transform industrial biocatalysis, making processes cheaper and simpler for manufacturing pharmaceuticals, specialty chemicals, or biofuels. The immediate work is fundamental—proving the concept works for complex reactions—but the potential payoff is a straightforward, scalable production system for valuable molecules.
View original technical description
The aim of this project is to develop an ERC synergy application (for submission in Nov 2025) to create and exploit biocatalytic nanoreactors for chemical and energy production industries. Realisation of this aim requires a new, close collaboration between my lab, at the University of Kent, with that of Professor Lars Jeuken (Leiden University, the Netherlands). Cells use small membrane bound envelopes, called vesicles, to store and export molecules out of the cell. The ability to reprogram a cell to control this process has huge potential for synthetic biology as it would allow us to harness the cell's machinery for the controlled packaging and release of commercially-valuable molecules neatly packaged into vesicles. We have recently discovered a way to hijack the cell to control this process. This simple and cost-effective invention results in bacteria that produce these membrane packages filled with molecules of interest that are exported from the cell into the growth broth, and can be stored for months in the fridge. This novel technology represents a major breakthrough in recombinant protein production as it facilitates simple, efficient and rapid purification of diverse proteins for use in biotechnology and medical applications. Merging the expertise in Vesicle Nucleating peptide -tagged proteins for the recombinant expression of vesicle-encapsulated biocatalysts (Mulvihill) with that of membrane transport, redox catalysis and nanoreactor engineering (Jeuken), will open up a new frontier in biocatalysis, by generating novel, self-contained synthetic chemical factories (nanoreactors). Success in this programme will see the development of a biotechnological platform in which engineered bacteria directly release nanoreactor for the biocatalysis of complex reactions. These nanoreactors will have functionality beyond the use of individual biocatalysts such multistep reactions (enzyme cascades) and compartmentalised chemistry. Furthermore, it will omit the requirement of biocatalyst purification as the nanoreactors can be straightforwardly and cheaply extracted from the growth media in an easily unscalable manner.
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