VLPs are non-infectious protein nanoparticles that mimic viral architec-ture without containing genetic material. Their highly ordered surfaces support epitope display for targeted delivery, vaccine design and related applications. Most VLPs are produced in insect, mammalian, plant or yeast systems, which can involve high costs, long timelines, heterogene-ity and scale-up or purification challenges. E. coli offers a fast, well-understood and cost-efficient alternative, but typically yields capsid proteins as inclusion bodies. Recovering function-al VLPs requires solubilization, contaminant removal and controlled re-folding and assembly – steps that are often laborious, hard to scale and associated with product loss in conventional workflows.