Glycans are ubiquitous in nature and are a key feature of glycoconjugate vaccines and therapeutic proteins. Glycoconjugate vaccines typically target cell surface glycans of bacterial pathogens and have been effectively deployed against Streptococcus pneumoniae, Neisseria meningitidis and Haemophilus influenzae. However, traditional methods to produce glycoconjugates are cumbersome and costly. Additionally, glycan structures are incredibly diverse. For example, there are over 100 different serotypes of S. pneumoniae each with a unique glycan capsule structure. Current glycoconjugate vaccines only cover ~20% of all serotypes. Here we combine a synthetic biology toolkit (Start-Stop Assembly, PMID: 30462270) and glycotechnology to engineer safe microbial strains that produce cost-effective therapeutic glycans. Further, we are employing automation to create a high-throughput production platform; the GlycoForge.  Start-Stop Assembly enables gene cluster refactoring, meaning that large glycan synthesis loci from pathogenic bacteria can be deconstructed for modular, bottom-up reassembly using standardised synthetic DNA parts. We have miniaturised and automated these DNA assemblies and have constructed the 10 gene pathway of an exemplar Campylobacter jejuni glycan as a large combinatorial library, showing highly efficient assembly and diverse glycan expression levels in E. coli. This GlycoForge pipeline is now in use for high-throughput production of S. pneumoniae capsule glycans, with the aim of producing glycoconjugate vaccines to cover a much higher proportion of the diverse S. pneumoniae population in comparison to current vaccines. In future applications, the GlycoForge pipeline will facilitate rapid production of a variety of glycan-based medicines and therapeutics, extending beyond cost-effective bacterial glycoconjugates.