What question did this study set out to answer?

The aim is to optimize the production of lacto-N-fucopentaose I using engineered E. coli strains.

April 10, 2026

Dynamic Regulation Coupled with Metabolic Pathway Optimization Enables High-Efficiency Lacto- N -fucopentaose I Biosynthesis in Escherichia coli

Puntos clave

The aim is to optimize the production of lacto-N-fucopentaose I using engineered E. coli strains.
Increased UDP-GlcNAc precursor pool through glmS overexpression.
Implemented a fructose-1,6-bisphosphate-responsive biosensor for dynamic regulation of pfkA expression.
Screened for effective transporters, identifying YhhS as a key exporter.
Optimized carbon source utilization and fermentation processes.
Achieved 3.50 g/L LNFP I in shake-flask fermentation.
Obtained 68.10 g/L LNFP I in a 5 L bioreactor.
Presented a conversion rate of 92.10% from LNT to LNFP I.
Demonstrated a productivity of 0.87 g/L/h.

Resumen

Lacto-N-fucopentaose I (LNFP I), the second most abundant fucosylated human milk oligosaccharide, plays important roles in infant health. In this study, we engineered an efficient Escherichia coli BL21star(DE3) cell factory for LNFP I production. The UDP-GlcNAc precursor pool was increased through glmSA overexpression, and a fructose-1,6-bisphosphate-responsive biosensor was implemented to dynamically regulate pfkA expression, thereby balancing cell growth with LNFP I biosynthesis. Transporter screening identified YhhS from E. coli as an effective exporter that enhanced LNFP I secretion. Strengthening carbon source utilization and optimizing the fermentation process enabled the development of a high-producing strain that achieved 3.50 g/L LNFP I in shake-flask fermentation and 68.10 g/L in a 5 L bioreactor, with an LNT-to-LNFP I conversion rate of 92.10% and a productivity of 0.87 g/L/h.

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