A Bacterial β1-3-Galactosyltransferase Enables Multigram-Scale Synthesis of Human Milk Lacto-N-tetraose (LNT) and Its Fucosides.

ABSTRACT: β1-3-Linked galactosides such as Galβ1‒3GlcNAcβOR are common carbohydrate motifs found in human milk oligosaccharides (HMOSs), glycolipids, and glycoproteins. Efficient and scalable enzymatic syntheses of these structures have proven challenging due to the lack of access to a highly active β1‒3-galactosyltransferase (β3GalT) in large amounts. Previously reported E. coli β3GalT (EcWbgO) has been identified as a limiting factor for producing a β1-3-galactose-terminated human milk oligosaccharide lacto-N-tetraose (LNT) by fermentation. Here we report the identification of an EcWbgO homolog from C. violaceum (Cvβ3GalT) which showed a high efficiency in catalyzing the formation of LNT from lacto-N-triose (LNT II). With the highly active Cvβ3GalT, multigram-scale (>10

SUBMITTER: McArthur JB 

PROVIDER: S-EPMC7785058 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature