Improved production of 2′-fucosyllactose in engineered Escherichia coli by expressing putative α-1,2-fucosyltransferase, WcfB from Bacteroides fragilis

2′-Fucosyllactose (2-FL) is one of most abundant oligosaccharides in human milk, which is involved in many biological functions for infant health. Since 2-FL has a great potential in application to functional food materials and pharmaceuticals, several microbial systems for mass production of 2-FL have been developed in recent years. Microbial production of 2-FL was suggested to be influenced by a number of factors including fucosylation activity of α-1,2-fucosyltransferase. In the present study, the wcfB gene coding for α-1,2-fucosyltransferase from Bacteroides fragilis was screened from eleven candidates of putative α-1,2-fucosyltransferase. Introduction of the wcfB gene allows the lacZ-deleted strain of E. coli expressing the genes for guanosine 5′-diphosphate (GDP)-l-fucose biosynthetic enzymes to produce 2-FL. As a result of fed-batch fermentation, 15.4 g/L extracellular concentration of 2-FL with 2-FL yield of 0.858 g/g lactose and productivity of 0.530 g/L/h were obtained. In addition, the feasibility of industrial production of 2-FL using this microbial system was demonstrated by performing fed-batch fermentation in a 75 L bioreactor.