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2′-Fucosyllactose (2′-FL), a major component of fucosylated human milk oligosaccharides, is beneficial to human health in various ways like prebiotic effect, protection from pathogens, anti-inflammatory activity and reduction of the risk of neurodegeneration. Here, a whole-cell fluorescence biosensor for 2′-FL was developed.  Escherichia coli  ( E. coli ) was engineered to catalyse the cleavage of 2′-FL into  l -fucose and lactose by constitutively expressing α- l -fucosidase.  Escherichia coli  ∆L YA, in which  lacZ  is deleted and  lacY  is retained, was employed to disable lactose consumption.  E. coli  ∆L YA constitutively co-expressing α- l -fucosidase and a red fluorescence protein (RFP) exhibited increased fluorescence intensity in media containing 2′-FL. However, the presence of 50 g/L lactose reduced the RFP intensity due to lactose-induced cytotoxicity. Preadaptation of bacterial strains to fucose alleviated growth hindrance by lactose and partially recovered the fluorescence intensity. The fluorescence intensity of the cell was linearly proportional to 1–5 g/L 2′-FL. The whole-cell sensor will be versatile in developing a 2′-FL detection system.

Development of fluorescent Escherichia coli for a whole-cell sensor of 2ʹ-fucosyllactose