Discovery and characterization of a novel α-l-fucosidase from the marine-derived Flavobacterium algicola and its application in 2'-fucosyllactose production.

Abstract 2′-Fucosyllactose (2′-FL) is one of the nutrient ingredients in human milk, which has various beneficial health effects. α-L-fucosidase is a biotechnological tool for 2′-FL preparation. Here, a novel and efficient α-L-fucosidase OUC-Jdch16 from the fucoidan-digesting strain Flavobacterium algicola 12076 was heterologously expressed and applied to produce 2′-FL in vitro. OUC-Jdch16 belonged to glycoside hydrolases (GH) family 29 and exhibited the highest 4-nitrophenyl-α-L-fucopyranoside-hydrolyzing activity at 25 ℃ and pH 6.0. OUC-Jdch16 could catalyze the synthesis of 2′-FL via transferring the fucosyl residue from pNP-α-fucose to lactose. Under the optimal transfucosylation conditions, the yield of the transfucosylation product reached 84.82% and 92.15% (mol/mol) from lactose within 48 h and 120 h, respectively. Moreover, OUC-Jdch16 was capable of transferring the fucosyl residue to other glycosyl receptors with the generation of novel fucosylated compounds. This study demonstrated that OUC-Jdch16 could be a promising tool to prepare 2′-FL and other novel glycosides.