Infant Gut Microbial Metagenome Mining of α- <scp>l</scp> -Fucosidases with Activity on Fucosylated Human Milk Oligosaccharides and Glycoconjugates
Eva M. Moya-Gonzálvez, Nazaret Peña-Gil, Antonio Rubio‐del‐Campo, José M. Coll-Marqués, Roberto Gozalbo‐Rovira, Vicente Monedero, Jesús Rodríguez‐Díaz, Marı́a J. Yebra
Abstract
α-l-Fucosyl residues are frequently present in many relevant glycans, such as human milk oligosaccharides (HMOs), histo-blood group antigens (HBGAs), and epitopes on cell surface glycoconjugate receptors. These fucosylated glycans are involved in a number of mammalian physiological processes, including adhesion of pathogens and immune responses. The modulation of l-fucose content in such processes may provide new insights and knowledge regarding molecular interactions and may help to devise new therapeutic strategies. Microbial α-l-fucosidases are exoglycosidases that remove α-l-fucosyl residues from free oligosaccharides and glycoconjugates and can be also used in transglycosylation reactions to synthesize oligosaccharides. In this work, α-l-fucosidases from the GH29 family were identified and characterized from the metagenome of fecal samples of breastfed infants. These enzymes showed different substrate specificities toward HMOs, HBGAs, naturally occurring glycoproteins, and neoglycoproteins. These novel glycosidase enzymes from the breast-fed infant gut microbiota, which resulted in a good source of α-l-fucosidases, have great biotechnological potential.