The intestinal anaerobic bacterium *Akkermansia muciniphila* is specialized in degrading mucins, which are heavily O-glycosylated proteins that form the mucus lining the intestine. Despite its critical role in the human intestinal tract, the mechanisms by which *A. muciniphila* recognizes and binds to mucins are not well understood. This study demonstrates that *A. muciniphila* binds to mucins independently of environmental oxygen concentrations and pasteurization. Using a cell-based mucin array, the study found that *A. muciniphila* specifically recognizes the unsialylated LacNAc disaccharide on core2 and core3 O-glycans, which are abundant on human colonic mucins. Endogenous *A. muciniphila* neuraminidase activity was shown to uncover this epitope and enhance binding. These findings provide insights into the mucin-binding properties of *A. muciniphila*, a key mucin-degrading bacterium in the human gut.The intestinal anaerobic bacterium *Akkermansia muciniphila* is specialized in degrading mucins, which are heavily O-glycosylated proteins that form the mucus lining the intestine. Despite its critical role in the human intestinal tract, the mechanisms by which *A. muciniphila* recognizes and binds to mucins are not well understood. This study demonstrates that *A. muciniphila* binds to mucins independently of environmental oxygen concentrations and pasteurization. Using a cell-based mucin array, the study found that *A. muciniphila* specifically recognizes the unsialylated LacNAc disaccharide on core2 and core3 O-glycans, which are abundant on human colonic mucins. Endogenous *A. muciniphila* neuraminidase activity was shown to uncover this epitope and enhance binding. These findings provide insights into the mucin-binding properties of *A. muciniphila*, a key mucin-degrading bacterium in the human gut.