To maintain the valid physiological effects of lactic acid bacteria (LAB) in large intestine, the adhesive properties of LAB to human colonic mucin (HCM) is essential. In this study, the primary factors associated with the adhesive property of LAB to rat colonic mucin (RCM) were investigated, which contains sugar chains similar to those in HCM. Specific lectins bound to RCM were isolated by using the reaction between the surface layer (Slayer) protein of Lactobacillus brevis FSB-1 and RCMcoated membrane. When the isolated specific lectins of L. brevis FSB-1 analyzed by sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE), 3 bands (about 24, 55, and 75 kDa) were observed on the electrophoretograms. And the specific sugar chains in glycoprotein of mucin also investigated by using modified colonic mucin-binding assay. The results indicated that Slayer protein of L. brevis FSB-1 bound to sialic acid and GalNAc${alpha}$1-3Gal. Therefore, it could be concluded that Slayer protein of L. brevis FSB-1 recognized the terminal sugar chains of RCM and bound to it.