The objective of this experiment was to purify and analyze adhesion protein from the surface of Lactobacillus. The surface adhesion ligand of Lactobacillus was isolated with of LiCl method and (NH4)2SO4 method, followed by sephadex chromatography, analyzed with discontinuous native polyacrylamide gel electrophoresis, and tested with a binding assay with intestinal epithelial cells. We get the adhesion matter by two methods: ammonium sulfate and LiCl extraction. Further purification with sephadex chromatography produced 3 components. The second component of eluted from chromatography had adhesion enhancing ability compared with the control. A single band was present in discontinuous native—poly-acrylamide gel electrophoresis analysis and molecular weight was determined to be 43-66 KDa. The purified adhesion ligand can improve the number of Lactobacillus adhering to the intestinal epithelial cells.
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