Extraction, purification and identification of surface adhesion ligand from Lactobacillus

Abstract

The objective of this experiment was to purify and analyze adhesion protein from the surface of Lacto-bacillus. The surface adhesion ligand of Lactobacillus was isolated with of LiCl method and (NH 4) 2 SO 4 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-acry-lamide gel electrophoresis analysis and molecular weight was determined to be 43-66 KDa. The purified adhesion ligand can improve the number of Lac-tobacillus adhering to the intestinal epithelial cells.