In the present study several lactobacillus carrying surface layer proteins had been screened from those owned by our laboratory.They were Lactobacillus acidophilus fb116,Lactobacillus acidophilus fb115 and Lactobacillus helveticus fb213.The thermal analysis of the lyophilized surface layer proteins were performed by differential scanning calorimetry(DSC).DSC analysis showed one phase transition with maxima located at ca.63.67℃,61.98 ℃ and 59.78 ℃ for these three proteins.The amino acid compositions of the three proteins were determined mostly the same,which had a high content(45%) of hydrophobic amino acids and a higher content(24%) of acidic amino acids then basic ones.By circular dichrosim(CD) spectra the secondary structures of the proteins were predicted to be composed similarly of 34% alpha-helix and 12% beta-sheet.After removal of surface layer proteins,the autoaggregation percentage and the cell surface hydrophobicity of the three lactobacillus were reduced.It was implied that the surface layer proteins played a role in adhesion property of Lactobacillus.