Our results will help further understanding of the new surface layer protein and the interaction between L. Molecular docking study revealed that mannan bind with the hydrophobic residues of SLP. The technique is based upon the principle that a charged molecule will migrate in an electric field towards an electrode with opposite sign. Sodium dodecyl sulfate gel electrophoresis (SDS-PAGE) and circular dichroism (CD) spectroscopy were used to study the stability of the S-layer protein incubated. In conclusion, the SLP of Lactobacillus kefiri HBA20 has a stable structure and the ability of adhesion to yeast. Principle of Polyacrylamide Gel Electrophoresis (PAGE) SDS-PAGE (Polyacrylamide Gel Electrophoresis), is an analytical method used to separate components of a protein mixture based on their size. Furthermore, SEM measurements were showed that after the SLP were removed from the cell surface, the coaggregation ability with Saccharomyces cerevisiae Y8 of the strain was significantly reduced. sion and according to the SDS PAGE, it was at least 97. Thermal analysis of SLP of Lactobacillus kefiri HBA20 exhibited one transition peak at 129.64 ☌. the protein layers thickness and optical properties refractive index and extinction coef. SLP had high β-sheet contents and low content of α-helix. Moreover, the protein secondary structure was evaluated by using circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR), respectively. kefiri HBA20 in the absence and presence of SLP were measured by AFM. The surface morphology and the adhesion potential of L. Once your proteins are on the resolving gel, you can increase the voltage. Again with the help of the scraper, gently slide your gel out to a container. Do not fight against nature let your gel pick whichever side it wants to stick with. Use a scraper to gently separate the two pieces of glasses. The larger the gel, the higher the voltage. Your SDS-PAGE is done and you need to take the delicate gel off the glass plates. This step should take about 30 minutes at 50-60V. The molecular mass of the SLP was approximately 64 kDa as analyzed via SDS-PAGE. Whether or not you use a stacking gel or other gradient acrylamide gel, it is best to start your SDS-PAGE at a low voltage or current to get the proteins lined up in the gel. In this study, the surface layer protein (SLP) from Lactobacillus kefiri HBA20 was characterized.