Characteristics of surface layer protein from Lactobacillus kefiri HBA20 and the role in mediating interactions with Saccharomyces cerevisiae Y8

In this study, the surface layer protein (SLP) from Lactobacillus kefiri HBA20 was characterized. The SLP was extracted by 5M LiCl. The molecular mass of the SLP was approximately 64 kDa as analyzed via SDS-PAGE. The surface morphology and the adhesion potential of L. kefiri HBA20 in the absence and presence of SLP were measured by AFM. Moreover, the protein secondary structure was evaluated by using circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR), respectively. SLP had high beta-sheet contents and low content of alpha-helix. Thermal analysis of SLP of Lactobacillus kefiri HBA20 exhibited one transition peak at 129.64 degrees C. 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. In conclusion, the SLP of Lactobacillus kefiri HBA20 has a stable structure and the ability of adhesion to yeast. Molecular docking study revealed that mannan bind with the hydrophobic residues of SLP. Our results will help further understanding of the new surface layer protein and the interaction between L. kefiri and S. cerevisiae.