Identification and analysis of the function of surface layer proteins from three Lactobacillus strains
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To identify and investigate the role of surface layer proteins (SLPs) on the probiotic properties of Lactobacillus strains, SLPs were extracted from Lactobacillus bulgaricus fb04, L. rhamnosus fb06, L. gasseri fb07, and L. acidophilus NCFM by 5 mol/L lithium chloride. The molecular masses of the four SLPs were approximately 45–47 kDa as analyzed by SDS-PAGE. Hydrophobic amino acids were the main components of the four SLPs. The secondary structure content of the four SLPs showed extensive variability among different strains. After the SLPs were removed from the cell surface, the autoaggregation ability, coaggregation ability, and gastrointestinal tolerability of the four lactobacilli were significantly reduced as compared with the intact cells (P < 0.05). When exposed to bile salt stress, L. rhamnosus fb06, L. gasseri fb07, and L. acidophilus NCFM expressed more SLPs as determined by Bradford method. In conclusion, the four lactobacilli all possessed functional SLPs, which had positive contributions to the probiotic properties of the four Lactobacillus strains. This research could reveal the biological contributions of SLPs from Lactobacillus strains and offer a theoretical basis for the application of lactobacilli and their SLPs in food and pharmaceutical industries.
KeywordsSurface layer proteins Lactobacillus Amino acid composition Secondary structure Probiotic function
This study was supported by the grant from the National Natural Science Foundation of China (No. 31471696, 31701542) and Province Key Laboratory of Transformation and Utilization of Cereal Resource (PL2016009).
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Conflict of interest
The authors declare that they have no conflict of interest.
- Golowczyc MA, Mobili P, Garrote GL, de los Angeles Serradell M, Abraham AG, De Antoni GL (2009) Interaction between Lactobacillus kefir and Saccharomyces lipolytica isolated from kefir grains: evidence for lectin-like activity of bacterial surface proteins. J Dairy Res 76:111–116CrossRefPubMedGoogle Scholar