Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 65, Issue -, Pages 110-114Publisher
ELSEVIER
DOI: 10.1016/j.ijbiomac.2014.01.024
Keywords
Surface layer protein; Lactobacillus; Secondary structure; Amino acid composition; Probiotic function
Funding
- National Natural Science Foundation of China [31071491]
- Twelfths 5-year National Key Technology R&D Program of China [2012BAD33B05]
- 863 project [2013AA102207]
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The objective of this study was the characterization of the surface layer proteins (SLPs) and their functional role in the probiotic activity of Lactobacillus helveticus fb213, L. acidophilus fb116 and I. acidophilus fb214. SLPs were extracted and identified by SDS-PAGE, circular dichroism spectra and LC-MS analysis. The results revealed that the molecular masses of the three proteins were 49.7 kDa, 46.0 kDa and 44.6 kDa, respectively. The secondary structures and amino acid compositions of the three proteins were found to be similar. After removing SLPs, the survival of the three lactobacilli in simulated gastric and intestinal juices was reduced by 2-3 log as compared with survival of the intact cells. And the adhesion ability of the three strains to HT-29 cells decreased by 61%, 65% and 92%, respectively. SLPs also inhibited the adhesion and invasion of Escherichia coli ATCC 43893 to HT-29 cells. These results suggest that SLPs are advantageous barriers for lactobacilli in the gastrointestinal tract, and these proteins help make it possible for lactobacilli to serve their probiotic functions. (C) 2014 Elsevier B.V. All rights reserved.
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