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• W3137095422 endingPage "9052" @default.
• W3137095422 startingPage "9039" @default.
• W3137095422 abstract "Lactic acid bacterial exopolysaccharides (EPS) are used in the food industry to improve the stability and rheological properties of fermented dairy products. β-Lactoglobulin (BLG), the dominant whey protein in bovine milk, is well known to bind small molecules such as fatty acids, vitamins, and flavors, and to interact with neutral and anionic polysaccharides used in food and pharmaceuticals. While sparse data are available on the affinity of EPS–milk protein interactions, structural information on BLG–EPS complexes, including the EPS binding sites, is completely lacking. Here, binding sites on BLG variant A (BLGA), for oligosaccharides prepared by mild acid hydrolysis of two EPS produced by Streptococcus thermophilus LY03 and Lactobacillus delbrueckii ssp. bulgaricus CNRZ 1187, respectively, are identified by NMR spectroscopy and supplemented by isothermal titration calorimetry (ITC) and molecular docking of complexes. Evidence of two binding sites (site 1 and site 2) on the surface of BLGA is achieved for both oligosaccharides (LY03-OS and 1187-OS) through NMR chemical shift perturbations, revealing multivalency of BLGA for EPS. The affinities of LY03-OS and 1187-OS for BLGA gave KD values in the mM range obtained by both NMR (pH 2.65) and ITC (pH 4.0). Molecular docking suggested that the BLGA and EPS complexes depend on hydrogen bonds and hydrophobic interactions. The findings provide insights into how BLGA engages structurally different EPS-derived oligosaccharides, which may facilitate the design of BLG–EPS complexation, of relevance for formulation of dairy products and improve understanding of BLGA coacervation." @default.
• W3137095422 created "2021-03-29" @default.
• W3137095422 creator A5002504519 @default.
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• W3137095422 date "2021-03-23" @default.
• W3137095422 modified "2023-10-16" @default.
• W3137095422 title "Binding Sites for Oligosaccharide Repeats from Lactic Acid Bacteria Exopolysaccharides on Bovine β-Lactoglobulin Identified by NMR Spectroscopy" @default.
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• W3137095422 doi "https://doi.org/10.1021/acsomega.1c00060" @default.
• W3137095422 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8028130" @default.
• W3137095422 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33842774" @default.
• W3137095422 hasPublicationYear "2021" @default.
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