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Quantification of the interactions between beta-lactoglobulin and pectin through capillary electrophoresis analysis.

Authors
  • Girard, Maude
  • Turgeon, Sylvie L
  • Gauthier, Sylvie F
Type
Published Article
Journal
Journal of agricultural and food chemistry
Publication Date
Sep 24, 2003
Volume
51
Issue
20
Pages
6043–6049
Identifiers
PMID: 13129314
Source
Medline
License
Unknown

Abstract

Biopolymer interactions have many potential applications in pharmaceutical, cosmetic, nutraceutical, and functional food industries. Attractive interactions between proteins and polysaccharides can lead to the formation of complexes. Binding parameters of beta-lactoglobulin (beta-lg)/pectin complexes were determined using frontal analysis continuous capillary electrophoresis and the overlapping binding site model. At pH 4, approximately 23 beta-lg molecules were cooperatively complexed on low-methoxyl pectin, where each beta-lg molecule covered an average of 12 galacturonic acid residues. The calculated binding constant was 1431 M(-1). The interactions between pectin and four selected peptides located on the outer surface of the beta-lg were investigated in order to identify which part of the protein was likely to interact with the pectin. The peptide beta-lg 132-148, which corresponds to the alpha-helix zone, and the peptides beta-lg 76-83, 41-60, and 1-14 would be involved in the interaction with the pectin.

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