Protein-phenolic interaction of tryptic digests of β-lactoglobulin and cloudberry ellagitannin

LC-ESI-MS was applied to investigate interaction reactions between a dimeric ellagitannin, sanguiin H-6, isolated from cloudberries (Rubus chamaemorus) and peptides of β-lactoglobulin (β-Lg). Three peptides, LIVTQTMK (m/z 934), ALPMHIR (m/z 838), and IPAVFK (m/z 674) were isolated from enzymatic (trypsin) digestion of β-Lg. Oxidation of the peptides with and without sanguiin H-6 was monitored by LC-ESI-MS for up to 7 days. Sanguiin H-6 showed radical scavenging activities toward oxidation of the selected peptides. An interaction product was found with sanguiin H-6 and peptide LIVTQTMK by using MS and supported by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). An observable (haze) but unstable interaction product of sanguiin H-6 was seen with peptide ALPMHIR, but no detectable interaction products were seen with peptide IPAVFK. A higher proportion of sanguiin H-6 toward the amount of peptide might allow for further characterization of these interaction products.