Enzymatically derived sunflower protein hydrolysate and peptides inhibit NFκB and promote monocyte differentiation to...

Enzymatic hydrolysis of proteins produces bioactive peptides that have the potential to provide health benefits. This study examined the inflammatory- and immune-modulating properties of a flavourzyme-derived sunflower protein hydrolysate (SPH) and peptides. The SPH was fractionated into <1, 1-3, 3-5, and >5 kDa peptides by membrane ultrafiltration. The SPH blunted IL-1β stimulated NFκB activation and boosted IL-4/GM-CSF induced expression of surface markers CD14 and CD86, indicating maturation into a dendritic cell (DC) phenotype. Testing of SPH membrane ultrafiltration and HPLC fractions indicated that smaller and non-polar peptides were the most potent, respectively. Four novel peptides (YFVP, SGRDP, MVWGP and TGSYTEGWS) were identified and all of them blunted IL-1β stimulated NFκB activation. The peptides also boosted IL-4/GM-CSF induction of CD14, while only MVWGP and TGSYTEGWS boosted the expression of CD86. MVWGP was the most potent immune-modulatory peptide across all cellular assays, which was attributed to the presence of a methionine residue.