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Novel strategy for the revalorization of olive (Olea europaea) residues based on the extraction of bioactive peptides

Esteve, C., Marina, M.L., García, M.C.
Food chemistry 2015 v.167 pp. 272-280
Olea europaea, antioxidant activity, antioxidants, hydrolysates, in vitro digestion, inhibitory concentration 50, molecular weight, olive oil, olives, peptides, protein isolates, subtilisin, ultrafiltration
This work proposes a new strategy for the revalorization of residual materials from table-olive and olive oil production based on the extraction of bioactive peptides. Enzymatic hydrolysates of olive seed protein isolate were prepared by treatment with five different proteases: Alcalase, Thermolysin, Neutrase, Flavourzyme and PTN. Although all hydrolysates presented antioxidant properties, Alcalase was the enzyme that yielded the hydrolysate with the highest antioxidant capacity. All hydrolysates showed antihypertensive capacity, obtaining IC50 values from 29 to 350μg/ml. Thermolysin was the enzyme which yielded the hydrolysate with the highest ACE-inhibitory capacity. Hydrolysates were fractionated by ultrafiltration showing a high concentration of short chain peptides, which exhibited significantly higher antioxidant and antihypertensive capacities than fractions with higher molecular weights. Peptides in most active fractions were identified by LC–MS/MS, observing homologies with other recognized antioxidant and antihypertensive peptides. Finally, their antioxidant and antihypertensive capacities were evaluated after in vitro gastrointestinal digestion.