CHARACTERIZATION OF SEED STORAGE PROTEIN OF MORINGA OLEIFERA AND ANALYSES OF THEIR BIOACTIVE PEPTIDE’S NUTRACEUTICAL PROPERTIES

Abstract

Background. Bioactive peptides derived from food proteins have been the subject of considerable interest in recent years. Therefore, the present study aimed to evaluate the nutraceutical properties (antioxidant, antihypertensive, and antidiabetic activities) of bioactive peptides encrypted in seed storage proteins of Moringa oleifera using in vitro gastrointestinal digestion. Materials and methods. Seeds were ground and sieved. Next, the flour was defatted, washed, and dried. Seed storage proteins were obtained from moreinga seed flour using different solvents. Total proteins were extracted with sodium borato, centrifuged, and precipitated. Finally, hydrolysates were obtained with pepsin, trypsin, and chymotrypsin. The hydrolysates were fractionated by ultrafiltration with 10 and 3 kDa membranes. Results. Based on the obtained results, total globulin hydrolysate possessed a high percentage of angiotensinconverting enzyme inhibition (79.51 ±6.89%) and α-amylase inhibition activity (61.19 ±2.93%). On the other hand, the fraction F < 3 kDa had good antioxidant activity (290.66 ±26.9 μM). Conclusion. This study suggests that total globulin hydrolysates and F < 3 kDa had excellent in vitro nutraceutical potential.