Evaluation Of Antioxidant And Anti-cancer Properties Of Purified Peptides From Enzymatic Hydrolysis Of Grape Seed

In this study, the antioxidant and anti-cancer properties of bioactive peptides resulting from enzymatic hydrolysis of grape seed were determined using the microbial protease enzymes alcalase and flavourzyme. Protein hydrolysis was produced at three different times (10, 20 and 30 minutes), using commercial alcalase and flavourzyme enzymes at pHs of 8.5 and 7 (optimal pH of alcalase and flavourzyme enzymes) and in a ratio of 1 percentage of enzyme to the protein at a temperature of 50 ° C. The results showed that with increasing the hydrolysis time, the amount of protein recovery and the degree of hydrolysis increased and also the values of the mentioned parameters by the alcalase enzyme were significantly higher than the flavourzyme enzyme (p <0.05). The highest antioxidant activity (DPPH free radical scavenging activity, ferric regenerative power and ABTS free radical scavenging activity) and anti-cancer properties against SW742 cells (colon cancer cells) was observed in the protein hydrolyzed by alcalase enzyme and in 30 minutes (p <0.05). Due to the bitterness of this treatment (alcalase enzyme at time 30 minutes) its amino acid profile was determined, the highest levels of essential amino acid, valine 7.98% and then the amino acid leucine 7.11% and the highest un-essential amino acid glutamic acid was 19.55% and then the amino acid glycine was 12.55%. Overall, the hydrolyzed grape seed protein appears to have high antioxidant and anti-cancer activity, which may be useful ingredients in food and formulated diets applications.