Angiotensin Converting Enzyme and Dipeptidyl Peptidase IV Inhibitory Activity of Protein Hydrolysates Obtained from Sunflower Meal

Abstract

In this study, the potential of sunflower protein hydrolysates to inhibit angiotensin converting enzyme (ACE) and dipeptidyl peptidase-IV (DPP-IV) enzyme was determined. Sunflower protein isolate was hydrolyzed with Alcalase and Trypsin+Chymotrypsin enzymes and the obtained protein hydrolysates were fractionated by ultrafiltration (<5 kDa and >5 kDa). The degrees of hydrolysis achieved by Alcalase and Trypsin+Chymotrypsin enzymes were 27% and 13%, respectively. The most potent ACE inhibitory activity (IC50=0.06 ± 0.01 mg/mL) was observed for the fraction that has molecular weight below 5 kDa, which was hydrolyzed by Trypsin+Chymotrypsin enzyme (P<0.05). The most potent DPP-IV inhibitory activity (IC50=0.30 ± 0.05 mg/mL) was obtained for the fraction that has molecular weight below 5 kDa with no significant difference between the enzymes used. The results of the study showed that sunflower meal protein is a potential source of bioactive peptide and the produced hydrolysates can be used as an alternative ingredient for functional food production.