In vitro multifunctional bioactive properties of Moringa stenopetala seed enzymatic protein hydrolysates

This study characterized protein hydrolysates derived from Moringa stenopetala (MS) seed proteins after digestion with alcalase (ALH), flavourzyme (FLH), and pepsin + pancreatin (PPH). The bioactive potential of MS protein hydrolysates (MSPHs) was assessed through in vitro enzyme inhibition and antioxidant assays. PPH had the highest peptide yield (86.23%) while ALH showed higher surface hydrophobicity (7.61). ALH and PPH had the lowest peptide molecular weight distribution (0.4–2.19 kDa) when compared to FLH (0.7 – 6.9 kDa). FLH had relatively higher levels of arginine and Glx (Glu+Gln) but lowest content of tryptophan. ALH had the strongest ACE (15.07–66.56%) and renin (24.89–51.68%) inhibitions while FLH showed the highest pancreatic lipase (42.06–64.38%) and arginase (13.18–34.57%) inhibitions. PPH had the highest superoxide and hydroxyl radical scavenging activities as well as better ferric reducing antioxidant power and metal chelation activity. These findings suggest MSPHs as multifunctional agents with potential use in the formulation of antihypertensive, antidiabetic, and antioxidative functional foods.