In vitro antihypertensive and antioxidative properties of trypsin‐derived Moringa oleifera seed globulin hydrolyzate and its membrane fractions

Protein isolate (globulin) was isolated from Moringa oleifera seed. This was hydrolyzed with trypsin and fractionated into different MW peptides sizes. Their antioxidant abilities (DPPH, FRAP, hydroxyl radical scavenging) were tested. Their in vitro antihypertensive properties were also tested. The peptide fractions showed good antioxidant and ACE inhibition abilities.

Abstract

Moringa oleifera seed globulin was hydrolyzed with trypsin and fractionated to produce <1, 1–3, and 3–5 kDa peptide sizes. These were evaluated for antioxidant properties: DPPH, hydroxyl radical scavenging assays, FRAP, and metal chelation tests; and in vitro antihypertensive properties: ACE and renin inhibition. Membrane fractionation led to improved antioxidative properties of 29.13% (<1 kDa), 180% (<1 kDa), and 30.58% (1–3 kDa) for DPPH, FRAP, and metal iron chelation, respectively. There was however 48.77% reduction (1–3 kDa) in hydroxyl radical scavenging activity. There was also improvement in ACE inhibitory potentials of the peptides with the 1–3 kDa peptide showing significantly highest ACE inhibition (72.48%)but very low (17.64%, 1–3 kDa) inhibition against the renin. It was concluded that hydrolysis of M oleifera seed globulin with trypsin produced peptides and peptide fractions with potential antioxidant and antihypertensive properties.

https://ift.tt/2r3JrY2