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.
Highlights
Moringa oleifera is a popularly grown plant in many tropical and subtropical countries including India, Thailand, Philippines, Pakistan, Nigeria, and Senegal (Anwar, Zafar, & Rashid, 2006)
Membrane fractionation led to improved activities in all the fractions though there was no statistically significant difference between the 50.92 and 49.75% obtained for 3–5 kDa peptide fraction and the unfractionated hydrolyzate (TGH), respectively
The better free radical scavenging ability of the
Summary
Moringa oleifera is a popularly grown plant in many tropical and subtropical countries including India, Thailand, Philippines, Pakistan, Nigeria, and Senegal (Anwar, Zafar, & Rashid, 2006). Previous studies had reported the high nutritional values and varied health benefits of M. oleifera. The ability of food proteins or peptide fractions to impart further health benefits beyond their basic roles of supplying the body with the needed nutrition had been reported (Bekhit, Carne, & Birch, 2014; Doyen et al, 2014; He, Girgih, Malomo, Ju, & Aluko, 2013). While many positive health benefits have been attributed to M. oleifera, most of such reports were based on phenolic extracts of the different parts of the plant GPF (4%, w/v, protein basis) was dispersed in deionized water in a beaker, stirred continuously, heated to the appropriate temperature, and adjusted to the appropriate pH value as stated above prior to addition of the enzymes. A portion of the supernatant containing target peptides was freeze-dried as MPH
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