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. 2018 Nov 25;7(1):132-138.
doi: 10.1002/fsn3.826. eCollection 2019 Jan.

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

Taiwo Ayodele Aderinola  1   2 , Tayo Nathaniel Fagbemi  1 , Victor Ndigwe Enujiugha  1 , Adeola Monisola Alashi  2 , Rotimi Emmanuel Aluko  2
Affiliations

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

Taiwo Ayodele Aderinola et al. Food Sci Nutr. .

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.

Keywords: ACE; Moringa oleifera seed; antihypertensive; globulin; hydrolyzate; membrane fractions; renin.

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Figures

Figure 1
Figure 1
Percentage DPPH radical scavenging capacities of Moringa oleifera seed protein hydrolyzate and its membrane fractions. Bars (means ± standard deviation) with different letters are significantly different at p < 0.05
Figure 2
Figure 2
Ferric reducing antioxidant power of Moringa oleifera seed protein hydrolyzate and its membrane fractions. Bars (means ± standard deviation) with different letters are significantly different at p < 0.05
Figure 3
Figure 3
Percentage hydroxyl radical scavenging capacities of Moringa oleifera seed protein hydrolyzate and its membrane fractions. Bars (means ± standard deviation) with different letters are significantly different at p < 0.05
Figure 4
Figure 4
Percentage metal chelation abilities of Moringa oleifera seed protein hydrolyzate and its membrane fractions. Bars (means ± standard deviation) with different letters are significantly different at p < 0.05. NA: no activity
Figure 5
Figure 5
Percentage angiotensin‐converting enzyme inhibition of Moringa oleifera seed protein hydrolyzate and its membrane fractions. Bars (means ± standard deviation) with different letters are significantly different at p < 0.05
Figure 6
Figure 6
Percentage renin inhibition of Moringa oleifera seed protein hydrolyzate and its membrane fractions. Bars (means ± standard deviation) with different letters are significantly different at p < 0.05
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References

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