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. 2018 Oct 23;4(10):e00877.
doi: 10.1016/j.heliyon.2018.e00877. eCollection 2018 Oct.

Amino acid composition and antioxidant properties of Moringa oleifera seed protein isolate and enzymatic hydrolysates

Affiliations

Amino acid composition and antioxidant properties of Moringa oleifera seed protein isolate and enzymatic hydrolysates

Taiwo Ayodele Aderinola et al. Heliyon. .

Abstract

The aim of this work was to compare the antioxidant and angiotensin converting enzyme (ACE) inhibitory properties of Moringa oleifera seed protein isolate (ISO) and its enzymatic protein hydrolysates. ISO was subjected to enzymatic (alcalase, pepsin and trypsin) hydrolysis to obtain alcalase isolate, pepsin isolate and trypsin isolate hydrolysates (AIH, PIH, TIH). Amino acid composition was similar for the samples except that TIH had lower Sulphur-containing amino acids while PIH was lower in tryptophan. All the samples were tested for antioxidant properties through free radical scavenging abilities such as 2,2 diphenyl-1-picrylhydrazyl (DPPH) and hydroxyl radical scavenging assays as well as ferric reducing antioxidant power (FRAP) and metal ion chelation assays. The maximum percentage inhibition obtained for the samples from the different assays are: DPPH, 36% (PIH); FRAP, 0.04% (PIH); hydroxyl radical scavenging activity, 42.98% (ISO); and inhibition of metal ion chelation, 29.46% (AIH). AIH (79.3%) had the highest ACE-inhibitory activity followed by TIH (75.1%) while PIH (43.0%) had the least. Generally, the hydrolysis process produced hydrolysates with improved antioxidant and ACE-inhibitory properties when compared to the isolate. We conclude that enzymatic hydrolysis with alcalase, pepsin and trypsin may be used to produce M. oleifera seed protein hydrolysates with potential to be used as ingredients for the formulation of functional foods and nutraceuticals.

Keywords: Food analysis; Food science.

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Figures

Fig. 1
Fig. 1
Percentage (mean ± standard deviation, n = 3) of DPPH radical scavenging ability of Moringa oleifera seed protein isolate (ISO) and hydrolysates (AIH, alcalase hydrolysate; PIH, pepsin hydrolysate; TIH, trypsin hydrolysate). Bars with different letters have means values that are significantly different (p < 0.05).
Fig. 2
Fig. 2
Ferric reducing antioxidant power of glutathione (GSH), Moringa oleifera seed protein isolate (ISO) and hydrolysates (AIH, alcalase hydrolysate; PIH, pepsin hydrolysate; TIH, trypsin hydrolysate). Bars (mean ± standard deviation, n = 3) with different letters have means values that are significantly different (p < 0.05).
Fig. 3
Fig. 3
Percentage (mean ± standard deviation, n = 3) of hydroxyl radical scavenging ability of Moringa oleifera seed protein isolate (ISO) and hydrolysates (AIH, alcalase hydrolysate; PIH, pepsin hydrolysate; TIH, trypsin hydrolysate). Bars with different letters have means values that are significantly different (p < 0.05).
Fig. 4
Fig. 4
Percentage (mean ± standard deviation, n = 3) of metal ion chelation of Moringa oleifera seed protein isolate (ISO) and hydrolysates (AIH, alcalase hydrolysate; PIH, pepsin hydrolysate; TIH, trypsin hydrolysate). Bars with different letters have means values that are significantly different (p < 0.05).
Fig. 5
Fig. 5
Percentage (mean ± standard deviation, n = 3) angiotensin converting enzyme inhibition ability of captopril, Moringa oleifera seed protein isolate (ISO) and hydrolysates (AIH, alcalase hydrolysate; PIH, pepsin hydrolysate; TIH, trypsin hydrolysate). Bars with different letters have means values that are significantly different (p < 0.05).

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