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. 2011;12(10):6685-702.
doi: 10.3390/ijms12106685. Epub 2011 Oct 11.

Effect of peptide size on antioxidant properties of African yam bean seed (Sphenostylis stenocarpa) protein hydrolysate fractions

Affiliations

Effect of peptide size on antioxidant properties of African yam bean seed (Sphenostylis stenocarpa) protein hydrolysate fractions

Comfort F Ajibola et al. Int J Mol Sci. 2011.

Abstract

Enzymatic hydrolysate of African yam bean seed protein isolate was prepared by treatment with alcalase. The hydrolysate was further fractionated into peptide sizes of <1, 1-3, 3-5 and 5-10 kDa using membrane ultrafiltration. The protein hydrolysate (APH) and its membrane ultrafiltration fractions were assayed for in vitro antioxidant activities. The <1 kDa peptides exhibited significantly better (p < 0.05) ferric reducing power, diphenyl-1-picryhydradzyl (DPPH) and hydroxyl radical scavenging activities when compared to peptide fractions of higher molecular weights. The high activity of <1 kDa peptides in these antioxidant assay systems may be related to the high levels of total hydrophobic and aromatic amino acids. In comparison to glutathione (GSH), the APH and its membrane fractions had significantly higher (p < 0.05) ability to chelate metal ions. In contrast, GSH had significantly greater (p < 0.05) ferric reducing power and free radical scavenging activities than APH and its membrane fractions. The APH and its membrane fractions effectively inhibited lipid peroxidation, results that were concentration dependent. The activity of APH and its membrane fractions against linoleic acid oxidation was higher when compared to that of GSH but lower than that of butylated hydroxyl toluene (BHT). The results show potential use of APH and its membrane fractions as antioxidants in the management of oxidative stress-related metabolic disorders and in the prevention of lipid oxidation in food products.

Keywords: African yam bean; antioxidant properties; butylated hydroxyl toluene; enzymatic protein hydrolysate; glutathione; peptide size; ultrafiltration.

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Figures

Figure 1
Figure 1
DPPH radical scavenging activities of African yam bean seed protein hydrolysate (APH) and its ultrafiltration membrane fractions.
Figure 2
Figure 2
Superoxide radical scavenging activities of African yam bean seed protein hydrolysate (APH) and its ultrafiltration membrane fractions.
Figure 3
Figure 3
Hydroxyl radical scavenging activities of African yam bean seed protein hydrolysate (APH) and its ultrafiltration membrane fractions.
Figure 4
Figure 4
Metal chelating effects of African yam bean seed protein hydrolysate (APH) and its ultrafiltration membrane fractions.
Figure 5
Figure 5
Ferric reducing power of African yam bean seed protein hydrolysate (APH) and its ultrafiltration membrane fractions.
Figure 6
Figure 6
Inhibition of linoleic acid oxidation by African yam bean seed protein hydrolysate (APH) and its ultrafiltration membrane fractions. Concentrations of APH, peptide fractions, glutathione (GSH) and butylated hydroxyl toluene: A, 1 mg/mL; B, 0.5 mg/mL; C, 0.25 mg/mL.

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