Characterization of the structure, stability, and activity of hypoglycemic peptides from Moringa oleifera seed protein hydrolysates. Issue 6 (5th March 2022)

• Record Type: Journal Article
• Authors: Wang, Xuefeng; Fan, Yaozhu; Xu, Feiran; Xie, Jing; Gao, Xiaoyu; Li, Lingfei; Tian, Yang; Sheng, Jun
• Is Part Of: Food & function. Volume 13:Issue 6(2022)
• Page Start: 3481
• Page End: 3494
• Publication Date: 2022-03-05
• Subjects: Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; Nutrition -- Periodicals; 664.07
• DOI: 10.1039/d1fo03413h
• Languages: English
• ISSNs: 2042-6496

Abstract

Abstract : Moringa oleifera seed protein hydrolysates exhibit good hypoglycemic activity, but their specific peptide components have not yet been characterized. Abstract : Moringa oleifera seed protein hydrolysates exhibit good hypoglycemic activity, but their specific peptide components have not yet been characterized. Here, we identified the ultrafiltration peptide components (<3 kDa) of M. oleifera seed protein hydrolysates. A highly active α-glucosidase inhibitory peptide with an IC50 value of 109.65 μM (MoHpP-2) with the amino acid sequence KETTTIVR was identified. We characterized its structural properties, stability, and hypoglycemic activity. MoHpP-2 was found to be an amphipathic peptide with a β-turn structure, and the hemolysis of red blood cells was not observed when its concentration was lower than 2 mg mL −1 . MoHpP-2 was stable under weakly acidic conditions, at temperatures lower than 60 °C, and at high ion concentrations. Western blotting revealed that MoHpP-2 affected the PI3K and AMPK pathways of HepG2 cells. Molecular docking revealed that MoHpP-2 interacted with α-glucosidase through hydrogen bonding and hydrophobic forces. Thus, MoHpP-2 from M. oleifera seeds could be used to make hypoglycemic functional foods.