Nutritional composition and proteomic analysis of soft-shelled turtle (Pelodiscus sinensis) egg and identification of oligopeptides with alpha-glucosidase inhibitory activity.

This study aimed to explore nutritional compositions and proteomics of soft-shelled turtle (SST) egg, as well as identify potential antidiabetic oligopeptides with α-glucosidase inhibitory property. Results revealed that SST egg is a promising source of highly nutritious proteins and minerals (54.64% and 5.81% of dry matter, respectively). Further proteomic analysis showed SST egg proteins contained at least 9 protein families, such as transferrin/iron binding protein and immunoregulation-related protein. Hydrolysis by different enzymes, especially papain, remarkably increased α-glucosidase inhibitory activity and scavenging activity for ABTS, DPPH, hydroxyl and oxygen radicals of SST egg proteins. Peptides from papain hydrolysate were fractionated using ultrafiltration followed by reverse phase chromatography, and 16 peptides were identified in the most active fraction by LC-QTOF-MS/MS. Molecular docking revealed that 14 of these peptides could easily dock into the substrate-binding pocket and/or inhibitor binding sites of α-glucosidase with the docking score below -150 kcal/mol, indicating their potential α-glucosidase inhibitory properties. The five most abundant oligopeptides with potent interaction with α-glucosidase were further synthesized, and oligopeptides HNKPEVEVR, ARDASVLK and SGTLLHK strongly inhibited the activity of α-glucosidase (IC of 56, 195 and 289 µmol/L, respectively). Therefore, oligopeptides from enzymatic hydrolysate of SST egg protein exhibit potential antidiabetic activity, making it a promising functional food ingredient.