Antioxidant properties of camel and bovine colostrum upon simulated infant gastrointestinal digestion: Peptide identification, molecular simulation and binding mechanism

This study assessed the digestibility, antioxidant properties and peptide released upon simulated infant gastrointestinal digestion (SIGID) of camel and bovine colostrum. After SIGID, significant increase in degree of protein hydrolysis (DH) was observed in camel and bovine colostrum as compared to undigested samples. 2,2-Diphenyl-1-picrylhydrazyl (DPPH) and 2,2' -azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activities showed a significant increase after SIGID. Peptides generated after SIGID were then identified using LCMS-QTOF and their interaction was studied with Kelch-Neh2 Complex (PDB:2FLU) using molecular docking and dynamic simulation method. The selected peptides (camel colostrum: FPLAP and EGGFDAKLMFIV; and bovine colostrum: PGPPGTPGPI and SLVYPFPGPI) formed stable interactions with Keap 1 protein having binding energy of -8.6 and - 8.1; and - 9.2 and - 9.2, respectively, thereby potentially activating the Keap 1-Nrf2 signalling pathway. Hence, this gives insight about the digestibility pattern and antioxidant properties of camel and bovine colostrum under SIGID conditions, demonstrating their potential use as an active ingredient in infant formula.