Novel antioxidant peptides from bovine blood: Purification, identification and mechanism of action

2024/07/18 by Lin Wang, Ziyu Li, Xia Fan +3 · 7 citations
Biochemistry, Genetics and Molecular Biology · Agricultural and Biological Sciences · Medicine · #Protein Hydrolysis and Bioactive Peptides #Insect Utilization and Effects #Biochemical effects in animals

paper · doi:10.1016/j.lwt.2024.116499

Abstract

The purpose of this study was to isolate, purify, identify, and characterize novel antioxidant peptides derived from bovine blood hydrolysates (BBH). Results showed that, BBH, obtained by two-step flavourzyme-alcalase hydrolysis, was used to obtain five fractions by ultrafiltration and gel filtration chromatography, where the Fraction B had the strongest antioxidant capacity. Five novel antioxidant peptides (GFAGDDAPRA, SGPGIHVR, APSADAPM, TQRFFESF and HVDPENFKLL) were identified utilizing RP-HPLC and LC-MS/MS, and exhibited excellent free radical scavenging ability. GFAGDDAPRA and TQRFFESF possessed the highest ABTS radical scavenging rate (95.70% and 93.20%, respectively), and the DPPH radical scavenging rate of APSADAPM was the highest (50.28%). Moreover, these five peptides could be docked with Recombinant Kelch Like ECH Associated Protein 1 (Keap1) with the binding energies less than −5 kcal/mol, which indicated that they may be able to promote the body's antioxidant capacity by activating the Keap1-Nrf2 signaling pathway of cell. Meaningfully, this work shed new light on the processing and utilization of bovine blood, as well as offered a valuable foundation for the study and development of food-borne antioxidant peptides.

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