Exploring the antioxidant stability of sheep bone protein hydrolysate -identification and molecular docking

• DOI: 10.1016/j.lwt.2023.115682
• Publication Date: 2023-12-28T07:08:11Z
• Authors: Guanhua Hu; Lu Dou; Jing Zhang; Rina Su; Mirco Corazzin; Lina Sun; Lihua Zhao; Ye Jin; Lin Su

The aim of this study was to obtain sheep bone protein hydrolysates (SBPHs) with antioxidant activity from byproducts and evaluate their stability processing characteristics under different conditions. Then, the peptides were identified synthesized, mechanism action investigated using molecular docking. results showed that SBPHs obtained by alkaline protease hydrolysis had high capacity a proportion hydrophobic amino acids (41.33%). intolerant temperatures weakly resistant alkalis. NaCl improved reducing power, sugars maintained activity, metal ions reduced SBPHs. higher after simulated gastrointestinal digestion. Three fractions isolated ultrafiltration, among which P–I (MW < 3 kDa) strongest activity. Liquid chromatography–tandem mass spectrometry (LC‒MS/MS) 17 Peptide Ranker >0.85 found in P–I. Among synthesized peptides, VYPFPGPIPN mainly exerted through hydrogen bonding, π-π stacking π-alkyl bonding Keap1. This provides reference for subsequent studies on production, storage function utilization