ArticleFood chemistry: X2026
Optimization of enzymatic hydrolysis for generating potential multifunctional peptides from goat milk: Bioactivity evaluation, structural characterization and molecular interaction analysis.
Article in Food chemistry: X, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Food-derived bioactive peptides have attracted increasing interest for functional food development. In this study, goat milk proteins were enzymatically hydrolyzed to generate peptides with inhibitory activities against α-glucosidase (α-G), dipeptidyl peptidase-IV (DPP-IV), and xanthine oxidase (XO). Protease screening and response surface methodology were applied to optimize the composite hydrolysis process. The optimized goat milk hydrolysate exhibited inhibitory activities of 73.05 ± 1.38%, 88.63 ± 2.76%, and 80.69 ± 1.65% against α-G, DPP-IV, and XO, respectively. The active peptide fraction was further purified and analyzed by LC-MS/MS, identifying 24 peptide sequences. Bioinformatic screening highlighted LRF and FLPYPYY as potential multifunctional enzyme-inhibitory peptides. Molecular docking, 100 ns molecular dynamics simulations, and MM/PBSA analysis revealed favorable peptide-enzyme interactions and structural stability. This study provides an integrated enzymatic, analytical, and computational strategy for the discovery of goat milk-derived potential multifunctional bioactive peptides.
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