Tyrosinase Inhibitory Peptide from the Hydrolysates of Eel Bone: Optimization of Preparation, Inhibition Kinetics and Molecular Docking

The main purpose of this study was to discover new tyrosinase inhibitory peptides from eel bone hydrolysates. After enzyme screening, alkaline protease was utilized, and optimal conditions were achieved through response surface optimization: solid-liquid ratio (1:25), time (5 h), and enzymolysis base ratio (3500 U/g). Inhibitory peptides of 1-3 kDa were isolated (IC50 = 2.162 mg/mL), and the inhibition was determined to be non-competitive and reversible. Subsequent LC-MS/MS and molecular docking revealed that the peptide with the lowest binding energy exhibited hydrogen bonding, hydrophobic interactions, and provided a potential explanation for the mechanism of inhibition by the peptides.