In this study,camel blood proteins were enzymatically digested using neutral protease,and the enzymatic process,pancreatic lipase (PL,PDB code:1ETH) inhibitory activity,molecular characteristics of the peptides,and molecular binding patterns were investigated with the aim of PL inhibitory peptides.The optimal processing conditions were 5% neutral protease,pH was 7.0,enzymolysis temperature was 55 ℃,and enzymolysis time was 3 h.Under optimized conditions,the PL inhibition rate reached 42.13%.A total of 533 peptides were identified using LC-MS/MS,of which eight peptides had a PeptideRanker score greater than 0.8.Among them,ALERMFLGF,GQPAVPVRF,and WDPSKVPPR exhibited significant binding with pancreatic lipase.Molecular dynamic simulation by AMBER 19 showed that all of them could interact with the residues in the active pocket residues of PL,primarily through electrostatic interactions,hydrogen bonding and hydrophobic interactions,thereby inhibiting its activity.Among them,CGPAVPVRF stands out the most potent PL inhibitor peptide,exhibiting the highest binding energy and possessing a greater number of binding sites.The study not only provides a reference for the development of novel PL inhibitor peptides,but also offers a new avenue for the high-value utilization of camel blood proteins.