摘要
Compared with chemical synthetic drugs, food derived bioactive compounds are increasingly become important in life sciences.In present study, ACE-inhibitory peptides were identified from Mactra veneriformis hydrolysate based on UPLC-Q-TOF MS coupled molecular docking method.Ultrafiltration was firstly used for separating hydrolysate into four fractions.The fraction with molecular weight lower than 1 kDa possesses the greatest ACE inhibitory activity.Active fraction then was analyzed by UPLC-Q-TOF MS/MS and sequences of peptides were calculated.Molecular docking was used to investigate the interactions between the calculated peptides and the ACE.Two ACE-inhibitory peptides with amino acid sequences of LASPTM and LL were obtained finally and LASPTM was verified as a potent peptide with an IC50 of 59.81 μM.