Two Novel Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides from Rice (Oryza sativa L.) Bran Protein

To realize the high-value utilization of rice byproducts, the rice bran protein hydrolysate was separated and purified by ultrafiltration and reversed-phase high-performance liquid chromatography (RP-HPLC), then the sequences of peptides were identified by liquid chromatography with tandem mass spectrometry (LC–MS/MS), and their molecular docking analysis and activities in vitro and in the cell were carried out. Two novel peptides FDGSPVGY (840.3654 Da) and VFDGVLRPGQ (1086.582 Da) were obtained with IC50 values of 0.079 mg/mL (94.05 μM) and 0.093 mg/mL (85.59 μM) on angiotensin I-converting enzyme (ACE) inhibitory activity in vitro, respectively. Molecular docking results showed that two peptides interacted with ACE receptor protein through hydrogen bonding, hydrophobic interactions, etc. Through the EA.hy926 cells, it was found that FDGSPVGY and VFDGVLRPGQ could promote the release of nitric oxide (NO) and reduce the content of ET-1 to achieve the effect of antihypertension. In conclusion, the peptides from rice bran protein exhibited significant antihypertension activity and may be expected to realize the high-value utilization of rice byproducts.