Identification and characterization of an angiotensin-I converting enzyme inhibitory peptide from enzymatic hydrolysate of rape (Brassica napus L.) bee pollen

Abstract

In this study, we identified a novel angiotensin-I converting enzyme (ACE) inhibitory peptide, His-Pro-Val-Thr-Gly-Leu (HPVTGL), derived from rape bee pollen (RBP) protein hydrolysate. HPVTGL was separated by ultrafiltration and purified using preparative high-performance liquid chromatography. The ACE inhibitory activity of HPVTGL was stable across a range of pH values (2.0–8.0) and temperatures (<100 °C) and retained after in vitro gastrointestinal digestion. A Lineweaver–Burk plot suggested that the inhibitory mode of HPVTGL was competitive. The molecular docking model revealed that HPVTGL can bind to important active pockets in the ACE active sites. Furthermore, the antihypertensive effects in spontaneously hypertensive rats (SHRs) also revealed that oral administration of HPVTGL can significantly decrease systolic blood pressure and diastolic blood pressure. These results suggest that HPVTGL has potential for use in functional foods or pharmaceutical agents against hypertension.