Screening, ACE-inhibitory mechanism and structure-activity relationship of a novel ACE-inhibitory peptide from Lepidium meyenii (Maca) protein hydrolysate  

作　　者：Zhengli Lin Junwen Lai Ping He Leiman Pan Yizhe Zhang Mengmeng Zhang Hui Wu 

机构地区：[1]College of Food Sciences and Engineering,South China University of Technology,Guangzhou,510640,PR China [2]College of Chemistry and Chemical Engineering,Zhongkai University of Agriculture and Engineering,Dongsha Street 24,Guangzhou,Guangdong,510225,China

出　　处：《Food Bioscience》2023年第2期281-289,共9页食品生物科学（英文）

基　　金：This work was supported by Guangzhou Science and Technology Planning Project(202102020773).

摘　　要：Maca is an edible functional plant with antihypertensive activity.However,there is still no clear understanding of angiotensin-converting enzyme(ACE)inhibitory substances in maca.In the present study,six novel angiotensin-converting enzyme inhibitor(ACEI)peptides(RSRGVFF,LGHPVFRNK,HGSCNYR,KANLGFRF,GGGHKRLY and SSYLGRN)were found in maca protein hydrolysates using in silico tools and molecular docking.RSRGVFF revealed prominent ACE inhibitory activity with an IC_(50) value of 5.01μM as a mixed-type ACE inhibitor.An analysis of the structure-activity connection demonstrated that the arginine at N-terminal is the most likely active residue in RSRGVFF,and two phenylalanines at the C-terminal also contributed to its inhibitory activity.Thus,these results indicate that maca protein may be one of the substances that leads to antihypertensive activity.This provides a new perspective to understanding the ACE inhibitory activity of maca and offers valuable insights to enlighten the structure-activity relationship of ACEI peptides.

关 键 词：Maca protein ACE inhibitory peptide Molecular docking Enzyme kinetics Structure-activity relationship 

分 类 号：TS201[轻工技术与工程—食品科学]