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 

作者机构：College of Food Sciences and EngineeringSouth China University of TechnologyGuangzhou510640PR China College of Chemistry and Chemical EngineeringZhongkai University of Agriculture and EngineeringDongsha Street 24GuangzhouGuangdong510225China 

出 版 物：《Food Bioscience》 (食品生物科学（英文）)

年 卷 期：2023年第52卷第2期

页      面：281-289页

核心收录：

学科分类：1002[医学-临床医学] 100201[医学-内科学(含：心血管病、血液病、呼吸系病、消化系病、内分泌与代谢病、肾病、风湿病、传染病)] 10[医学] 

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

主　　题：Maca protein ACE inhibitory peptide Molecular docking Enzyme kinetics Structure-activity relationship 

摘      要：Maca is an edible functional plant with antihypertensive ***,there is still no clear understanding of angiotensin-converting enzyme(ACE)inhibitory substances 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 *** revealed prominent ACE inhibitory activity with an IC50 value of 5.01μM as a mixed-type ACE *** 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 ***,these results indicate that maca protein may be one of the substances that leads to antihypertensive *** 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.