ACE-inhibitory peptides from Laminaria japonica and their potential anti-hypertensive mechanism. Issue 1 (1st January 2021)

• Record Type: Journal Article
• Authors: Wang, Jie; Ye, Xianjiang; Su, Zhichen; Zou, Ping; Pang, Jie; Chen, Ji-Cheng
• Is Part Of: CyTA: journal of food. Volume 19:Issue 1(2021)
• Page Start: 333
• Page End: 340
• Publication Date: 2021-01-01
• Subjects: Laminaria japonica proteins (LJPs) -- anti-hypertensive peptides -- ACE inhibitory -- enzymatic hydrolysis -- molecular docking; Proteínas de Laminaria japonica (LJP) -- péptidos antihipertensivos -- inhibidores de la ECA -- hidrólisis enzimática -- acoplamiento molecular; Food -- Periodicals; Nutrition -- Periodicals; Food -- Research -- Periodicals; 641.05
• DOI: 10.1080/19476337.2021.1900923
• Languages: English
• ISSNs: 1947-6337

Abstract

ABSTRACT: Bioactive peptides have been extensively applied for developing health-promoting foods. To improve the value of Laminaria japonica proteins ( LJPs ), anti-hypertensive peptides were prepared by using controlled enzymatic hydrolysis along with response surface methodology to improve their yields. Eight anti-hypertensive peptides with tyrosine (Tyr) at the C-terminal were determined through an efficient RP-HPLC method and molecular docking was performed to reveal the underlying mechanisms behind their effectiveness of anti-hypertension. According to the results, the strongest activity of hydrolysates was achieved under enzyme ratio (papain: alcalase: trypsin) 1:2:1, pH 8.0, temperature 60°C, substrate concentration 1.7%, enzyme addition 4.4%, and hydrolysis time 5.1 h. Furthermore, molecular docking results displayed that anti-hypertensive peptides could bind with ACE active sites through forming a stable composite structure, thus causing a significant reduction to activities. These results demonstrated the potential applications of LJPs as a source of anti-hypertensive peptides and provided a reference for the industrialized anti-hypertensive productions.