ACE inhibitory peptides derived from de-fatted lemon basil seeds: optimization, purification, identification, structure–activity relationship and molecular docking analysis

2020 ◽  
Vol 11 (9) ◽  
pp. 8161-8178
Author(s):  
Norhameemee Kheeree ◽  
Papassara Sangtanoo ◽  
Piroonporn Srimongkol ◽  
Tanatorn Saisavoey ◽  
Onrapak Reamtong ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Process Conditions ◽  
Inhibitory Peptide ◽  
Docking Analysis ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptide ◽  
Structure Activity ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory ◽  
Molecular Docking Analysis

The study determines optimized process conditions to maximize ACE inhibitory peptide production. The two novel hexa-peptides (LGRNLPPI and GPAGPAGL) from de-fatted lemon basil seeds (DLBS) was achieved.

Production, optimisation and characterisation of angiotensin converting enzyme inhibitory peptides from sea cucumber (Stichopus japonicus) gonad

2018 ◽  
Vol 9 (1) ◽  
pp. 594-603 ◽  
Author(s):  
Chan Zhong ◽  
Le-Chang Sun ◽  
Long-Jie Yan ◽  
Yi-Chen Lin ◽  
Guang-Ming Liu ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Sea Cucumber ◽  
Docking Study ◽  
Converting Enzyme ◽  
Molecular Docking Study ◽  
Inhibitory Peptide ◽  
Stichopus Japonicus ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptide ◽  
Ace Inhibitory

The purification, characterization, and molecular docking study of a novel ACE inhibitory peptide (NAPHMR) derived from sea cucumber gonad hydrolysates.

ACE-Inhibitory Peptide Isolated from Fermented Soybean Meal as Functional Food

2013 ◽  
Vol 9 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Haikuan Wang ◽  
Shanting Zhang ◽  
Yan Sun ◽  
Yujie Dai
Keyword(s):  
Solid State ◽  
Soybean Meal ◽  
Functional Food ◽  
Inhibitory Peptide ◽  
Fermented Soybean Meal ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptide ◽  
Ace Inhibitory Peptides ◽  
Good Potential ◽  
Ace Inhibitory

AbstractBiologically active peptides as components in functional foods exhibit diverse activities and exert health effects in humans, just as the angiotensin I-converting enzyme (ACE)-inhibitory peptide exerts an antihypertensive effect. The solid-state fermentation of soybean meal was conducted using Bacillus subtilis natto at an appropriate temperature to accelerate proteolytic hydrolysis, and the crude extract containing ACE-inhibitory peptides was sequentially purified by ultrafiltration, gel chromatography and reverse phase-HPLC. A novel ACE-inhibitory peptide was obtained and its ACE-inhibitory activity was 84.1% with an IC50 value of 0.022 mg/ml. The results suggest that these ACE-inhibitory peptides obtained from the solid-state fermentation of soybean meal using B. subtilis natto have good potential for application in the management of hypertension and the fermented soybean meal has good potential for application in the production of a novel physiologically functional food.

scholarly journals Novel ACE Inhibitory Peptides Derived from Simulated Gastrointestinal Digestion in Vitro of Sesame (Sesamum indicum L.) Protein and Molecular Docking Study

2020 ◽  
Vol 21 (3) ◽  
pp. 1059 ◽  
Author(s):  
Ruidan Wang ◽  
Xin Lu ◽  
Qiang Sun ◽  
Jinhong Gao ◽  
Lin Ma ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Molecular Docking ◽  
Ace Inhibition ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Simulated Gastrointestinal Digestion ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

The aim of this study was to isolate and identify angiotensin I-converting enzyme (ACE) inhibitory peptides from sesame protein through simulated gastrointestinal digestion in vitro, and to explore the underlying mechanisms by molecular docking. The sesame protein was enzymatically hydrolyzed by pepsin, trypsin, and α-chymotrypsin. The degree of hydrolysis (DH) and peptide yield increased with the increase of digest time. Moreover, ACE inhibitory activity was enhanced after digestion. The sesame protein digestive solution (SPDS) was purified by ultrafiltration through different molecular weight cut-off (MWCO) membranes and SPDS-VII (< 3 kDa) had the strongest ACE inhibition. SPDS-VII was further purified by NGC Quest™ 10 Plus Chromatography System and finally 11 peptides were identified by Nano UHPLC-ESI-MS/MS (nano ultra-high performance liquid chromatography-electrospray ionization mass spectrometry/mass spectrometry) from peak 4. The peptide GHIITVAR from 11S globulin displayed the strongest ACE inhibitory activity (IC50 = 3.60 ± 0.10 μM). Furthermore, the docking analysis revealed that the ACE inhibition of GHIITVAR was mainly attributed to forming very strong hydrogen bonds with the active sites of ACE. These results identify sesame protein as a rich source of ACE inhibitory peptides and further indicate that GHIITVAR has the potential for development of new functional foods.

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