Production of ACE inhibitory peptides from sweet sorghum grain protein using alcalase: Hydrolysis kinetic, purification and molecular docking study

2016 ◽  
Vol 199 ◽  
pp. 140-149 ◽  
Author(s):  
Qiongying Wu ◽  
Jinjuan Du ◽  
Junqiang Jia ◽  
Cong Kuang
Keyword(s):  
Molecular Docking ◽  
Sweet Sorghum ◽  
Docking Study ◽  
Grain Protein ◽  
Molecular Docking Study ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Sorghum Grain ◽  
Ace Inhibitory

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.

scholarly journals Identification, structure-activity relationship and in silico molecular docking analyses of five novel angiotensin I-converting enzyme (ACE)-inhibitory peptides from stone fish hydrolysates

2018 ◽  
Author(s):  
Shehu Muhammad Auwal ◽  
Najib Zainal Abidin ◽  
Mohammad Zarei ◽  
Chin Ping Tan ◽  
Nazamid Saari
Keyword(s):  
Molecular Docking ◽  
Raw Materials ◽  
Docking Study ◽  
Inhibitory Effects ◽  
Molecular Docking Study ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
In Silico Molecular Docking ◽  
Ace Inhibitory ◽  
Antihypertensive Peptides

AbstractStone fish is an under-utilized sea cucumber with many health benefits. Hydrolysates with strong ACE-inhibitory effects were generated from stone fish protein under the optimum conditions of hydrolysis using bromelain and fractionated based on hydrophobicity and isoelectric properties of the constituent peptides. Five novel peptide sequences with molecular weight (mw) < 1000 daltons (Da) were identified using LC-MS/MS. The peptides including ALGPQFY (794.44 Da), KVPPKA (638.88 Da), LAPPTM (628.85 Da), EVLIQ (600.77 Da) and EHPVL (593.74 Da) were evaluated for ACE-inhibitory activity and showed IC50 values of 0.012 mM, 0.980 mM, 1.31 mM, 1.44 mM and 1.68 mM, respectively. The ACE-inhibitory effects of the peptides were further verified using molecular docking study. The docking results demonstrated that the peptides exhibit their effect mainly via hydrogen and electrostatic bond interactions with ACE. These findings provide evidence about stone fish as a valuable source of raw materials for the manufacture of antihypertensive peptides that can be incorporated to enhance therapeutic relevance and commercial significance of formulated functional foods.

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.

Generation and identification of angiotensin converting enzyme (ACE) inhibitory peptides from a brewers’ spent grain protein isolate

2015 ◽  
Vol 176 ◽  
pp. 64-71 ◽  
Author(s):  
Alan Connolly ◽  
Martina B. O’Keeffe ◽  
Charles O. Piggott ◽  
Alice B. Nongonierma ◽  
Richard J. FitzGerald
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Protein Isolate ◽  
Grain Protein ◽  
Converting Enzyme ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Spent Grain ◽  
Ace Inhibitory

Potential angiotensin I converting enzyme inhibitory peptides from gluten hydrolysate: Biochemical characterization and molecular docking study

2014 ◽  
Vol 60 (1) ◽  
pp. 92-98 ◽  
Author(s):  
Ahmad Asoodeh ◽  
Leyla Haghighi ◽  
Jamashidkhan Chamani ◽  
Mohamad Amin Ansari-Ogholbeyk ◽  
Zahra Mojallal-Tabatabaei ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Biochemical Characterization ◽  
Docking Study ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Molecular Docking Study ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme

scholarly journals Preparation and Identification of ACE Inhibitory Peptides from the Marine Macroalga Ulva intestinalis

Marine Drugs ◽  
2019 ◽  
Vol 17 (3) ◽  
pp. 179 ◽  
Author(s):  
Siqi Sun ◽  
Xiaoting Xu ◽  
Xue Sun ◽  
Xiaoqian Zhang ◽  
Xinping Chen ◽  
...  
Keyword(s):  
Liquid Chromatography ◽  
High Performance ◽  
Protein Hydrolysate ◽  
Molecular Docking Study ◽  
Protein Ratio ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ulva Intestinalis ◽  
Marine Macroalga ◽  
Ace Inhibitory

Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from seaweed represent a potential source of new antihypertensive. The aim of this study was to isolate and purify ACE inhibitory peptides (ACEIPs) from the protein hydrolysate of the marine macroalga Ulva intestinalis. U. intestinalis protein was hydrolyzed by five different proteases (trypsin, pepsin, papain, α-chymotrypsin, alcalase) to prepare peptides; compared with other hydrolysates, the trypsin hydrolysates exhibited the highest ACE inhibitory activity. The hydrolysis conditions were further optimized by response surface methodology (RSM), and the optimum conditions were as follows: pH 8.4, temperature 28.5 °C, enzyme/protein ratio (E/S) 4.0%, substrate concentration 15 mg/mL, and enzymolysis time 5.0 h. After fractionation and purification by ultrafiltration, gel exclusion chromatography and reverse-phase high-performance liquid chromatography, two novel purified ACE inhibitors with IC50 values of 219.35 μM (0.183 mg/mL) and 236.85 μM (0.179 mg/mL) were obtained. The molecular mass and amino acid sequence of the ACE inhibitory peptides were identified as Phe-Gly-Met-Pro-Leu-Asp-Arg (FGMPLDR; MW 834.41 Da) and Met-Glu-Leu-Val-Leu-Arg (MELVLR; MW 759.43 Da) by ultra-performance liquid chromatography-tandem mass spectrometry. A molecular docking study revealed that the ACE inhibitory activities of the peptides were mainly attributable to the hydrogen bond and Zn(II) interactions between the peptides and ACE. The results of this study provide a theoretical basis for the high-valued application of U. intestinalis and the development of food-derived ACE inhibitory peptides.

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