Antioxidant properties and inhibition of angiotensin-converting enzyme by highly active peptides from wheat gluten

AbstractThis study aimed to focus on the high-value utilization of raw wheat gluten by determining the potent antioxidant peptides and angiotensin I-converting enzyme (ACE) inhibitory peptides from wheat gluten oligopeptides (WOP). WOP were analyzed for in vitro antioxidant activity and inhibition of ACE, and the identification of active peptides was performed by reversed-phase high-performance liquid chromatography and mass spectrometry. Quantitative analysis was performed for highly active peptides. Five potent antioxidant peptides, Leu-Tyr, Pro-Tyr, Tyr-Gln, Ala-Pro-Ser-Tyr and Arg-Gly-Gly-Tyr (6.07 ± 0.38, 7.28 ± 0.29, 11.18 ± 1.02, 5.93 ± 0.20 and 9.04 ± 0.47 mmol 6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid (Trolox) equivalent/g sample, respectively), and five potent ACE inhibitory peptides, Leu-Tyr, Leu-Val-Ser, Tyr-Gln, Ala-Pro-Ser-Tyr and Arg-Gly-Gly-Tyr (half maximal inhibitory concentration (IC50) values = 0.31 ± 0.02, 0.60 ± 0.03, 2.00 ± 0.13, 1.47 ± 0.08 and 1.48 ± 0.11 mmol/L, respectively), were observed. The contents of Leu-Tyr, Pro-Tyr, Tyr-Gln, Ala-Pro-Ser-Tyr, Arg-Gly-Gly-Tyr, and Leu-Val-Ser were 155.04 ± 8.36, 2.08 ± 0.12, 1.95 ± 0.06, 22.70 ± 1.35, 0.25 ± 0.01, and 53.01 ± 2.73 μg/g, respectively, in the WOP. Pro-Tyr, Tyr-Gln, Ala-Pro-Ser-Tyr, Arg-Gly-Gly-Tyr, and Leu-Val-Ser are novel antioxidative/ACE inhibitory peptides that have not been previously reported. The results suggest that WOP could potentially be applied in the food industry as a functional additive.

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Optimization of process conditions for production of angiotensin I-converting enzyme (ACE) inhibitory peptides from vital wheat gluten using response surface methodology

Food Science and Biotechnology ◽

10.1007/s10068-013-0248-9 ◽

2013 ◽

Vol 22 (6) ◽

pp. 1531-1537 ◽

Cited By ~ 25

Author(s):

Rosemond Godbless Dadzie ◽

Haile Ma ◽

Ernest Ekow Abano ◽

Wenjuan Qu ◽

Shuyun Mao

Keyword(s):

Response Surface Methodology ◽

Wheat Gluten ◽

Process Conditions ◽

Converting Enzyme ◽

Angiotensin I ◽

Inhibitory Peptides ◽

Angiotensin I Converting Enzyme ◽

Ace Inhibitory Peptides ◽

Vital Wheat Gluten ◽

Ace Inhibitory

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Discovery of Novel Angiotensin-Converting Enzyme Inhibitory Peptides from Todarodes pacificus and Their Inhibitory Mechanism: In Silico and In Vitro Studies

International Journal of Molecular Sciences ◽

10.3390/ijms20174159 ◽

2019 ◽

Vol 20 (17) ◽

pp. 4159 ◽

Cited By ~ 6

Author(s):

Dingyi Yu ◽

Cong Wang ◽

Yufeng Song ◽

Junxiang Zhu ◽

Xiaojun Zhang

Keyword(s):

Angiotensin Converting Enzyme ◽

In Silico ◽

Ace Inhibition ◽

Degree Of Hydrolysis ◽

Converting Enzyme ◽

Inhibitory Peptides ◽

Todarodes Pacificus ◽

Ace Inhibitory Peptides ◽

Ace Inhibitory

In order to rapidly and efficiently excavate antihypertensive ingredients in Todarodes pacificus, its myosin heavy chain was hydrolyzed in silico and the angiotensin-converting enzyme (ACE) inhibitory peptides were predicted using integrated bioinformatics tools. The results showed the degree of hydrolysis (DH) theoretically achieved 56.8% when digested with papain, ficin, and prolyl endopeptidase (PREP), producing 126 ACE inhibitory peptides. By predicting the toxicity, allergenicity, gastrointestinal stability, and intestinal epithelial permeability, 30 peptides were finally screened, of which 21 had been reported and 9 were new. Moreover, the newly discovered peptides were synthesized to evaluate their in vitro ACE inhibition, showing Ile-Ile-Tyr and Asn-Pro-Pro-Lys had strong effects with a pIC50 of 4.58 and 4.41, respectively. Further, their interaction mechanisms and bonding configurations with ACE were explored by molecular simulation. The preferred conformation of Ile-Ile-Tyr and Asn-Pro-Pro-Lys located in ACE were successfully predicted using the appropriate docking parameters. The molecular dynamics (MD) result indicated that they bound tightly to the active site of ACE by means of coordination with Zn(II) and hydrogen bonding and hydrophobic interaction with the residues in the pockets of S1 and S2, resulting in stable complexes. In summary, this work proposed a strategy for screening and identifying antihypertensive peptides from Todarodes pacificus.

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Transepithelial transport across Caco-2 cell monolayers of angiotensin converting enzyme (ACE) inhibitory peptides derived from simulated in vitro gastrointestinal digestion of cooked chicken muscles

Food Chemistry ◽

10.1016/j.foodchem.2018.01.047 ◽

2018 ◽

Vol 251 ◽

pp. 77-85 ◽

Cited By ~ 13

Author(s):

Papungkorn Sangsawad ◽

Sittiruk Roytrakul ◽

Kiattawee Choowongkomon ◽

David D. Kitts ◽

Xiu-Min Chen ◽

...

Keyword(s):

Angiotensin Converting Enzyme ◽

Transepithelial Transport ◽

Converting Enzyme ◽

Gastrointestinal Digestion ◽

Cell Monolayers ◽

Inhibitory Peptides ◽

Ace Inhibitory Peptides ◽

Chicken Muscles ◽

Ace Inhibitory

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Bioavailability of angiotensin I converting enzyme inhibitory peptides

British Journal Of Nutrition ◽

10.1079/bjn20041189 ◽

2004 ◽

Vol 92 (3) ◽

pp. 357-366 ◽

Cited By ~ 343

Author(s):

Vanessa Vermeirssen ◽

John Van Camp ◽

Willy Verstraete

Keyword(s):

Blood Pressure ◽

Antihypertensive Effect ◽

Converting Enzyme ◽

Angiotensin I ◽

Inhibitory Peptides ◽

Angiotensin I Converting Enzyme ◽

Ace Inhibitory Peptides ◽

Ace Inhibitory

Hypertension or high blood pressure is a significant health problem worldwide. Bioactive peptides that inhibit angiotensin I converting enzyme (ACE) in the cardiovascular system can contribute to the prevention and treatment of hypertension. These ACE inhibitory peptides are derived from many food proteins, especially milk proteins. An ACE inhibitory activity in vitro does not always imply an antihypertensive effect in vivo. Even if it does, it is very difficult to establish a direct relationship between in vitro and in vivo activity. This is mainly due to the bioavailability of the ACE inhibitory peptides after oral administration and the fact that peptides may influence blood pressure by mechanisms other than ACE inhibition. To exert an antihypertensive effect after oral ingestion, ACE inhibitory peptides have to reach the cardiovascular system in an active form. Therefore, they need to remain active during digestion by human proteases and be transported through the intestinal wall into the blood. The bioavailability of some ACE inhibitory peptides has been studied. It is also known that (hydroxy)proline-containing peptides are generally resistant to degradation by digestive enzymes. Peptides can be absorbed intact through the intestine by paracellular and transcellular routes, but the potency of the bioactivity after absorption is inversely correlated to chain length. In addition, some strategies are proposed to increase the bioavailability of ACE inhibitory peptides. Further research into the bioavailability of ACE inhibitory peptides will lead to the development of more effective ACE inhibitory peptides and foods.

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Identification of novel angiotensin I-converting enzyme (ACE) inhibitory peptides from wheat gluten hydrolysate by the protease of Pseudomonas aeruginosa

Journal of Functional Foods ◽

10.1016/j.jff.2019.103751 ◽

2020 ◽

Vol 65 ◽

pp. 103751 ◽

Cited By ~ 6

Author(s):

Peng Zhang ◽

Chang Chang ◽

Haijie Liu ◽

Bo Li ◽

Qiaojuan Yan ◽

...

Keyword(s):

Pseudomonas Aeruginosa ◽

Wheat Gluten ◽

Converting Enzyme ◽

Angiotensin I ◽

Inhibitory Peptides ◽

Angiotensin I Converting Enzyme ◽

Ace Inhibitory Peptides ◽

Ace Inhibitory

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Angiotensin converting enzyme (ACE) inhibitory peptides derived from the simulated in vitro gastrointestinal digestion of cooked chicken breast

Journal of Functional Foods ◽

10.1016/j.jff.2016.12.005 ◽

2017 ◽

Vol 29 ◽

pp. 77-83 ◽

Cited By ~ 31

Author(s):

Papungkorn Sangsawad ◽

Sittiruk Roytrakul ◽

Jirawat Yongsawatdigul

Keyword(s):

Angiotensin Converting Enzyme ◽

Chicken Breast ◽

Converting Enzyme ◽

Gastrointestinal Digestion ◽

Inhibitory Peptides ◽

In Vitro Gastrointestinal Digestion ◽

Ace Inhibitory Peptides ◽

Ace Inhibitory

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Angiotensin I Converting Enzyme Inhibitory Peptides Obtained afterIn VitroHydrolysis of Pea (Pisum sativumvar. Bajka) Globulins

BioMed Research International ◽

10.1155/2014/438459 ◽

2014 ◽

Vol 2014 ◽

pp. 1-8 ◽

Cited By ~ 28

Author(s):

Anna Jakubczyk ◽

Barbara Baraniak

Keyword(s):

Inhibitory Activity ◽

Deae Cellulose ◽

Degree Of Hydrolysis ◽

Converting Enzyme ◽

Angiotensin I ◽

Inhibitory Peptides ◽

Angiotensin I Converting Enzyme ◽

Ace Inhibitory Peptides ◽

Ace Inhibitory

Pea seeds represent a valuable source of active compounds that may positively influence health. In this study, the pea globulins were digestedin vitrounder gastrointestinal condition and potentially bioaccessible angiotensin I converting enzyme (ACE) inhibitory peptides were identified. The degree of hydrolysis after pepsin, 14.42%, and pancreatin, 30.65%, were noted. The peptides with the highest ACE inhibitory properties were separated using ion exchange chromatography on DEAE-cellulose. Thirteen peptides fractions were obtained but only four showed potential antihypertensive properties. The highest inhibitory activity was determined for the fraction F8 (IC50 = 0.0014 mg/mL). This fraction was separated on Sephadex G10 and two peptide fractions were obtained. The peptides fraction (B) with the highest ACE inhibitory activity (IC50 = 0.073 mg/mL) was identified by ESI-MS/MS. The sequences of ACE inhibitory peptides were GGSGNY, DLKLP, GSSDNR, MRDLK, and HNTPSR. Based on Lineweaver-Burk plots for the fraction B, the kinetic parameters asKm,Vmax, andKiand mode of inhibition were determined. This fraction belongs to uncompetitive inhibitor of ACE activity. The seeds of pea are the source of precursor protein, which releases the ACE inhibitory peptides as a result of enzymatic hydrolysis.

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