The milk macromolecular peptide: preparation and evaluation of antihypertensive activity in rats

2020 ◽  
Vol 11 (5) ◽  
pp. 4403-4415 ◽  
Author(s):  
Pengfei Cui ◽  
Xue Yang ◽  
Yunliang Li ◽  
Qiufang Liang ◽  
Yucheng Wang ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Milk Protein ◽  
Antihypertensive Activity ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Digestive Function ◽  
Peptide Preparation ◽  
Preparation And Evaluation ◽  
Ace Inhibitory

In order to avoid the discomfort of digesting milk protein and make full use of the gastrointestinal digestive function, a milk macromolecular peptide was prepared with ACE inhibitory activity after gastrointestinal digestion as the index.

Effect of simulated gastrointestinal digestion on the antihypertensive properties of synthetic β-lactoglobulin peptide sequences

2007 ◽  
Vol 74 (3) ◽  
pp. 336-339 ◽  
Author(s):  
Blanca Hernández-Ledesma ◽  
Marta Miguel ◽  
Lourdes Amigo ◽  
Maria Amaya Aleixandre ◽  
Isidra Recio
Keyword(s):  
Inhibitory Activity ◽  
Ace Inhibition ◽  
Antihypertensive Activity ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Simulated Gastrointestinal Digestion ◽  
The Impact ◽  
Β Lactoglobulin ◽  
Ace Inhibitory

In this study, the antihypertensive activity in spontaneously hypertensive rats of two peptides isolated from β-lactoglobulin hydrolysates with thermolysin was evaluated. These peptides, with sequences LLF [β-lg f(103–105)] and LQKW [β-lg f(58–61)], showed potent in vitro ACE-inhibitory activity. Two hours after administration, both sequences caused a clear and significant decrease in the blood pressure of these rats. The impact of a simulated gastrointestinal digestion on ACE-inhibitory and antihypertensive activities of these peptides was also studied. The results showed that both fragments were susceptible to proteolytic degradation after incubation with pepsin and Corolase PP®. In addition, their in vitro ACE-inhibitory activity decreased after the simulated digestion. It is likely that fragment LQK was the active end product of the gastrointestinal digestion of peptide LQKW. The fragment LL, observed after digestion of peptide LLF, probably exert its antihypertensive effect through a mechanism of action different than ACE-inhibition.

scholarly journals Antioxidant and angiotensin I-converting enzyme inhibitory activities of Xuanwei ham before and after cooking and in vitro simulated gastrointestinal digestion

2018 ◽  
Vol 5 (7) ◽  
pp. 180276 ◽  
Author(s):  
Le Wang ◽  
Xiang Li ◽  
Yingnan Li ◽  
Wenying Liu ◽  
Xiaoyun Jia ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Scavenging Activity ◽  
Angiotensin I ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Before And After ◽  
Inhibitory Activities ◽  
Ace Inhibitory ◽  
Significant Increment

Xuanwei ham is especially rich in a large amount of peptides and free amino acids under the action of protein degradation. Some of these peptides can potentially exert bioactivities of interest for human health. Traditionally, Xuanwei ham should undergo Chinese household cooking treatments before eating. However, it has not been known how its bioactivity changes after cooking and gastrointestinal digestion. Herein, Xuanwei ham is analysed before and after cooking, as well as gastrointestinal digestion being simulated so as to evaluate and compare its effect on antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activities. The antioxidant activity is analysed using five different methods, and results demonstrate that cooking has some negative effects on antioxidative capacity when determined using different antioxidant methods except for a significant increment in 1,1'-diphenyl-2-picrylhydrazyl radical-scavenging activity, while ACE inhibitory activity increases significantly after cooking compared with control samples. After gastrointestinal digestion of samples, there is a significant increment of the antioxidant and ACE inhibitory activities in comparison with control and cooked samples. Particularly, after gastrointestinal digestion, free thiols content and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) radical-cation-scavenging activity of Xuanwei ham, respectively, increase about twice and fourfold, while ACE inhibitory activity increases about twice compared to cooked samples, reaching the value of 83.73%. Therefore, through cooking the antioxidant activity and ACE inhibitory activity of Xuanwei ham are not completely lost and a part of them is still maintained, while gastrointestinal digestion produces a significant enhancement in both bioactivities, highlighting a greater potential for a beneficial physiological effect on human health after eating it.

Angiotensin I Converting Enzyme–Inhibitory Activity of Bovine, Ovine, and Caprine κ-Casein Macropeptides and Their Tryptic Hydrolysates

2003 ◽  
Vol 66 (9) ◽  
pp. 1686-1692 ◽  
Author(s):  
M. A. MANSO ◽  
R. LÓPEZ-FANDIÑO
Keyword(s):  
Inhibitory Activity ◽  
Converting Enzyme ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Gastrointestinal Conditions ◽  
Tryptic Hydrolysate ◽  
Inhibitory Activities ◽  
Ace Inhibitory

This work evaluated the angiotensin-converting enzyme (ACE)–inhibitory activities of bovine, ovine, and caprine κ-casein macropeptides (CMPs) and their tryptic hydrolysates. The results obtained indicate that bovine, ovine, and caprine CMPs exhibited moderate in vitro ACE-inhibitory activities that increased considerably after digestion under simulated gastrointestinal conditions. Active peptides could also be produced from CMPs via proteolysis with trypsin, with tryptic hydrolysates exhibiting a more extensive ACE-inhibitory activity than intact CMPs during simulated gastrointestinal digestion. Two active fractions were chromatographically separated from the tryptic hydrolysate of the bovine CMP, but their complexity hampered the assignment of the ACE-inhibitory activity to specific peptide sequences. Evidence for the release of the strong ACE-inhibitory tripeptide IPP was found upon simulation of the gastrointestinal digestion of peptides released by trypsin from the CMP sequence. These findings might help to promote further exploitation of cheese whey in the preparation of nutraceuticals for inclusion in the composition of functional food products with high added values.

Optimisation of the hydrolysis of goat milk protein for the production of ACE-inhibitory peptides

2013 ◽  
Vol 80 (2) ◽  
pp. 214-222 ◽  
Author(s):  
Francisco Javier Espejo-Carpio ◽  
Raúl Pérez-Gálvez ◽  
Emilia M Guadix ◽  
Antonio Guadix
Keyword(s):  
Inhibitory Activity ◽  
Milk Protein ◽  
Goat Milk ◽  
Degree Of Hydrolysis ◽  
Ace Inhibitory Activity ◽  
Enzyme Substrate ◽  
Substrate Ratio ◽  
Input Variables ◽  
The Individual ◽  
Ace Inhibitory

Goat milk protein was hydrolysed with subtilisin and trypsin. As input variables, temperature was assayed in the interval 45–70 °C for subtilisin and 30–55 °C for trypsin, while the enzyme-substrate ratio varied from 1 to 5%. The effect of the input variables on the degree of hydrolysis and ACE-inhibitory activity (output variables) was modelled by second order polynomials, which were able to fit the experimental data with deviations below 10%. The individual maximum values of the degree of hydrolysis and the ACE-inhibitory activity were found at conflicting conditions of temperature and enzyme-substrate ratio. Since such maximum values could not be reached simultaneously, a bi-objective optimisation procedure was undertaken, producing a set of non-inferior solutions that weighted both objectives.

scholarly journals Whey-Derived Peptides Interactions with ACE by Molecular Docking as a Potential Predictive Tool of Natural ACE Inhibitors

2020 ◽  
Vol 21 (3) ◽  
pp. 864 ◽  
Author(s):  
Yara Chamata ◽  
Kimberly A. Watson ◽  
Paula Jauregi
Keyword(s):  
Molecular Docking ◽  
Amino Acid ◽  
Ace Inhibitors ◽  
Inhibitory Activity ◽  
Antihypertensive Activity ◽  
Ace Inhibitory Activity ◽  
Predictive Tool ◽  
Ace Inhibitory

Several milk/whey derived peptides possess high in vitro angiotensin I-converting enzyme (ACE) inhibitory activity. However, in some cases, poor correlation between the in vitro ACE inhibitory activity and the in vivo antihypertensive activity has been observed. The aim of this study is to gain insight into the structure-activity relationship of peptide sequences present in whey/milk protein hydrolysates with high ACE inhibitory activity, which could lead to a better understanding and prediction of their in vivo antihypertensive activity. The potential interactions between peptides produced from whey proteins, previously reported as high ACE inhibitors such as IPP, LIVTQ, IIAE, LVYPFP, and human ACE were assessed using a molecular docking approach. The results show that peptides IIAE, LIVTQ, and LVYPFP formed strong H bonds with the amino acids Gln 259, His 331, and Thr 358 in the active site of the human ACE. Interestingly, the same residues were found to form strong hydrogen bonds with the ACE inhibitory drug Sampatrilat. Furthermore, peptides IIAE and LVYPFP interacted with the amino acid residues Gln 259 and His 331, respectively, also in common with other ACE-inhibitory drugs such as Captopril, Lisinopril and Elanapril. Additionally, IIAE interacted with the amino acid residue Asp 140 in common with Lisinopril, and LIVTQ interacted with Ala 332 in common with both Lisinopril and Elanapril. The peptides produced naturally from whey by enzymatic hydrolysis interacted with residues of the human ACE in common with potent ACE-inhibitory drugs which suggests that these natural peptides may be potent ACE inhibitors.

scholarly journals Effect of in Vitro Gastrointestinal Digestion on Bioactivity of Poultry Protein Hydrolysate

2016 ◽  
Vol 4 (Special-Issue-October) ◽  
pp. 77-86 ◽  
Author(s):  
Torkova Anna ◽  
Kononikhin Alexey ◽  
Bugrova Anna ◽  
Khotchenkov Vyacheslav ◽  
Tsentalovich Mikhail ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Inhibitory Activity ◽  
Protein Hydrolysate ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Food Ingredient ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

In vitro simulated gastrointestinal digestion (GID) was performed to evaluate changes in bioactive properties of Poultry protein hydrolysate HCP Premium P150 (PPH) showing strong antioxidant (448.2±37.0 µM TE/g of protein) and moderate Angiotensin-I converting enzyme inhibitory activity (IC50 0.617±0.022 mg/ml). Antioxidant and ACE-inhibitory activity were measured with use of ORAC assay and FRET-substrate methods, correspondingly. Gastric digestion (GD) increased ACE inhibitory activity 2.23 times and didn’t change antioxidant activity of PPH significantly. The subsequent intestinal digestion increased antioxidant activity 1.29 times and didn’t change ACE-inhibitory activity significantly. New potent ACE-inhibitory peptides: APGAPGPVG (IC50 16.2±3.8 µM), PDLVF (IC50 84.9±6.3 µM) and antioxidant dipeptide WG (2.29±0.04 µM TE/µM) were identified in the digested PPH. The digested PPH proved to be a rich source of antioxidant and ACE inhibiting molecules and could be a potential new food ingredient used for prevention or treatment of socially significant diseases.

scholarly journals Antihypertensive Effects of Virgin Olive Oil (Unfiltered) Low Molecular Weight Peptides with ACE Inhibitory Activity in Spontaneously Hypertensive Rats

Nutrients ◽  
2020 ◽  
Vol 12 (1) ◽  
pp. 271 ◽  
Author(s):  
Juan María Alcaide-Hidalgo ◽  
Miguel Romero ◽  
Juan Duarte ◽  
Eduardo López-Huertas
Keyword(s):  
Molecular Weight ◽  
Inhibitory Activity ◽  
Spontaneously Hypertensive Rats ◽  
Virgin Olive Oil ◽  
Antihypertensive Activity ◽  
Low Molecular Weight ◽  
Hypertensive Rats ◽  
Ace Inhibitory Activity ◽  
Spontaneously Hypertensive ◽  
Ace Inhibitory

The low molecular weight peptide composition of virgin olive oil (VOO) is mostly unknown. We hypothesised that unfiltered VOO could possess low molecular weight peptides with antihypertensive activity. We produced unfiltered VOO and obtained a water-soluble peptide extract from it. The peptides were separated by size-exclusion using fast protein liquid chromatography, and the low molecular weight fraction was analysed by nanoscale liquid chromatography-Orbitrap coupled with tandem mass spectrometry and de novo sequencing. We selected 23 peptide sequences containing between 6 and 9 amino acids and molecular masses ranging 698–1017 Da. Those peptides were chemically synthesised and their angiotensin-converting enzyme (ACE) inhibitory activity was studied in vitro. Seven peptides showed a strong activity, with half maximal inhibitory concentration (IC50) <10 µm. The antihypertensive effects of the four most active synthesised ACE inhibitor peptides were studied in spontaneously hypertensive rats (SHR). Acute oral administration of synthetic peptides RDGGYCC and CCGNAVPQ showed antihypertensive activity in SHR. We conclude that unfiltered VOO naturally contains low molecular weight peptides with specific ACE inhibitory activity and antihypertensive effects in SHR.

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