scholarly journals Antioxidant and ACE-inhibitory activities of hydrolysates obtained from lupin and faba bean proteins via enzymatic hydrolysis and fermentation

2020 ◽  
Vol 12 (2) ◽  
pp. 99-114
Author(s):  
Blanca Elizabeth Hernández-Rodríguez ◽  
Eleazar Aguirre-Mandujano ◽  
Arely Prado-Barragán ◽  
Guillermo Ismael Koh-Kantún ◽  
Consuelo Lobato-Calleros
Keyword(s):  
Faba Bean ◽  
Radical Scavenging Activity ◽  
Radical Scavenging ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Native Proteins ◽  
Health Promoting ◽  
Inhibitory Activities ◽  
Ace Inhibitory

Introduction: Legumes and pseudocereals protein hydrolysates have been recognized as having improved potential health-promoting properties as compared with native proteins. Objectives: 1) Produce bioactive hydrolysates from lupin and faba bean proteins by enzymatic hydrolysis (EH) and solid-state fermentation (SF), 2) compare the angiotensin converting enzyme (ACE)-inhibitory and antioxidant activities of the hydrolysates and 3) evaluate the effect of in vitro gastrointestinal digestion on the antioxidant and antihypertensive activities of the hydrolysates. Methodology: Hydrolysates from proteins of faba bean (Vicia faba) and lupin (Lupinus gredensis) were obtained by EH using Flavourzyme and SF by Aspergillus niger. The antioxidant and ACE-inhibitory activities of the hydrolysates were assessed. Results: All the hydrolysates presented DPPH radical scavenging activity, with IC50 ranging from 1.23-2.08 mgprotein·mL-1. Only EH and SF hydrolysates obtained from lupin proteins had ACE-inhibitory activity (IC50: 2.39 and 14.08 mgprotein·mL-1, respectively). Radical scavenging activity hydrolysates was significantly reduced after in vitro gastrointestinal digestion, while ACE-inhibitory activity showed variable behavior. Study limitations: Specific molecules responsible for the in vitro health-promoting properties should be identified. Originality: Relevant information is provided on health-promoting attributes of faba bean and lupin hydrolysates obtained by EH and SF. Conclusions: EH and SF improved the health-promoting properties of faba bean and lupin native proteins.

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.

scholarly journals Evaluation of Selected Culinary-Medicinal Mushrooms for Antioxidant and ACE Inhibitory Activities

2012 ◽  
Vol 2012 ◽  
pp. 1-12 ◽  
Author(s):  
Noorlidah Abdullah ◽  
Siti Marjiana Ismail ◽  
Norhaniza Aminudin ◽  
Adawiyah Suriza Shuib ◽  
Beng Fye Lau
Keyword(s):  
Antioxidant Capacity ◽  
Radical Scavenging Activity ◽  
Schizophyllum Commune ◽  
Radical Scavenging ◽  
Reducing Power ◽  
Mushroom Species ◽  
Medicinal Mushrooms ◽  
Inhibitory Activities ◽  
Ace Inhibitory

Considering the importance of diet in prevention of oxidative stress-related diseases including hypertension, this study was undertaken to evaluate thein vitroantioxidant and ACE inhibitory activities of selected culinary-medicinal mushrooms extracted by boiling in water for 30 min. Antioxidant capacity was measured using the following assays: DPPH free radical scavenging activity,β-carotene bleaching, inhibition of lipid peroxidation, reducing power ability, and cupric ion reducing antioxidant capacity (CUPRAC). Antioxidant potential of each mushroom species was calculated based on the average percentages relative to quercetin and summarized as Antioxidant Index (AI).Ganoderma lucidum(30.1%),Schizophyllum commune(27.6%), andHericium erinaceus(17.7%) showed relatively high AI. Total phenolics in these mushrooms varied between 6.19 to 63.51 mg GAE/g extract. In the ACE inhibitory assay,G. lucidumwas shown to be the most potent species (IC50= 50 μg/mL). Based on our findings, culinary-medicinal mushrooms can be considered as potential source of dietary antioxidant and ACE inhibitory agents.

scholarly journals Bioactivity of Hydrolysates Obtained from Chicken Egg Ovalbumin Using Artichoke (Cynara scolymus L.) Proteases

Foods ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 246
Author(s):  
Estefanía Bueno-Gavilá ◽  
Adela Abellán ◽  
Francisco Girón-Rodríguez ◽  
José María Cayuela ◽  
Luis Tejada
Keyword(s):  
Inhibitory Activity ◽  
Radical Scavenging Activity ◽  
Radical Scavenging ◽  
Ace Inhibitory Activity ◽  
Hydrolysis Time ◽  
Cynara Scolymus ◽  
Chicken Egg ◽  
In Vitro Hydrolysis ◽  
Ace Inhibitory

The aim of this work was to obtain chicken egg ovalbumin hydrolysates using aspartic proteinases present in extracts from the artichoke flower (Cynara scolymus L.) and evaluate their antioxidant, antimicrobial, and angiotensin I-converting enzyme (ACE) inhibitory activity in vitro. Hydrolysis time and molecular weight (<3 kDa) had a significant influence on the hypertensive and antioxidant activity of the hydrolysates. The <3 kDa fraction of the 16 h hydrolysate had an ACE inhibitory activity with an IC50 of 64.06 µg peptides/mL. The fraction <3 kDa of ovalbumin hydrolysate at 2 h of hydrolysis showed a DPPH radical scavenging activity of 30.27 µM of Trolox equivalents/mg peptides. The fraction <3 kDa of the hydrolysate of 16 h had an ABTS+ caption activity of 4.30 mM of Trolox equivalents/mg peptides. The fraction <3 kDa of the hydrolysate of 2 h had an iron (II) chelating activity of 32.18 µg peptides/mL. From the peptide sequences identified in the hydrolysates, we detected four peptides (from the BIOPEP database) that were already in their bioactive form (IAAEVYEHTEGSTTSY, HLFGPPGKKDPV, PIAAEVYEHTEGSTTSY, and YAEERYPIL), and are reported to display antioxidant and ACE inhibitory activity.

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.

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.

scholarly journals IN VITRO ANTI-DIABETIC AND ANTI-OXIDANT ACTIVITIES OF ETHANOL EXTRACT OF TINOSPORA SINENSIS

2017 ◽  
Vol 9 (2) ◽  
pp. 42 ◽  
Author(s):  
Anindita Banerjee ◽  
Bithin Maji ◽  
Sandip Mukherjee ◽  
Kausik Chaudhuri ◽  
Tapan Seal
Keyword(s):  
Plant Extract ◽  
Antioxidant Activities ◽  
Radical Scavenging Activity ◽  
Radical Scavenging ◽  
Reducing Power ◽  
Ethanol Extract ◽  
Total Phenolic ◽  
Inhibitory Activities ◽  
Ethanol Extracts

Objective: The aim of the present study was to evaluate the alpha (α)-amylase and alpha (α)-glucosidase inhibitory activities and in vitro antioxidant activities of the 80 % aqueous ethanol extracts of Tinosporasinensis Lour (Merr.).Methods: The 80% aq. ethanol extract of the plant was prepared. The plant extract was examined for its antioxidant activity by using free radical 1,1-diphenyl-2-picryl hydrazyl (DPPH) scavenging method, ABTS radical scavenging ability, reducing power capacity, estimation of total phenolic content, flavonoid content and flavonol content. Different concentrations (2, 4, 8,10and 15 μg/ml) of the extract was subjected to α-amylase inhibitory and α-glucosidase inhibitory activities and IC50were calculated.Results: The study revealed that the different concentrations of the plant extract possessed a very good amount of total phenolics, flavonoid and flavonol and exhibited potent radical scavenging activity using DPPH and ABTS as a substrate. The ethanol extracts exhibited significant α-amylase and α-glucosidase inhibitory activities with an IC50 value1.093µg and 1.04µg dry extract respectively and well compared with standard acarbose drug.Conclusion: Thus, it could be concluded that due to the presence of antioxidant components the plant extracts could be used for the treatment of hyperglycemia, diabetes and the related condition of oxidative stress. This knowledge will be useful in finding more potent components from the natural resources for the clinical development of antidiabetic therapeutics.

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.

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