scholarly journals Enhancement or Suppression of ACE Inhibitory Activity by a Mixture of Tea and Foods for Specified Health Uses (FOSHU) That Are Marketed as “Support for Normal Blood Pressure”

2011 ◽  
Vol 2011 ◽  
pp. 1-4 ◽  
Author(s):  
Isao Murakami ◽  
Hiroyuki Hosono ◽  
Shigeto Suzuki ◽  
Junichi Kurihara ◽  
Fumio Itagaki ◽  
...  
Keyword(s):  
Blood Pressure ◽  
Inhibitory Activity ◽  
Tea Polyphenols ◽  
Normal Blood Pressure ◽  
Ace Inhibitory Activity ◽  
Active Peptides ◽  
Time Points ◽  
Combined Administration ◽  
Inhibitory Activities ◽  
Ace Inhibitory

The ACE inhibitory activities of mixtures of FOSHUs (Healthya, Goma-Mugicha, Lapis Support and Ameal) were examined in order to identify any antihypertensive interactions. Among combinations of Healthya with other samples that contain active peptides, only that with Ameal was found to have no inhibitory activity. Enhanced activity was observed in 2 other mixtures. The activity of a mixture of tea polyphenols and the whey component extracted from an Ameal solution was significantly decreased, thus demonstrating that whey protein lowered the ACE inhibitory activity of Healthya. Although oral administration of tea polyphenols alone significantly decreased SBP in SHR at 2 and 4 hr, combined administration with Ameal failed to decrease SBP at the same time points. In conclusion, the simultaneous intake of tea and FOSHUs that contain active peptides might affect daily self-antihypertensive management via enhancement or suppression of 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 Comparative Study of Angiotensin I-Converting Enzyme (ACE) Inhibition of Soy Foods as Affected by Processing Methods and Protein Isolation

Processes ◽  
2020 ◽  
Vol 8 (8) ◽  
pp. 978 ◽  
Author(s):  
Cíntia L. Handa ◽  
Yan Zhang ◽  
Shweta Kumari ◽  
Jing Xu ◽  
Elza I. Ida ◽  
...  
Keyword(s):  
Blood Pressure ◽  
Inhibitory Activity ◽  
Ace Inhibition ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Soy Foods ◽  
Inhibitory Capacity ◽  
Inhibitory Potential ◽  
Ace Inhibitory

Angiotensin converting enzyme (ACE) converts angiotensin I into the vasoconstrictor angiotensin II and eventually elevates blood pressure. High blood pressure is a major risk factor for heart disease and stroke. Studies show peptides present anti-hypertensive activity by ACE inhibition. During food processing and digestion, food proteins may be hydrolyzed and release peptides. Our objective was to determine and compare the ACE inhibitory potential of fermented and non-fermented soy foods and isolated 7S and 11S protein fractions. Soy foods (e.g., soybean, natto, tempeh, yogurt, soymilk, tofu, soy-sprouts) and isolated proteins were in vitro digested prior to the determination of ACE inhibitory activity. Peptide molecular weight distribution in digested samples was analyzed and correlated with ACE inhibitory capacity. Raw and cooked soymilk showed the highest ACE inhibitory potential. Bacteria-fermented soy foods had higher ACE inhibitory activity than fungus-fermented soy food, and 3 day germinated sprouts had higher ACE inhibition than those germinated for 5 and 7 days. The 11S hydrolysates showed higher ACE inhibitory capacity than 7S. Peptides of 1–4.5 kDa showed a higher contribution to reducing IC50. This study provides evidence that soy foods and isolated 7S and 11S proteins may be used as functional foods or ingredients to prevent or control hypertension.

scholarly journals ACE Inhibitory Activity and Molecular Docking of Gac Seed Protein Hydrolysate Purified by HILIC and RP-HPLC

Molecules ◽  
2020 ◽  
Vol 25 (20) ◽  
pp. 4635
Author(s):  
Samuchaya Ngamsuk ◽  
Tzou-Chi Huang ◽  
Jue-Liang Hsu
Keyword(s):  
Liquid Chromatography ◽  
Molecular Docking ◽  
Amino Acid ◽  
Inhibitory Activity ◽  
Seed Proteins ◽  
Inhibition Mechanism ◽  
Ace Inhibitory Activity ◽  
Rp Hplc ◽  
Inhibitory Activities ◽  
Ace Inhibitory

Gac (Momordica cochinchinensis Spreng.) seed proteins (GSPs) hydrolysate was investigated for angiotensin I-converting enzyme (ACE) inhibitory activities. GSPs were hydrolyzed under simulated gastrointestinal digestion using a combination of enzymes, including pepsin, trypsin, and chymotrypsin. The screening of ACE inhibitory peptides from GSPs hydrolysate was performed using two sequential bioassay-guided fractionations, namely hydrophilic interaction liquid chromatography (HILIC) and reversed-phase high-performance liquid chromatography (RP-HPLC). Then, the peptides in the fraction with the highest ACE inhibitory activity were identified by LC-MS/MS. The flow-through (FT) fraction showed the most potent ACE inhibitory activity when HILIC fractionation was performed. This fraction was further separated using RP-HPLC, and the result indicated that fraction 8 (RP-F8) showed the highest ACE inhibitory activity. In the HILIC-FT/RP-F8 fraction, 14 peptides were identified using LC-MS/MS analysis coupled with de novo sequencing. These amino acid chains had not been recorded previously and their ACE inhibitory activities were analyzed in silico using the BIOPEP database. One fragment with the amino acid sequence of ALVY showed a significant ACE inhibitory activity (7.03 ± 0.09 µM). The Lineweaver-Burk plot indicated that ALVY is a competitive inhibitor. The inhibition mechanism of ALVY against ACE was further rationalized through the molecular docking simulation, which revealed that the ACE inhibitory activities of ALVY is due to interaction with the S1 (Ala354, Tyr523) and the S2 (His353, His513) pockets of ACE. Bibliographic survey allowed the identification of similarities between peptides reported as in gac fruit and other proteins. These results suggest that gac seed proteins hydrolysate can be used as a potential nutraceutical with inhibitory activity against ACE.

scholarly journals A Novel Angiotensin-I-Converting Enzyme (ACE) Inhibitory Peptide from Takifugu flavidus

Marine Drugs ◽  
2021 ◽  
Vol 19 (12) ◽  
pp. 651
Author(s):  
Yongchang Su ◽  
Shicheng Chen ◽  
Shuilin Cai ◽  
Shuji Liu ◽  
Nan Pan ◽  
...  
Keyword(s):  
Blood Pressure ◽  
Inhibitory Activity ◽  
Gel Chromatography ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptide ◽  
Ace Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Alcalase, neutral protease, and pepsin were used to hydrolyze the skin of Takifugu flavidus. The T. flavidus hydrolysates (TFHs) with the maximum degree of hydrolysis (DH) and angiotensin-I-converting enzyme (ACE)-inhibitory activity were selected and then ultra-filtered to obtain fractions with components of different molecular weights (MWs) (<1, 1–3, 3–10, 10–50, and >50 kDa). The components with MWs < 1 kDa showed the strongest ACE-inhibitory activity with a half-maximal inhibitory concentration (IC50) of 0.58 mg/mL. Purification and identification using semi-preparative liquid chromatography, Sephadex G-15 gel chromatography, RP-HPLC, and LC–MS/MS yielded one new potential ACE-inhibitory peptide, PPLLFAAL (non-competitive suppression mode; IC50 of 28 μmmol·L−1). Molecular docking and molecular dynamics simulations indicated that the peptides should bind well to ACE and interact with amino acid residues and the zinc ion at the ACE active site. Furthermore, a short-term assay of antihypertensive activity in spontaneously hypertensive rats (SHRs) revealed that PPLLFAAL could significantly decrease the systolic blood pressure (SBP) and diastolic blood pressure (DBP) of SHRs after intravenous administration. These results suggested that PPLLFAAL may have potential applications in functional foods or pharmaceuticals as an antihypertensive agent.

scholarly journals Partial Purification and Characterization of Bioactive Peptides from Cooked New Zealand Green-Lipped Mussel (Perna canaliculus) Protein Hydrolyzates

Foods ◽  
2020 ◽  
Vol 9 (7) ◽  
pp. 879
Author(s):  
Ramya Jayaprakash ◽  
Conrad O. Perera
Keyword(s):  
New Zealand ◽  
Inhibitory Activity ◽  
Bioactive Peptides ◽  
Protein Hydrolysate ◽  
Gel Filtration ◽  
Partial Purification ◽  
Ace Inhibitory Activity ◽  
Perna Canaliculus ◽  
Inhibitory Activities ◽  
Ace Inhibitory

Proteins from fresh New Zealand green-lipped mussels were hydrolyzed for 240 min using pepsin and alcalase. The extent of the hydrolysis, antioxidant, antimicrobial, and angiotensin-converting enzyme (ACE) inhibitory activities of each protein hydrolysate were investigated. Peptides obtained from pepsin hydrolysis after 30 min, named GPH, exhibited the highest antioxidant and ACE inhibitory activity, but no antimicrobial activity. Purification of the GPH using gel-filtration chromatography revealed that the protein fraction (GPH-IV*) containing peptides with a molecular weight (MW) below 5 kDa had the strongest antioxidant and ACE inhibitory activities. Further purification was done using reverse-phase HPLC (RP-HPLC) and the only major peak obtained (GPH-IV*-P2) had the highest antioxidant and ACE inhibitory activity. From this fraction, several bioactive peptides with an MW ≈ 5 kDa were identified using LC-MS and in silico analyses. This research highlights that green-lipped mussel protein hydrolysates could be used as a good source of bioactive peptides with potential therapeutic applications.

scholarly journals Blood Pressure-Lowering Peptides from Neo-Fermented Buckwheat Sprouts: A New Approach to Estimating ACE-Inhibitory Activity

PLoS ONE ◽  
2014 ◽  
Vol 9 (9) ◽  
pp. e105802 ◽  
Author(s):  
Masahiro Koyama ◽  
Seiji Hattori ◽  
Yoshihiko Amano ◽  
Masanori Watanabe ◽  
Kozo Nakamura
Keyword(s):  
Blood Pressure ◽  
Inhibitory Activity ◽  
Blood Pressure Lowering ◽  
Ace Inhibitory Activity ◽  
New Approach ◽  
Pressure Lowering ◽  
Ace Inhibitory

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 Changes in arterial blood pressure in hypertensive rats caused by long-term intake of milk fermented by Enterococcus faecalis CECT 5728

2005 ◽  
Vol 94 (1) ◽  
pp. 36-43 ◽  
Author(s):  
M. Miguel ◽  
B. Muguerza ◽  
E. Sánchez ◽  
M. A. Delgado ◽  
I. Recio ◽  
...  
Keyword(s):  
Blood Pressure ◽  
Inhibitory Activity ◽  
Tap Water ◽  
Fermented Milk ◽  
Negative Control ◽  
Hypertensive Rats ◽  
Ace Inhibitory Activity ◽  
Arterial Blood ◽  
Ace Inhibitory

We have evaluated the changes in arterial blood pressure caused in spontaneously hypertensive rats (SHR) by long-term intake of an Enterococcus faecalis CECT 5728-fermented milk with significant angiotensin-converting enzyme (ACE)-inhibitory activity. After being weaned, male 3-week-old SHR were randomized into five groups. Until the 20th week of life, rats in each group were given one of the following drinking fluids: tap water (negative control 1), a fermented milk without ACE-inhibitory activity (negative control 2), captopril (100 mg/kg) (positive control), the E. faecalis CECT 5728-fermented milk that had significant ACE-inhibitory activity, or Ca-enriched E. faecalis CECT 5728-fermented milk. Animals in the different groups were then given tap water as drinking fluid from the 20th to 25th week of life. Systolic blood pressure (SBP) and diastolic blood pressure (DBP) were measured weekly in the rats, from the 6th to 25th week of life, by the tail-cuff method. A definite decrease in SBP and DBP could be observed in the rats treated with captopril and also in the rats that received the E. faecalis CECT 5728-fermented milks. The greatest antihypertensive effect was observed when the pharmacological treatment was administered. The effect of the Ca-enriched fermented milk was slightly more accentuated and more constant than the effect of the E. faecalis CECT 5728-fermented milk that had not been enriched in Ca. SBP and DBP increased in the treated SHR when the corresponding antihypertensive treatment was removed. Fermentation of milk with E. faecalis CECT 5728 may therefore be a successful strategy to produce a functional food with antihypertensive activity.

scholarly journals Antioxidant, Angiotensin-Converting Enzyme Inhibitory Properties and Blood-Pressure-Lowering Effect of Rice Bran Protein Hydrolysates

Foods ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 812
Author(s):  
Inajara Beatriz Brose Piotrowicz ◽  
Marta Garcés-Rimón ◽  
Silvia Moreno-Fernández ◽  
Amaya Aleixandre ◽  
Myriam Salas-Mellado ◽  
...  
Keyword(s):  
Blood Pressure ◽  
Angiotensin Converting Enzyme ◽  
Rice Bran ◽  
Inhibitory Activity ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Rice Bran Protein ◽  
Defatted Rice Bran ◽  
Wky Rats ◽  
Ace Inhibitory

This research aimed to investigate the biological properties of different hydrolysates derived from industrial and laboratory defatted rice bran proteins. Industrial and laboratory defatted rice bran protein concentrates were hydrolyzed with alcalase or flavorzyme. The degree of hydrolysis (DH), oxygen radical absorbance capacity (ORAC), reducing power, total phenolic compounds (TPC), and angiotensin-converting enzyme (ACE) inhibitory activity, were determined in the hydrolysates and the molecular fractions lower than 3 kDa. Systolic blood pressure (SBP) was measured using the tail-cuff method before and after oral administration of 80 mg/kg of different rice bran protein hydrolysate (RBPH) fractions lower than 3 kDa in male spontaneously hypertensive rats (SHR) and normotensive Wistar–Kyoto (WKY) rats. The highest values of in vitro antioxidant activity and TPC were observed in RBPH with alcalase defatted by industry (RBPH2A), and, in all cases, these bioactivities were higher in the molecular fractions lower than 3 kDa. Once again, fractions lower than 3 kDa obtained with alcalase showed a potent ACE inhibitory activity (RBPH1A<3 and RBPH2A<3). The administration of RBPH1A<3 caused a significant decrease in the SBP in SHR, where the maximum decrease was reached at 8 h after administration. SBP in WKY rats was not modified after the administration of RBPH1A<3. These results suggest that the rice bran protein hydrolysates obtained from industry after treatment with alcalase could be an interesting source of bioactive peptides, with potential action on hypertension and other related pathologies.

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