scholarly journals Angiotensin-converting enzyme (ACE) inhibitory activity of Solanum torvum and isolation of a novel methyl salicylate glycoside

2014 ◽  
Vol 11 ◽  
pp. 557-562 ◽  
Author(s):  
Arunee Simaratanamongkol ◽  
Kaoru Umehara ◽  
Hiroki Niki ◽  
Hiroshi Noguchi ◽  
Pharkphoom Panichayupakaranant
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Inhibitory Activity ◽  
Methyl Salicylate ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Solanum Torvum ◽  
Ace Inhibitory

scholarly journals The Potential Angiotensin-Converting Enzyme Inhibitory Activity of Oleanolic Acid in the Hydroethanolic Extract of Crataegus monogyna Jacq

2006 ◽  
Vol 1 (5) ◽  
pp. 1934578X0600100 ◽  
Author(s):  
Everaldo Attard ◽  
Henrietta Attard
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Oleanolic Acid ◽  
Inhibitory Activity ◽  
Acid Group ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Crataegus Monogyna ◽  
Triterpenic Acids ◽  
Hydroethanolic Extract ◽  
Ace Inhibitory

The hydroethanolic extract of Crataegus monogyna was studied for its chemical constitution and angiotensin-converting enzyme (ACE) inhibitory activity. The extract contained triterpenic acids, flavonoids and coumarins. The ACE inhibitory activity was studied using captropril, as a control drug, and oleanolic acid, as a constituent of the hydroethanolic extract and a member of the triterpenic acid group. The hydroethanolic extract and oleanolic acid showed higher IC50 values (335.00 μg/mL and 3.61 μM, respectively) in comparison to captopril (46.9 nM). However, these results indicate the anti-ACE activity of oleanolic acid and the triterpenic acids, which has not been demonstrated earlier for hawthorn extracts. In previous studies, the ACE inhibitory activity of C. monogyna extracts was always attributed to flavonoids and proanthocyanidins.

The synthesis and Angiotensin Converting Enzyme (ACE) inhibitory activity of chalcones and their pyrazole derivatives

2010 ◽  
Vol 20 (6) ◽  
pp. 1990-1993 ◽  
Author(s):  
Marco Bonesi ◽  
Monica R. Loizzo ◽  
Giancarlo A. Statti ◽  
Sylvie Michel ◽  
François Tillequin ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Inhibitory Activity ◽  
Pyrazole Derivatives ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Ace Inhibitory

Insects as source of angiotensin converting enzyme inhibitory peptides

2017 ◽  
Vol 3 (4) ◽  
pp. 231-240 ◽  
Author(s):  
A. Cito ◽  
M. Botta ◽  
V. Francardi ◽  
E. Dreassi
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Inhibitory Activity ◽  
Bioactive Peptides ◽  
Hypertension Treatment ◽  
Converting Enzyme ◽  
Oecophylla Smaragdina ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

Hypertension is well known as one of the major risk for cardiovascular diseases which annually affect millions of people. The angiotensin converting enzyme (ACE) plays a key role in blood pressure regulation process. Indeed, hypertension treatment by synthetic ACE inhibitors (e.g. captopril, lisinopril and ramipril) is effective; however, their use can cause serious side effects, such as hypotension, cough, reduced renal function and angioedema. Thus, research was focused on natural ACE inhibitory peptides sources such as foodstuffs and also, more recently, edible insects. In the last decades, ACE inhibitory activity has been detected in protein hydrolysates from insect species belonging to the orders of Coleoptera, Diptera, Hymenoptera, Lepidoptera and also Orthoptera. Further investigations led to identify specific ACE inhibitory peptides from the silkworm Bombyx mori (Lepidoptera: Bombycidae), the yellow mealworm Tenebrio molitor (Coleoptera: Tenebrionidae), the cotton leafworm Spodoptera littoralis (Lepidoptera: Noctuidae) and also from the weaver ant Oecophylla smaragdina (Hymenoptera: Formicidae). Even if ACE inhibitory activity of these bioactive peptides has been in vitro assayed and is comparable to those of some bioactive peptides derived from other animal protein sources, the in vivo effectiveness of most of these bioactive peptides still needs to be confirmed. The aim of this review is to present an outline of the currently available data on the potential use of insects for hypertension treatment with a focus on the ACE inhibitory peptides identified in these invertebrates to date.

scholarly journals Bioactive properties of protein hydrolysate of cottonseed byproduct: antioxidant, antimicrobial, and angiotensin‐converting enzyme (ACE) inhibitory activity

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Mariana Buranelo Egea ◽  
Josemar Gonçalves de Oliveira Filho ◽  
Ailton Cesar Lemes ◽  
Erika Valencia-Mejia ◽  
Katia Flavia Fernandes ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Inhibitory Activity ◽  
Protein Hydrolysate ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Bioactive Properties ◽  
Ace Inhibitory

scholarly journals High protein yogurt with addition of Lactobacillus helveticus: Peptide profile and angiotensin-converting enzyme ACE-inhibitory activity

2020 ◽  
Vol 333 ◽  
pp. 127482 ◽  
Author(s):  
Flávia Giacometti Cavalheiro ◽  
Débora Parra Baptista ◽  
Bruno Domingues Galli ◽  
Fernanda Negrão ◽  
Marcos Nogueira Eberlin ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Inhibitory Activity ◽  
High Protein ◽  
Lactobacillus Helveticus ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Peptide Profile ◽  
Ace Inhibitory

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.

THE PHYSICOCHEMICAL CHARACTERISTICS AND ANGIOTENSIN CONVERTING ENZYME (ACE) INHIBITORY ACTIVITY OF SKIPJACK TUNA (Katsuwonus pelamis) “BAKASANG”

2016 ◽  
Vol 78 (4-2) ◽  
Author(s):  
Max Robinson Wenno ◽  
Eddy Suprayitno ◽  
Aulanni’am Aulanni’am ◽  
Hardoko Hardoko
Keyword(s):  
Amino Acid ◽  
Angiotensin Converting Enzyme ◽  
Inhibitory Activity ◽  
Enzyme Inhibitor ◽  
Physicochemical Characteristics ◽  
Chemical Characteristics ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Physical And Chemical ◽  
Ace Inhibitory

Bakasang is a traditional fermented fish product which is often used as condiments. This study aimed to determine the physical and chemical characteristics and potential ACE (Angiotensin Converting Enzyme) inhibitor of bakasang. Color and viscosity were physical characteristics measured in which color was presented in value of L* (36.05), a* (18.76), b* (15.65), while viscosity value was 6 950 cP. The result of chemical characteristics including salinity, acidity, pH, TVB-N and LAB were 72 %, 2.56 %, 4.66, 36.88 mg N per 100 g and 3.32 log CFU g–1 respectively. Proximate and amino acid compositions analysis were also identified, resulting in 14.77 % protein, 1.11 % fat, 57.15 % moisture, 25.97 % ash and 1.00 % carbohydrate while the predominant amino acid found was histidine. The ACE inhibitory activity of the isolated bioactive peptides of bakasang was 68.80 %.

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