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

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.

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Antioxidant and angiotensin-converting enzyme (ACE) inhibitory activity of thymosin alpha-1 (Thα1) peptide

Bioorganic Chemistry ◽

10.1016/j.bioorg.2019.04.003 ◽

2019 ◽

Vol 87 ◽

pp. 743-752 ◽

Cited By ~ 7

Author(s):

Jasmin Kharazmi-Khorassani ◽

Ahmad Asoodeh ◽

Hamid Tanzadehpanah

Keyword(s):

Angiotensin Converting Enzyme ◽

Inhibitory Activity ◽

Converting Enzyme ◽

Ace Inhibitory Activity ◽

Thymosin Alpha 1 ◽

Ace Inhibitory

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

Bioorganic & Medicinal Chemistry Letters ◽

10.1016/j.bmcl.2010.01.113 ◽

2010 ◽

Vol 20 (6) ◽

pp. 1990-1993 ◽

Cited By ~ 51

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

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Angiotensin I-Converting-Enzyme-Inhibitory and Antibacterial Peptides from Lactobacillus helveticus PR4 Proteinase-Hydrolyzed Caseins of Milk from Six Species

Applied and Environmental Microbiology ◽

10.1128/aem.69.9.5297-5305.2003 ◽

2003 ◽

Vol 69 (9) ◽

pp. 5297-5305 ◽

Cited By ~ 177

Author(s):

F. Minervini ◽

F. Algaron ◽

C. G. Rizzello ◽

P. F. Fox ◽

V. Monnet ◽

...

Keyword(s):

Inhibitory Activity ◽

Sodium Caseinate ◽

Lactobacillus Helveticus ◽

Converting Enzyme ◽

Angiotensin I ◽

Ace Inhibitory Activity ◽

Inhibitory Peptides ◽

Angiotensin I Converting Enzyme ◽

Ace Inhibitory Peptides ◽

Ace Inhibitory

ABSTRACT Sodium caseinates prepared from bovine, sheep, goat, pig, buffalo or human milk were hydrolyzed by a partially purified proteinase of Lactobacillus helveticus PR4. Peptides in each hydrolysate were fractionated by reversed-phase fast-protein liquid chromatography. The fractions which showed the highest angiotensin I-converting-enzyme (ACE)-inhibitory or antibacterial activity were sequenced by mass spectrum and Edman degradation analyses. Various ACE-inhibitory peptides were found in the hydrolysates: the bovine αS1-casein (αS1-CN) 24-47 fragment (f24-47), f169-193, and β-CN f58-76; ovine αS1-CN f1-6 and αS2-CN f182-185 and f186-188; caprine β-CN f58-65 and αS2-CN f182-187; buffalo β-CN f58-66; and a mixture of three tripeptides originating from human β-CN. A mixture of peptides with a C-terminal sequence, Pro-Gly-Pro, was found in the most active fraction of the pig sodium caseinate hydrolysate. The highest ACE-inhibitory activity of some peptides corresponded to the concentration of the ACE inhibitor (S)-N-(1-[ethoxycarbonyl]-3-phenylpropyl)-ala-pro maleate (enalapril) of 49.253 μg/ml (100 μmol/liter). Several of the above sequences had features in common with other ACE-inhibitory peptides reported in the literature. The 50% inhibitory concentration (IC50) of some of the crude peptide fractions was very low (16 to 100 μg/ml). Some identified peptides were chemically synthesized, and the ACE-inhibitory activity and IC50s were confirmed. An antibacterial peptide corresponding to β-CN f184-210 was identified in human sodium caseinate hydrolysate. It showed a very large spectrum of inhibition against gram-positive and -negative bacteria, including species of potential clinical interest, such as Enterococcus faecium, Bacillus megaterium, Escherichia coli, Listeria innocua, Salmonella spp., Yersinia enterocolitica, and Staphylococcus aureus. The MIC for E. coli F19 was ca. 50 μg/ml. Once generated, the bioactive peptides were resistant to further degradation by proteinase of L. helveticus PR4 or by trypsin and chymotrypsin.

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Insects as source of angiotensin converting enzyme inhibitory peptides

Journal of Insects as Food and Feed ◽

10.3920/jiff2017.0017 ◽

2017 ◽

Vol 3 (4) ◽

pp. 231-240 ◽

Cited By ~ 9

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.

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