Identification of water-soluble peptides in distilled spent grain and its angiotensin converting enzyme (ACE) inhibitory activity based on UPLC-Q-TOF-MS and proteomics analysis

2021 ◽  
Vol 353 ◽  
pp. 129521
Author(s):  
Dong Wei ◽  
Wen-lai Fan ◽  
Yan Xu
2018 ◽  
Vol 9 (5) ◽  
pp. 2755-2761 ◽  
Author(s):  
Wenzhu Zhao ◽  
Yuejiao Chen ◽  
Siyu Xue ◽  
Zhipeng Yu ◽  
Hanjie Yu ◽  
...  

Herein, the ability of ginger glycoproteins to inhibit the angiotensin-converting enzyme (ACE) is characterized.


2014 ◽  
Vol 11 ◽  
pp. 557-562 ◽  
Author(s):  
Arunee Simaratanamongkol ◽  
Kaoru Umehara ◽  
Hiroki Niki ◽  
Hiroshi Noguchi ◽  
Pharkphoom Panichayupakaranant

2006 ◽  
Vol 1 (5) ◽  
pp. 1934578X0600100 ◽  
Author(s):  
Everaldo Attard ◽  
Henrietta Attard

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.


2010 ◽  
Vol 20 (6) ◽  
pp. 1990-1993 ◽  
Author(s):  
Marco Bonesi ◽  
Monica R. Loizzo ◽  
Giancarlo A. Statti ◽  
Sylvie Michel ◽  
François Tillequin ◽  
...  

2015 ◽  
Vol 11 (5) ◽  
pp. 659-665
Author(s):  
Tuba Erkaya ◽  
Aykut Öztekin ◽  
Hasan Özdemir ◽  
Mustafa Şengül

Abstract Angiotensin converting enzyme (ACE)-inhibitory activity in water soluble extracts (WSEs) of kefir was investigated. Kefir was produced traditionally using kefir grains and stored at refrigerated temperature for 20 days. During storage period (on 1, 5, 10, 15 and 20 days) in vitro ACE-inhibitory activity in WSEs was determined. ACE was purified from human plasma to determine kinetic parameters. Purified ACE had a specific activity of 20.75 EU.mg−1, a yield of 16.6% with a factor of 22100. The inhibition effects of kefir on ACE increased at 15 storage days than other storage days. Some microbiological and physicochemical characteristics of kefir were also studied. Counts of presumptive LAB on M-17 and presumptive LAB on MRS in the kefir were about 108 CFU.ml−1 throughout the storage period. Yeast counts were lower than lactic acid bacteria counts and the average of the counts was approximately 106 log CFU.ml−1. Storage period had a significant effect (P < 0.05) on titratable acidity and pH values. On the contrary, it had no significant effect (P > 0.05) on viscosity and serum separation values of kefir.


2017 ◽  
Vol 3 (4) ◽  
pp. 231-240 ◽  
Author(s):  
A. Cito ◽  
M. Botta ◽  
V. Francardi ◽  
E. Dreassi

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.


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 ◽  
...  

2014 ◽  
Vol 81 (4) ◽  
pp. 394-402 ◽  
Author(s):  
Didem Sahingil ◽  
Ali A. Hayaloglu ◽  
Huseyin A. Kirmaci ◽  
Barbaros Özer ◽  
Osman Simsek

The effects of use of adjunct cultures (Lactobacillus helveticus and Lb. casei) and ripening temperatures (6 or 12 °C) on proteolysis and angiotensin-I converting enzyme (ACE)-inhibitory activity in white-brined cheeses were investigated during 120 d ripening. Proteolysis was monitored by urea-polyacrylamide gel electrophoresis (urea-PAGE) and reversed phase-HPLC (RP-HPLC) of water-insoluble and -soluble fractions of the cheeses, respectively. Urea-PAGE patterns of the samples revealed that the intensities of the bands representing casein fractions decreased in the experimental cheeses, being more pronounced in the cheeses made with adjunct cultures. Similarly, peptide profiles and the concentrations of individual and total free amino acids were influenced by both the adjunct cultures and ripening temperatures. The ACE-inhibitory activity of the water-soluble extracts of the cheeses were higher in the cheeses made using adjunct cultures (especially Lb. helveticus) and ripened at 12 °C. The ACE-inhibitory activity did not decrease during ripening. The contribution of Lb. helveticus to the development of proteolysis and ACE-inhibitory peptide activities were higher than that of Lb. casei. To conclude, the use of Lb. helveticus as adjunct culture in white-brined cheese and ripening at 12 °C would be recommended to obtain white-brined cheese with high ACE-I-inhibitory peptides activity and higher levels of preoteolysis.


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