Angiotensin I-Converting Enzyme (ACE) Inhibitory and Antioxidant Activity of Umami Peptides after In Vitro Gastrointestinal Digestion

2020 ◽  
Vol 68 (31) ◽  
pp. 8232-8241 ◽  
Author(s):  
Li Hao ◽  
Xinchang Gao ◽  
Tingyi Zhou ◽  
Jinxuan Cao ◽  
Yangying Sun ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Gastrointestinal Digestion ◽  
Angiotensin I Converting Enzyme ◽  
In Vitro Gastrointestinal Digestion ◽  
Ace Inhibitory

scholarly journals Multivesicular Liposomes for the Sustained Release of Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides from Peanuts: Design, Characterization, and In Vitro Evaluation

Molecules ◽  
2019 ◽  
Vol 24 (9) ◽  
pp. 1746 ◽  
Author(s):  
Ning Li ◽  
Aimin Shi ◽  
Qiang Wang ◽  
Guoquan Zhang
Keyword(s):  
Drug Delivery ◽  
Zeta Potential ◽  
Sustained Release ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Release Drug ◽  
Ace Inhibitory

The multivesicular liposome (MVL) provides a potential delivery approach to avoid the destruction of the structure of drugs by digestive enzymes of the oral cavity and gastrointestinal system. It also serves as a sustained-release drug delivery system. In this study, we aimed to incorporate a water-soluble substance into MVLs to enhance sustained release, prevent the destruction of drugs, and to expound the function of different components and their mechanism. MVLs were prepared using the spherical packing model. The morphology, structure, size distribution, and zeta potential of MVLs were examined using an optical microscope (OM), confocal microscopy (CLSM), transmission electron cryomicroscope (cryo-EM) micrograph, a Master Sizer 2000, and a zeta sizer, respectively. The digestion experiment was conducted using a bionic mouse digestive system model in vitro. An in vitro release and releasing mechanism were investigated using a dialysis method. The average particle size, polydispersity index, zeta potential, and encapsulation efficiency are 47.6 nm, 1.880, −70.5 ± 2.88 mV, and 82.00 ± 0.25%, respectively. The studies on the controlled release in vitro shows that MVLs have excellent controlled release and outstanding thermal stability. The angiotensin I-converting enzyme (ACE) inhibitory activity of ACE-inhibitory peptide (AP)-MVLs decreased only 2.84% after oral administration, and ACE inhibitory activity decreased by 5.03% after passing through the stomach. Therefore, it could serve as a promising sustained-release drug delivery system.

scholarly journals Angiotensin-I-Converting Enzyme Inhibitory and Antioxidant Activities of Protein Hydrolysate from Muscle of Barbel (Barbus callensis)

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Assaad Sila ◽  
Anissa Haddar ◽  
Oscar Martinez-Alvarez ◽  
Ali Bougatef
Keyword(s):  
Antioxidant Activities ◽  
Muscle Protein ◽  
Protein Hydrolysate ◽  
Radical Scavenging ◽  
Reducing Power ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

The present study investigated angiotensin-I-converting enzyme (ACE) inhibitory and antioxidant activities of barbel muscle protein hydrolysate prepared with Alcalase. The barbel muscle protein hydrolysate displayed a high ACE inhibitory activity (CI50=0.92 mg/mL). The antioxidant activities of protein hydrolysate at different concentrations were evaluated using variousin vitroantioxidant assays, including 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical method and reducing power assay. The barbel muscle protein hydrolysate exhibited an important radical scavenging effect and reducing power. These results obtained byin vitrosystems obviously established the antioxidant potency of barbel hydrolysate to donate electron or hydrogen atom to reduce the free radical. Furthermore, these bioactive substances can be exploited into functional foods or used as source of nutraceuticals.

scholarly journals Angiotensin I-converting Enzyme (ACE) Inhibitory Activity and Chemical Composition of Alchemilla Viridiflora Rothm.

2021 ◽  
Author(s):  
Jelena Radović ◽  
Relja Suručić ◽  
Marjan Niketić ◽  
Tatjana Kundakovic-Vasovic
Keyword(s):  
Inhibitory Activity ◽  
Methanol Extract ◽  
Flavonoid Glycosides ◽  
Herbaceous Plant ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Abstract Alchemilla viridiflora Rothm., Rosaceae is a herbaceous plant widespread in central Greece, Bulgaria, North Macedonia and Serbia with Kosovo. LC-MS analysis leads to the identification of 20 compounds in methanol extract, mainly ellagitannins and flavonoid glycosides. Considering that different plant extracts were traditionally used for treatment of hypertension and that some of the analyzed methanol extract constituents possess beneficial cardiovascular effects, we hypothesized that some of these effects are achieved through inhibition of angiotensin I-converting enzyme (ACE). The dose-dependent activities ACE inhibitory activity of A. viridiflora and miquelianin were observed with an IC50 of 2.51 ± 0.00 µg/ml of A. viridiflora compared to IC50 of 2.59 ± 0.00 µg/mL for miquelianin. Contribution of the single compounds to the tested activity was further analyzed through the in silico experimental approach. Computational docking results showed that tiliroside, ellagic acid pentose and galloyl-HHDP-glucose exhibited even better binding affinity for ACE active site than miquelianin, which ACE activity was confirmed by an in vitro assay.

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