Macroporous resin purification of grass carp fish (Ctenopharyngodon idella) scale peptides with in vitro angiotensin-I converting enzyme (ACE) inhibitory ability

2009 ◽  
Vol 117 (3) ◽  
pp. 387-392 ◽  
Author(s):  
Fengxiang Zhang ◽  
Zhang Wang ◽  
Shiying Xu
Keyword(s):  
Grass Carp ◽  
Ctenopharyngodon Idella ◽  
Converting Enzyme ◽  
Macroporous Resin ◽  
Angiotensin I ◽  
Inhibitory Ability ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory ◽  
Carp Fish

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.

scholarly journals Studies on angiotensin I converting enzyme (ACE) inhibitory effect of imidapril. (I). Inhibition of various tissue ACEs in vitro.

1992 ◽  
Vol 100 (1) ◽  
pp. 39-45 ◽  
Author(s):  
Takeshi SUGAYA ◽  
Satoshi MINOBE ◽  
Tomoyasu TANIGUCHI ◽  
Yoshikatsu HASHIMOTO ◽  
Masami KUBO ◽  
...  
Keyword(s):  
Inhibitory Effect ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

scholarly journals Bioavailability of angiotensin I converting enzyme inhibitory peptides

2004 ◽  
Vol 92 (3) ◽  
pp. 357-366 ◽  
Author(s):  
Vanessa Vermeirssen ◽  
John Van Camp ◽  
Willy Verstraete
Keyword(s):  
Blood Pressure ◽  
Antihypertensive Effect ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

Hypertension or high blood pressure is a significant health problem worldwide. Bioactive peptides that inhibit angiotensin I converting enzyme (ACE) in the cardiovascular system can contribute to the prevention and treatment of hypertension. These ACE inhibitory peptides are derived from many food proteins, especially milk proteins. An ACE inhibitory activity in vitro does not always imply an antihypertensive effect in vivo. Even if it does, it is very difficult to establish a direct relationship between in vitro and in vivo activity. This is mainly due to the bioavailability of the ACE inhibitory peptides after oral administration and the fact that peptides may influence blood pressure by mechanisms other than ACE inhibition. To exert an antihypertensive effect after oral ingestion, ACE inhibitory peptides have to reach the cardiovascular system in an active form. Therefore, they need to remain active during digestion by human proteases and be transported through the intestinal wall into the blood. The bioavailability of some ACE inhibitory peptides has been studied. It is also known that (hydroxy)proline-containing peptides are generally resistant to degradation by digestive enzymes. Peptides can be absorbed intact through the intestine by paracellular and transcellular routes, but the potency of the bioactivity after absorption is inversely correlated to chain length. In addition, some strategies are proposed to increase the bioavailability of ACE inhibitory peptides. Further research into the bioavailability of ACE inhibitory peptides will lead to the development of more effective ACE inhibitory peptides and foods.

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