Angiotensin I-converting enzyme inhibitory peptide from yellowfin sole (Limanda aspera) frame protein and its antihypertensive effect in spontaneously hypertensive rats

Jung, Won‐Kyo; Mendis, Eresha; Je, Jae‐Young; Park, Pyo-Jam; Son, Byeng Wha; Kim, Hyoung Chin; Choi, Yang Kyu; Kim, Se-Kwon

doi:10.1016/j.foodchem.2004.09.048

Cited by 268 publications

(139 citation statements)

References 31 publications

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“…The IC 50 value of FPHPe was 0.57 mg/mL, which was similar to the IC 50 value of pepsin-catalyzed krill ( Euphausia superba ) protein hydrolysate (0.58 mg/mL) [33] but lower than that of <5 kDa chymotrypsin hydrolysate from yellowfin sole ( Limanda aspera ) frame (0.88 mg/mL) [34]; the ACE-inhibitory activity of FPHPe was also stronger than the pepsin hydrolysate from sea squirt ( Styela plicata ) (IC 50 : 2.43 mg/mL) [35]. On the other hand, while SPHs showed weaker ACE inhibition effects, hydrolysis by serial protease-treatments may be a feasible way to overcome this obstacle.…”

Section: Resultsmentioning

confidence: 70%

Antihypertensive properties of tilapia (Oreochromis spp.) frame and skin enzymatic protein hydrolysates

Lin

Alashi

Aluko

et al. 2017

Food & Nutrition Research

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Proteins from tilapia frame and skin can potentially be precursors of antihypertensive peptides according to the result of BIOPEP analyses. The aim was to generate peptides with inhibitory effects against angiotensin-converting enzyme (ACE) and renin from tilapia frame and skin protein isolates (FPI and SPI). The most active hydrolysate was then tested for blood pressure-lowering ability in spontaneously hypertensive rats (SHRs). Tilapia frame and skin protein hydrolysates (FPHs and SPHs) were respectively produced from FPI and SPI hydrolysis using pepsin, papain, or bromelain. The ACE-inhibitory activities of tilapia protein hydrolysates with varying degree of hydrolysis (DH) were evaluated. In order to enhance the activity, the hydrolysate was fractionated into four fractions (<1 kDa, 1–3 kDa, 3–5 kDa, and 5–10 kDa) and the one with the greatest ability to inhibit in vitro ACE and renin activities was subjected to oral administration (100 mg/kg body weight) to SHRs. Systolic and diastolic blood pressure (SBP and DBP), mean arterial pressure (MAP), and heart rates (HR) were subsequently measured within 24 h. The pepsin-hydrolyzed FPH (FPHPe) with the highest DH (23%) possessed the strongest ACE-inhibitory activity (IC50: 0.57 mg/mL). Its <1 kDa ultrafiltration fraction (FPHPe1) suppressed both ACE (IC50: 0.41 mg/mL) and renin activities more effectively than larger peptides. In addition, FPHPe1 significantly (p < 0.05) reduced SBP (maximum −33 mmHg), DBP (maximum −24 mmHg), MAP (maximum −28 mmHg), and HR (maximum −58 beats) in SHRs. FPHPe1 showed both in vitro and in vivo antihypertensive effects, which suggest tilapia processing coproducts may be valuable protein raw materials for producing antihypertensive peptides.

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Section: Resultsmentioning

confidence: 70%

Antihypertensive properties of tilapia (Oreochromis spp.) frame and skin enzymatic protein hydrolysates

Lin

Alashi

Aluko

et al. 2017

Food & Nutrition Research

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“…It is considered a high risk factor for such complications as arteriosclerosis, stroke, myocardial infarction and end-stage renal disease (Jung et al, 2006).…”

Section: Ace Inhibitory and Antihypertensive Effectmentioning

confidence: 99%

“…Therefore, special attention has been given to ACE inhibitory effects of nutraceuticals from bio-resources. Bioactive peptides from natural resources have been found to have a high level of ACE-inhibitory and antihypertensive effects (Je et al, 2005a, b, c;Jung et al, 2006;Nii et al, 2008;Lee et al, 2010;Yamamoto, 2010;Adje et al, 2011;Norris and FitzGerald, 2013;Singh et al, 2014;Mohanty et al, 2015;Capriotti et al, 2015;Esteve et al, 2015;El Hatmi et al, 2016). These peptides are very valuable because they have variety of functions and they are easily absorbed in the body and therefore, they can potentially be considered a great alternative for the synthetic antihypertensive drugs (Lee et al, 2010).…”

Section: Ace Inhibitory and Antihypertensive Effectmentioning

confidence: 99%

Peptides: Production, bioactivity, functionality, and applications

Hajfathalian

Ghelichi

Moreno

et al. 2017

Critical Reviews in Food Science and Nutrition

138

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Production of peptides with various effects from proteins of different sources continues to receive academic attention. Researchers of different disciplines are putting increasing efforts to produce bioactive and functional peptides from different sources such as plants, animals, and food industry by-products. The aim of this review is to introduce production methods of hydrolysates and peptides and provide a comprehensive overview of their bioactivity in terms of their effects on immune, cardiovascular, nervous, and gastrointestinal systems. Moreover, functional and antioxidant properties of hydrolysates and isolated peptides are reviewed. Finally, industrial and commercial applications of bioactive peptides including their use in nutrition and production of pharmaceuticals and nutraceuticals are discussed.

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“…However, a medicine is accompanied by side effects. Many investigators (1)(2)(3)(4)(5) have attempted to prepare and isolate an ACE inhibitor in various food substances. We have isolated and purified nicotianamine (NA) from several kinds of plants ( 6 -8 ).…”

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confidence: 99%

Nicotianamine Preferentially Inhibits Angiotensin I-Converting Enzyme

Hayashi

Kimoto

2007

J Nutr Sci Vitaminol

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Summary Nicotianamine (NA) is a nonprotein amino acid that inhibits the angiotensin I-converting enzyme (ACE) in the renin-angiotensin system (RAS). The purpose of this study is to prove that NA contributes to the suppression of hypertension by preferential inhibition of ACE. On comparison with EDTA-a chelator-we found that the inhibition pattern of NA for ACE is that of mixed inhibition and that NA exhibits weak chelation effects for zinc, copper, and cobalt ions. Therefore, we investigated whether NA inhibited zinc-containing enzymes other than ACE in vitro. The results revealed that NA does not inhibit leucine aminopeptidase or alkaline phosphatase in rat serum. On the other hand, NA demonstrated specific inhibitory effects for rat serum ACE and aortic ACE. These results suggest that the preferential inhibition of circulatory and tissue ACE by NA can contribute to the suppression of hypertension. Key Words nicotianamine, angiotensin I-converting enzyme (ACE), renin-angiotensin system (RAS), hypertensionThe renin-angiotensin system (RAS) plays an important role in the maintenance of blood pressure and fluid and electrolyte homeostasis. The primary enzymes involved in this process are renin (EC 3.4.23.15) and angiotensin I-converting enzyme (ACE) (EC 3.4.15.1). ACE is a zinc-dependent carboxypeptidase that hydrolyzes di-and tri-peptides from the C-terminus of peptides. Each active site of the enzyme appears to bind one atom of zinc; this is crucial for its catalytic activity. Zinc is considered to participate directly in the catalysis of peptide substrates since its replacement with other divalent cations affects the rate of conversion with little effect on the substrate affinity.ACE inhibitors are now widely used for the treatment of patients with hypertensive disorders. However, a medicine is accompanied by side effects. Many investigators ( 1-5 ) have attempted to prepare and isolate an ACE inhibitor in various food substances. We have isolated and purified nicotianamine (NA) from several kinds of plants ( 6 -8 ). It has been reported that a longterm administration of NA exerts an antihypertensive effect in spontaneously hypertensive rats (SHR) ( 7 ) and that it is absorbed from the intestine and detected in the blood after administration into the stomach in Tsukuba hypertensive mice (THM) ( 8 ). Furthermore, we established a quick and simple assay system for identifying the presence of NA in plants using the high performance liquid chromatography (HPLC) method ( 9 ). If it can be proved that NA is absorbed from the intestinal tract and that it effectively affects the RAS that regulates the blood pressure, the prevention or improvement of hypertension without depending on a drug is possible through adequate daily dietary intake.NA, a chelator of metals, is ubiquitously present in higher plants. It chelates metal ions-such as iron-in plants and mediates their transport; further, it is considered to contribute to their stability within cells ( 10 ).In this study, we examined the chelation properties of NA with...

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Angiotensin I-converting enzyme inhibitory peptide from yellowfin sole (Limanda aspera) frame protein and its antihypertensive effect in spontaneously hypertensive rats

Cited by 268 publications

References 31 publications

Antihypertensive properties of tilapia (Oreochromis spp.) frame and skin enzymatic protein hydrolysates

Antihypertensive properties of tilapia (Oreochromis spp.) frame and skin enzymatic protein hydrolysates

Peptides: Production, bioactivity, functionality, and applications

Nicotianamine Preferentially Inhibits Angiotensin I-Converting Enzyme

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