• Asian-Australasian Journal of Animal Sciences
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• v.21 no.5
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• pp.732-737
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• 2008

This study developed a natural ingredient as a functional food possessing properties of attenuation of hypertension and cardiovascular hypertrophy. In a previous study hydrolysates obtained from chicken leg bone protein using Alcalase strongly inhibited angiotensin I converting enzyme (ACE) in vitro. In particular, hydrolysate (A4H) from four hours of incubation exhibited the highest ACE inhibitory activity (IC50 = 0.545 mg/ml). A4H was selected as a potent ACE inhibitor and orally administrated to spontaneously hypertensive rats (SHR) for eight weeks to investigate attenuating effects on age-related development of hypertension and cardiovascular hypertrophy. Results showed that treatment with A4H of SHRs attenuated the development of hypertension as effectively as the clinical antihypertensive drug captopril. Moreover, a significantly lower heart to body weight ratio and thinness of coronary arterial wall was observed in SHRs that had been treated with A4H or captopril. The results suggest that A4H can be utilized in developing an ACE inhibitor as a potential ingredient of functional foods to alleviate hypertension and cardiovascular hypertrophy.

• The Journal of Korean Medicine
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• v.31 no.1
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• pp.162-173
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• 2010

Objectives: In order to confirm a remedial effect and related influence of the clinic treatment by prescribing herb medicines to hypertensives experiencing angiotensin converting enzyme (ACE) inhibitor dosage and suffering from common side effect generally known as dry cough. Methods: 1. We selected the 19 patients who visited National Oriental Medical Center, from August 21, 2007 to August 16, 2008 and suffering from dry cough caused by taking ACE inhibitor, with no other possible diseases causing dry cough. 2. We separated the 19 patients into two groups (Type 1: Bi-Qi hie (脾氣虛) group prescribed Samchuljojung-tang & Type 2: Qi-hie dam-wul (氣虛痰鬱) group prescribed Samsoumgamibang). 3. We then observed the symptom level and post-treatment effect, and recorded changes of dry cough intensity level for each group. Results: 1. Type 1: In the survey of 12 patients, initial level recorded 16.33 at entry diagnosis, and next level meant changing of symptoms, recorded as 2.75 at Stage 1 and reaching 3.33 at Stage 2. 2. Type 2: 7 patients, with initial level recorded as 18.71 at entry diagnosis, and 1.86 at Stage 1 and reaching to 3.29 at Stage 2. 3. No additional prescriptions were issued at Stage 2 or afterwards, and final result indicates that the mean value ended at 3.95 in the total group. Conclusions: It is concluded that there is a significant remedial effect and related influence of the clinic treatment between the Oriental medicine treatment and one of the common side effects of ACE inhibitor, dry cough.

• The Korean Journal of Mycology
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• v.31 no.3
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• pp.148-154
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• 2003

Extracts from 52 samples of mushrooms were prepared by using water, ethanol and methanol, and then yields and angiotensin I-converting enzyme(ACE) inhibitory activity were investigated. Sample mushrooms contained crude proteins of $7.1{\sim}56.5%$, curde lipids of $0.2{\sim}4.4%$ and carbohydrates of $30.3{\sim}86.6%$. Among 52 samples, the water extract from fruiting body of Pholiota spp. ASI 24027 showed the highest extraction yield of 68%. Water extract of Pholiota spp. ASI 24012 fruiting body had potential ACE inhibitory activity of 66%. The optimal extraction condition of the ACE inhibitor from the fruiting bodyies of Pholiota spp. ASI 24012 was In water at $30^{\circ}C$ for 1 hr and ACE inhibitory activity was 67.6% on the condition with 0.2 mg of $IC_{50}$.

• Fisheries and Aquatic Sciences
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• v.15 no.3
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• pp.183-190
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• 2012

The purpose of this study was the purification and characterization of an angiotensin I converting enzyme (ACE) inhibitory peptide purified from enzymatic hydrolysates of rainbow trout Oncorhynchus mykiss muscle. After removal of lipid, the approximate composition analysis of the rainbow trout revealed 24.4%, 1.7%, and 68.3% for protein, lipid, and moisture, respectively. Among six hydrolysates, the peptic hydrolysate exhibited the highest ACE inhibitory activity. We attempted to purify ACE inhibitory peptides from peptic hydrolysate using high performance liquid chromatography on an ODS column. The $IC_{50}$ value of purified ACE inhibitory peptide was $63.9{\mu}M$. The amino acid sequence of the peptide was identified as Lys-Val-Asn-Gly-Pro-Ala-Met-Ser-Pro-Asn-Ala-Asn, with a molecular weight of 1,220 Da, and the Lineweaver-Burk plots suggested that they act as a competitive inhibitor against ACE. Our study suggested that novel ACE inhibitory peptides purified from rainbow trout muscle protein may be beneficial as anti-hypertension compounds in functional foods.

• YAKHAK HOEJI
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• v.37 no.1
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• pp.41-48
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• 1993

The effect of captopril on the lung angiotensin converting enzyme (ACE) was investigated after 3 weeks oral administration (120~160 mg/kg/day) through drinking water in SpragueDawley rats. On the $^{125}$I-351A, an ACE inhibitor, binding assay in the isolated perpused lungs, the number of ACE molecules at the intrapulmonary endothelial cell surface was significantly decreased (p<0.001), and recovered to the normal level 7 days after discontinuation of captopril treatment. Intrapulmonary conversion ratio of Al to All was also significantly decreased (p<0.05) in the isolated perpused lungs. Bolus intravenous injection of angiotensin I did not showed pressor response in the both of systemic and pulmonary blood pressure of the anesthetized rats. ACE activity of the lung homogenates was also significantly reduced. These data consistently indicate the decrease of functionally active ACE molecule at the pulmonary artery after chronic captopril treatment. However, serum ACE activity was increased three fold in captopril treated rats compared to the normal rats. So, these results suggest that the functionally active ACE molecule at the pulmonary artery was still inhibited, which is directly associated with the antihypertensive effects, even if the total angiotensn converting enzyme induction was resulted after chronic captopril treatment.

• The Korean Journal of Physiology and Pharmacology
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• v.2 no.6
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• pp.771-778
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• 1998

To investigate interaction of angiotensin converting enzyme (ACE) inhibitor with local tissue renin- angiotensin system (RAS), changes in gene expression of the RAS components in various tissues in response to chronic administration of an ACE inhibitor, enalapril, were examined in Sprague-Dawley male rats. Enalapril was administered in their drinking water $(3{\sim}4\;mg/day)$ over 8 wk. Plasma and renal ACE activity increased significantly after 4 and 8 wk of enalapril treatment. Renin levels of the plasma and kidney of the enalapril-treated rats markedly increased after 4 wk and decreased thereafter, but still remained significantly higher than those of control rats. Kidney mRNA levels of renin markedly increased after 4 and 8 wk of enalapril treatment, but those of angiotensinogen and ANG II-receptor subtypes, $AT_{1A}$ and $AT_{1B}$, did not change significantly. The liver expressed genes for renin, angiotensinogen and $AT_{1A}$ receptor subtype, but $AT_{1B}$ receptor subtype mRNA was not detectable by RT-PCR. None of mRNA for these RAS components in the liver changed significantly by enalapril treatment. The hypothalamus showed mRNA expressions of renin, angiotensinogen, $AT_{1A}$ and $AT_{1B}$ receptor subtypes. $AT_{1A}$ receptor subtype mRNA was more abundant than $AT_{1B}$ receptor subtype in the hypothalamus as shown in the kidney. However, gene expression of the RAS components remained unchanged during 8-wk treatment of enalapril. In the present study, chronic ACE inhibition increased plasma and renal levels of ACE and renin, but did not affect mRNA levels of other RAS components such as angiotensinogen, ANG II receptor subtypes in the kidney. Gene levels of the RAS components in the liver and hypothalamus were not altered by chronic treatment of enalapril. These results suggest the differential expression of the RAS components in response to enalapril, and localized action and some degree of tissue specificity of enalapril.

• Food Science and Preservation
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• v.8 no.3
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• pp.296-301
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• 2001

Physiological functionalities in various extracts of Heugjinju rice bran were determined and its optimal extraction condition were also investigated Angiotensin-converting enzyme(ACE) inhibitory activity, fibrinolytic activity and tyrosinase inhibitory activity were higher in water extracts than those of 80% ethanol and methanol, hexane. Electron donating abilities were 97.8% in hexane extract and 83% in water extracts. ACE inhibitor was maximally extracted from Heugjinju rice bran when it was treated with 20 times of distilled water for 12 h at 20 $\^{C}$. Fibrinolytic compound was also maximally extracted by treatment of 10 times of distilled water for 18 h at 20 $\^{C}$. Electron donating compound and tyrosinase inhibitor were maximally extracted by treatment of 20 times of hexane and 10 times of distilled water at 20 $\^{C}$ for 18 h, respectively

• Journal of Life Science
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• v.10 no.2
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• pp.140-149
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• 2000

In order to utilize marine processing waste which would normally be discarded, cod liver protein was hydrolysed by ${\alpha}$-chymotrysin, and the hydrolysate was investigated for the new angiotensin I converting enzyme (ACE) inhibitor. Thy hydrolysate was separated into three major types, with molecular weight cut-off (MWCO) values less than 10 kDa, 5 kDa and 1 kDa of ultrafiltration membranes, respectively. ACE inhibitory peptides were isolated from the fractions passed through MWCO 1 kDa membrane, and purified by using ion-exchange chromatography on a SP-Sephadex C-25 column, gel filtration on a Sephadex G-15 column, and HPLC on an ODS column. The purity was identified with capillary electrophoresis. The amino acid sequences of two peptides were Met-Ile-Pro-Pro-Tyr-Tyr (IC50=10.9 ${\mu}$M) and Gly-Leu-Arg-Asn-Gly-Ile (IC50=35.0 ${\mu}$M)

• Preventive Nutrition and Food Science
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• v.8 no.1
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• pp.66-69
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• 2003

An angiotensin converting enzyme (ACE) inhibitory peptide was isolated and purified from the hydrolysates of duck meat protein. Duck meat protein was hydrolyzed using trypsin at 37$^{\circ}C$ for 2 hrs. An ACE inhibitory peptide was purified using membrane filtration, anion exchange chromatography, gel permeation chromatography, fast protein liquid chromatography, normal phase HPLC. The purified inhibitory peptide was identified to be a tetrapeptide, Glu-Asp-Leu-Glu having $IC_{50}$/ value of 85.9 $\mu$M.

• Food Science of Animal Resources
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• v.43 no.1
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• pp.184-194
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• 2023

Recently, interest in food-derived bioactive peptides as promising ingredients for the prevention and improvement of hypertension is increasing. The purpose of this study was to determine the structure and antihypertensive effect of an antioxidant peptide purified from velvet antler in a previous study and evaluate its potential as a various bioactive peptide. Molecular weight (MW) and amino acid sequences of the purified peptide were determined by quadrupole time-of-flight electrospray ionization mass spectroscopy. The angiotensin I-converting enzyme (ACE) inhibition activity of the purified peptide was assessed by enzyme reaction methods and in silico molecular docking analysis to determine the interaction between the purified peptide and ACE. Also, antihypertensive effect of the purified peptide in spontaneously hypertensive rats (SHRs) was investigated. The purified antioxidant peptide was identified to be a pentapeptide Asp-Asn-Arg-Tyr-Tyr with a MW of 730.31 Da. This pentapeptide showed potent inhibition activity against ACE (IC₅₀ value, 3.72 μM). Molecular docking studies revealed a good and stable binding affinity between purified peptide and ACE and indicated that the purified peptide could interact with HOH2570, ARG522, ARG124, GLU143, HIS387, TRP357, and GLU403 residues of ACE. Furthermore, oral administration of the pentapeptide significantly reduced blood pressure in SHRs. The pentapeptide derived from enzymatic hydrolysate of velvet antler is an excellent ACE inhibitor. It might be effectively applied as an animal-based functional food ingredient.