• Biomolecules & Therapeutics
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• v.1 no.2
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• pp.220-225
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• 1993

Effect of BR-900317 on the angiotensin I-induced pressor response in pithed rats and the effects of its single oral administration on plasma angiotensin converting enzyme (ACE) activities in normotensive rats and on the cardiovascular system in hypertensive model rats (SHR, RHR), were compared with those of captopril. BR-900317 attenuated the angiotensin I-induced pressor effects in pithed rats. In a single oral dose administration study, BR-900317 inhibited the plasma ACE activities in a dose-dependent fashion. Duration of the action of BR-900317 was similar to that of captopril. BR-900317 produced antihypertensive effect in spontaneously hypertensive rats and dose-dependent antihypertensive effect in 2-kidney Goldblatt hypertensive rats without affecting heart rate. These results suggest that the main mechanism of the antihypertensive effect of BR-900317 is the suppression of angiotensin II production due to the inhibition of the ACE.

• Asian-Australasian Journal of Animal Sciences
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• v.16 no.3
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• pp.417-424
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• 2003

Inhibitory activities against angiotensin I-converting enzyme (ACE) of enzymatic hydrolysates of porcine skeletal muscle proteins were investigated. Myosin B, myosin, actin, tropomyosin, troponin and water-soluble proteins extracted from pork loin were digested by eight kinds of proteases, including pepsin, $\alpha$-chymotrypsin, and trypsin. After digestion, hydrolysates produced from all proteins showed ACE inhibitory activities, and the peptic hydrolysate showed the strongest activity. In the case of myosin B, the molar concentration of peptic hydrolysate required to inhibit 50% of the activity increased gradually as digestion proceeded. The hydrolysates produced by sequential digestion with pepsin and $\alpha$-chymotrypsin, pepsin and trypsin or pepsin and pancreatin showed weaker activities than those by pepsin alone, suggesting that ACE inhibitory peptides from peptic digestion might lose their active sequences after digestion by the second protease. However, the hydrolysates produced by sequential digestion showed stronger activities than those by $\alpha$-chymotrypsin, trypsin or pancreatin alone. These results suggested that the hydrolysates of porcine meat were able to show ACE inhibitory activity, even if they were digested in vivo, and that pork might be a useful source of physiologically functional factors.

• Mycobiology
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• v.39 no.1
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• pp.67-69
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• 2011

A cell-free extract of Saccharomyces cerevisiae containing the angiotensin I-converting enzyme (ACE) inhibitory peptide was treated in a successive simulated gastric-intestinal bioreactor (step 1: amylase digestion, step 2: gastric fluid digestion, step 3: intestinal fluid digestion) to illustrate the absorption pattern of antihypertensive ACE inhibitory peptide, and the ACE inhibitory activities of each step were determined. Total ACE inhibitory activities of step 1, step 2, and step 3 were 55.96%, 80.09%, and 76.77%, respectively. The peptide sequence of each steps was analyzed by MS/MS spectrophotometry. Eleven kinds of representative peptide sequences were conserved in each step, and representative new peptides including RLPTESVPEPK were identified in step 3.

• Journal of Animal Science and Technology
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• v.49 no.1
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• pp.129-136
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• 2007

This study was performed to determine the protein profiles using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Angiotensin-I-converting enzyme(ACE) inhibitory activity (IC50) as affected by the various meat cuts, digestion times with pepsin. Hydrolysates having the protein concentration of 10 ug/mL had approximately 36∼39% ACE inhibitory activities, regardless of meat cut and digestion time. Protein concentration and ACE inhibitory activity of the diluted hydrolysate increased after 1-hr digestion. In original hydrolysates, ACE inhibitory activities of loin had higher than those of round (P<0.05). In addition, non-heated hydrolysates had higher ACE inhibitory activities than heated counterparts. When myosin B was digested by pepsin more than 1 hr, improved ACE inhibitory activities were observed as compared to the non-digested control.

• Journal of Life Science
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• v.20 no.5
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• pp.768-774
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• 2010

In this study, we investigated the antioxidant activities, alcohol metabolizing activities, nitrite scavenging ability, angiotensin converting enzyme (ACE), and elastase inhibitory effects of hot water extract from Makgeoly (HWM). Antioxidant activities were measured by using 2,2.diphenyl.1.picryl.hydrazyl (DPPH) free radical scavenging activity and SOD (superoxide dismutase).like activity. The DPPH radical scavenging activity and SOD.like activity of HWM were remarkably increased in a dose.dependent manner and were 48.0% and 98.7% at 10 mg/ml, respectively. To determine the influence of HWM on alcohol metabolizing activity, the generating activities of reduced.nicotinamide adenine dinucleotide (NADH) by alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) were measured. The facilitating rates of ADH and ALDH activity by HWM were remarkably increased in a dose.dependent manner and were 70.2% and 64.1% at 10 mg/ml, respectively. The inhibitory activity against angiotensin converting enzyme (ACE) of HWM was increased in a dose.dependent manner and was 74.2% at 10 mg/ml. The nitrite scavenging ability of HWM showed the most remarkable effect at pH 1.2 and 2 mg/ml. These results indicated that HWM may have valuable biological properties owing to their antioxidant activities, ADH and ALDH activity, nitrite scavenging ability, and ACE inhibitory activity.

• ALGAE
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• v.21 no.3
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• pp.343-348
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• 2006

This study was conducted to screen in vitro angiotensin - I converting enzyme (ACE) inhibitory activities of methanol (MeOH) and aqueous extracts at 20°C and 70°C, respectively, prepared from twenty-six red algae obtained from the coast of Jeju Island in Korea. Among aqueous extracts at 20°C (20AE) from red algae Lomentaria catenata showed the strongest ACE inhibitory activity and Lithophyllum okamurae recorded the second highest activity. From MeOH extract at 20°C (20ME) Ahnfeltiopsis flabelliformis possessed the strongest ACE inhibitory activity. Remarkable activities from MeOH extracts at 70°C (70ME) were observed in Grateloupia filicina, Sinkoraena lancifolia and Grateloupia lanceolata. However, no significant activity was found in aqueous extracts at 70°C (70AE). The IC50 values, which are concentrations required to inhibit 50% activity of ACE, for ACE inhibitory activities of 20AE from Lithophyllum okamurae and L. catenata were 13.78 and 12.21 μg mL–1, respectively. The IC50 values of 20ME from A. flabelliformis and Laurencia okamurae were 13.84 and 106.15 μg mL–1. Those of the 70ME from Bonnemaisonia hamifera, Grateloupia filicina, Sinkoraena lancifolia, G. lanceolata, Gracilaria vermiculophylla and L. okamurae ranged from 25.82 to 124.69 μg mL–1.

• Fisheries and Aquatic Sciences
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• v.5 no.1
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• pp.21-27
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• 2002

Angiotensin I converting enzyme inhibitory activities of shelled krill (Euphausia superba) hydrolysates by autolysis and by hydrolysis with commercial proteases were analyzed. Among the proteases, Alcalase was the most effective protease for the hydrolysis of krill considering the degree of hydrolysis $(87.5\%)$ and the ACE inhibitory activity $(60\%)$. Four hour hydrolysis suggested as the most suitable and economic. In order to establish the optimum hydrolysis condition of krill, degree of hydrolysis and ACE inhibitory activity as affected by Alcalase concentration and water amount added were statistically analyzed by response surface methodology (RSM). The optimum hydrolysis condition was $2.0\%$ Alcalase hydrolysis in 2 volumes (v/w) of water at $55\% for 4 hr. The hydrolysate prepared from the optimum hydrolysis condition was fractionated by molecular weight. The lower molecular weight fraction showed the higher ACE inhibitory activity. $IC_{50}$ of the fraction under 500 Da was 0.57mg protein/mL.

• Korean Journal of Medicinal Crop Science
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• v.10 no.5
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• pp.399-402
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• 2002

Angiotensin converting enzyme(ACE) belongs to the class of zinc protease and plays an important role in the regulation of blood pressure. In this experiment, we investigated the inhibitory activities of medicinal plant extracts on ACE. Fifty medicinal plants were selected and the extracts were prepared by refluxing with 70% methanol. Among the extracts, eleven medicinal plant extracts such as Sedum sarmentosum Bunge, Petasites japonicus(s.et z.) Max, Rubus coreanus, Morus bombycis Koidz, Acorus calamus var. angustatus, Glycyrhiza glabra, Equisetum hyemale, Portulaca oleracea L., Prunella vulgaris var. lilacina Nakai, Sorbus commixta Hedl, Allium thunbergii showed more than 50% inhibitory activities, and Paeonia suffruticosa Andr., lnula helenium, Acanthopanax senticosus Harms, Dendrobium moniliforme, Juglans mandshurica, Zizyphus jujuba, Leonurus artemisia, Aster scaber Thunb, Vitex rotundifolia, Platycodon grandiflorum, Prunus persica, Ligularia fischeri showed $40{\sim}49%$ inhibitory activities. Therefore these extracts which contain high ACE inhibitory activities may be useful as antihypertension agents and to the treatment of hypertension.

• Fisheries and Aquatic Sciences
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• v.16 no.4
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• pp.237-242
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• 2013

We investigated the antioxidant and angiotensin I converting enzyme (ACE) inhibitory activities of red snow crab Chionoecetes japonicas shell (RSCS) hydrolysate by enzymatic hydrolysis and its molecular weight cut-off fractions. The RSCS hydrolysate was fractionated through two ultrafiltration membranes of 3 and 10 kDa cut-offs. Three fractions (<3 kDa, 3-10 kDa, and >10 kDa) were evaluated for total amino acid composition, antioxidant activities using 2'-azino-bis[3-ethylbenzthiazoline-6-sulfonic acid] ($ABTS^+$) radical scavenging and superoxide dismutase (SOD)-like activities and reducing power assays, and ACE inhibitory activity using Hou's method. Although all fractions showed activity, the <3 kDa fraction of RSCS hydrolysate exhibited the greatest $ABTS^+$ radical scavenging, SOD-like and ACE inhibitory activities. However, these fractions exhibited low reducing power. These results suggest that the low-molecular-weight enzymatic hydrolysate of RSCS could be used as a functional ingredient to control oxidative stress and ACE activity.

• Microbiology and Biotechnology Letters
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• v.31 no.1
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• pp.51-56
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• 2003

The angiotensin I converting enzyme (ACE) has an important role in the maintenance of blood pressure. The ACE inhibitory activities of foods have recently been studied. We tried to isolate ACE inhibitory peptides from the Flavourzyme (FZ), Pescalase (PE), and Thermolysine (TH) protease digests of corn gluten, which was restricted to the use the source of food for digestion problem. The FZ, PE, TH/PE protease hydrolyzed corn gluten and the inhibitory activities of the hydrolyzates for ACE were measured. Major fractions were isolated from the digests using ODS chromatography after treating with ethanol in step gradient. The ACE inhibitors were further purified by Bio-Gel P-2 column and reverse phase HPLC. Five inhibitory peptides were isolated. Their amino acids were sequenced as LPF ($IC_{50}$ = 40$\mu$M), GPP ($IC_{50}$ = 17.6$\mu$M), PNPY ($IC_{50}$ = 30.7$\mu$M), SPPPFYL ($IC_{50}$ = 63 $\mu$M), and SQPP ($IC_{50}$ = 17.2$\mu$M).