• Title/Summary/Keyword: Angiotensin converting enzyme (ACE)

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Production of Antihypertensive Angiotensin I-Converting Enzyme Inhibitor from Malassezia pachydermatis G-14

  • Jeong, Seung-Chan;Kim, Jae-Ho;Kim, Na-Mi;Lee, Jong-Soo
    • Mycobiology
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    • v.33 no.3
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    • pp.142-146
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    • 2005
  • To produce a novel antihypertensive angiotensin I-converting enzyme (ACE) inhibitor from yeast, a yeast isolate, designated G-14 showing the highest ACE inhibitory activity was obtained and identified as Malassezia pachydermatis based on morphological, biochemical and cultural characteristics. The maximal extracellular ACE inhibitor production was obtained from M. pachydermatis G-14 when the strain was cultured in YEPD medium containing 0.5% yeast extract, 3.0% peptone and 2.0% glucose at $30^{\circ}C$ for 24 h and the final ACE inhibitory activity was 48.9% under the above condition.

Isolation of Angiotensin I-Converting Enzyme Inhibitory Peptide from Chungkookjang (청국장으로부터 Angiotensin I 전환효소 저해 Peptide의 분리)

  • Matsui Toshiro;Yoo Hyung Jae;Hwang Jae Sung;Lee Dong Seok;Kim Han Bok
    • Korean Journal of Microbiology
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    • v.40 no.4
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    • pp.355-358
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    • 2004
  • Chunkookjang, Korean traditional fermented soybean food emerges as a functional food to improve intestinal function and blood circulation. During Chungkookjang fermentation, microorganisms, enzymes, and diverse bioactive compounds increase sharply. Chungkookjang contains diverse oligo-peptides. Formation of peptides was confirmed by SDS-PAGE. Solube fermented soybean in our sample contained Tyr, Gln-Lys, Trp, Gln, and Lys-Pro as major components. Lys-Pro (0.083 mg/100 g sample) was purified by HPLC analysis. Angiotensin I­converting enzyme (ACE) causes hypertension by converting angiotensin I to angiotension II. ACE inhibitory activity of Lys-Pro was determined to be $IC_{50}=32.1\;{\mu}M.$ Whether or not eating Chungkookjang can lower blood pressure was also determined. Sistolic blood pressure dropped by 15 mmHg, and diastolic blood pressure by 8 mmHg 2 hr after a single administration of 20 g of fermented soybean. Chungkookjang might be helpful in improving blood circulation since it has ACE inhibitor and antihypertenisve effect.

Evaluation of Angiotensin -I- Converting Enzyme Inhibitory Activity and Protein Changes of Enzymatic Hydrolysate Extracted from Hanwoo Loin and Round Myosin B (한우 등심과 우둔에서 추출한 Myosin B의 효소적 가수분해물의 단백질 변화와 Angiotensin -I- Converting Enzyme(ACE) 저해효과)

  • Kim, Y.J.;Chin, Koo-Bok
    • 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.

A Case of Angioedema Induced by Angiotensin-Converting Enzyme Inhibitor (Angiotensin-Converting Enzyme Inhibitor(ACE Inhibitor)에 의해 유발된 안면부 맥관부종(angioedema) 치험례)

  • Hsia, Yu-Chun;Jung, Ki-Yong;Baik, Jong-Woo;Kim, Dong-Woo;Park, Jong-Hyung;Jun, Chan-Yong;Choi, You-Kyung
    • The Journal of Internal Korean Medicine
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    • v.28 no.2
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    • pp.399-407
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    • 2007
  • Angioedema is a localized transient swelling of sudden onset that can occur in the face, lips, tongue, hand, feet, respiratory system and gastrointestinal system. Angioedema is classified as allergy, hereditary, idiopathic or induced by medication as like aspirin, nonsteroidal anti-inflammatory agents, opiates, antibiotics, and angiotensin-converting enzyme. Angiotensin-converting enzyme inhibitors are widely prescribed for hypertension and heart failure. This drug is commonly associated with angioedema which may be potentially life threatening. We experienced a case of angioedema induced by ACE inhibitor (angiotensin-converting enzyme inhibitor) in a 74-year-old patient who took ACE inhibitor to control hypertension during hospitalization. We thought the angioedema in the face had relation to myenzhong (面腫, mienjong) in oriental medicine. Weiling-tang (Wiryung-tang) was effective for angioedema in the face. As a result the symptoms disappeared rapidly. After 6 days, the patient's symptoms had notably improved.

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Inhibitory Effect of Onion Seasoning on Angitensin Converting Enzyme (양파 조미액의 Angiotensin Converting Enzyme 저해활성)

  • 마상조
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.29 no.3
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    • pp.395-400
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    • 2000
  • 양파 조미액으로부터 ACE 저해활성 물질을 분리하기 위해 hexane, ethylether, ethylacetate, butanol과 물로 분획시, 4.8g의 당 함량과 31.9 mg의 phenol성 물질을 함유한 butanol 분획이 82.1%의 ACE 저해활성을 나타내었고, 70.3%의 ACE 저해활성을 보인 양퍄 조미액보다 높은 저해활성을 보였다. Butanol 분획을 Amberite XAD-2column으로 분리한 결과, ACE 저해활성을 보이는 미흡착 분획(F1)를 얻었다. 활성분획 F1을 Sephadex LH-20column으로 분획한 결과, 4개(F1-1,F1-2,F1-3,F1-4)의 분획을 얻었으며, 이중 F1-3 분획의 ACE 저해활성은 93%로 가장 높은 저해활성을 보였다. Sephadex LH-20 column chromatography에 의해 얻어진 활성분획F1-3을 Supercosil LC-18 column을 이용하여 분리한 결과, 6분대에서 ACE 저해활성을 가지는 단일 peak(F1-3a)를 얻었다. 각 정제 과정에서 얻은 분획들은 전형적인 flavonoid의 band I과 bandII의 피크를 보였다. 또한 ACE에 대한 저해기작은 flavonoid 물질이 보이는 전형적인 비경쟁적 저해양상을 보였다.

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Angiotensin- I Converting Enzyme Inhibitory Properties of Bovine Casein Hydrolysates in Different Enzymatic hydrolysis Conditions (효소가수분해 조건에 따른 우유 케이신의 Angiotensin-I 전환효소 저해효과)

  • 김현수;인영민;정석근;함준상;강국희;이수원
    • Food Science of Animal Resources
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    • v.22 no.1
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    • pp.87-93
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    • 2002
  • Angiotensiri-I converting enzyme(ACE) catalyst the removal of the C-terminal dipeptide from the angiotensin-I to give the angiotensin-II, a potent peptide that causes constriction of regulation of blood pressure. Recently, ACE inhibitor peptides have been isolated from enzymatic digests of food protein. The aim of this study was to identify bovine casein hydrolysates with ACE inhibitory properties in different enzymatic hydrolysis conditions. The casein were hydrolyzed neutrase, alcalase, protamax, flavourzyme, premed 192, sumizyme MP, sumizyme LP and pescalase alone and with an enzyme combination. Premed 192 produced ACE inhibitory peptides most efficiently. In order to ACE inhibitory peptide produced enzymatic hydrolysis condition were premed 192 added to casein ratio of 1:100(w/w), and incubated at 47$\^{C}$ for 12hrs. Casein hydrolysate gave 50% inhibition(IC$\_$50/ value) of ACE activity at concentration with 248ug/ml(general method) and 265ug/ml(pretreatment method) respectively.

Inhibition Effect of ACE (Angiotensin Converting Enzyme) and Kinetics of Aloe Acethylmannan (알로에 아세칠만난의 ACE (Angiotensin Converting Enzyme) 저해효과 및 동력학적 분석)

  • Ryu, Il-Whan;Shin, Yong-Seo
    • Korean Journal of Food Science and Technology
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    • v.29 no.6
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    • pp.1269-1274
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    • 1997
  • This study was researched to purify and characterize variety bioactive material acethylmannan from Aloe vera. Purified acethylmannan was mannose (67%), acetyl group (23%) and the rest glucose, galactose that consisting of long chain polydispered ${\beta}-1,4$ linked mannan polymers. The sugar and acetyl group in molecular were linked molar ration one third. $IC_{50}$ value (i.e that concentration which exhibits 50% more enzyme inhibition than control) on angiotensin converting enzyme were 0.58 mM. This compound were found to be a competitive inhibition of Angiotensin Converting Enzyme with apparent Ki values of 0.068 mM.

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Association between Angiotensin I-Converting Enzyme Gene Polymorphism and Hypertension in Selected Individuals of the Bangladeshi Population

  • Morshed, Mahboob;Khan, Haseena;Akhteruzzaman, Sharif
    • BMB Reports
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    • v.35 no.3
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    • pp.251-254
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    • 2002
  • The genetic factors that contribute to the development of coronary artery disease (CAD) are poorly understood. It is likely that multiple genes that act independently or synergistically contribute to the development of CAD and the outcome. Recently, an insertion/deletion (I/D) polymorphism of the human angiotensin I-converting enzyme (ACE) gene, a major component of the renin-angiotensin system (RAS), was identified. The association of the ACE gene D allele with essential hypertension and CAD has been reported in the African-American, Chinese, and Japanese populations. However, other studies have failed to detect such an association. It has been suggested that these inconsistencies may be due to the difference in backgrounds of the population characteristics. In the present study, we investigated the I/D polymorphism of the ACE gene in 103 subjects of both sexes, consisting of 59 normal controls and 44 patients with hypertension. The allele and genotype frequency were significantly different between the hypertensive and control groups (p < 0.01). Among the three ACE I/D variants, the DD genotype was associated with the highest value of the mean systolic blood pressure [SBP] and mean diastolic blood pressure [DBP] (p = < 0.05) in men, but not in women. In the overall population, the mean SBP and DBP was highest in DD subjects, intermediate in I/D subjects, and the least in II subjects.

Production of Angiotensin-I Converting Enzyme Inhibitory Hydrolysates from Egg Albumen

  • Kim, H.S.;Ham, J.S.;Jeong, S.G.;Yoo, Y.M.;Chae, H.S.;Ahn, C.N.;Lee, J.M.
    • Asian-Australasian Journal of Animal Sciences
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    • v.16 no.9
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    • pp.1369-1373
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    • 2003
  • ACE (Angiotensin-I converting enzyme) inhibitory peptides derived from foods are thought to suppress high blood pressure by inhibiting ACE. We tried to make efficient production of the ACE inhibitory hydrolysate from egg albumen. A hydrolysate digested by neutrase presented the highest ACE inhibitory activity ($IC_50\;value=256.35{\mu}g/ml$) and the proper proteolysis was occurred by 1.0% enzyme addition and 4 h incubation at $47^{\circ}C$. Antihypertensive effect of neutrase hydrolysate was investigated in spontaneously hypertensive rats (SHR, n=5). Systolic blood pressure (SBP) was decrease by 6.88% (-14.14 mmHg, p<0.05) at 3 h after oral administration of 300 mg/kg body weight, and by 13.33% (-27.72 mmHg, p<0.05) by emulsified hydrolysate. These results showed that it is very effective to utilize egg albumen as a protein source for the production of ACE inhibitory peptides. However, further studies are required to investigate the methods to increase recovery yield and the isolation of active peptide is necessary for determining its sequence responsible for ACE inhibitory activity.

Effect of phlorotannins isolated from Ecklonia cava on angiotensin I-converting enzyme (ACE) inhibitory activity

  • Wijesinghe, W.A.J.P.;Ko, Seok-Chun;Jeon, You-Jin
    • Nutrition Research and Practice
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    • v.5 no.2
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    • pp.93-100
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    • 2011
  • Inhibition of angiotensin I-converting enzyme (ACE) activity is the most common mechanism underlying the lowering of blood pressure. In the present study, five organic extracts of a marine brown seaweed Ecklonia cava were prepared by using ethanol, ethyl acetate, chloroform, hexane, and diethyl ether as solvents, which were then tested for their potential ACE inhibitory activities. Ethanol extract showed the strongest ACE inhibitory activity with an $IC_{50}$ value of 0.96 mg/ml. Five kinds of phlorotannins, phloroglucinol, triphlorethol-A, eckol, dieckol, and eckstolonol, were isolated from ethanol extract of E. cava, which exhibited potential ACE inhibition. Dieckol was the most potent ACE inhibitor and was found to be a non-competitive inhibitor against ACE according to Lineweaver-Burk plots. Dieckol had an inducible effect on the production of NO in EAhy926 cells without having cytotoxic effect. The results of this study indicate that E. cava could be a potential source of phlorotalnnins with ACE inhibitory activity for utilization in production of functional foods.