• Title/Summary/Keyword: angiotensin I-converting enzyme (ACE)

Search Result 228, Processing Time 0.034 seconds

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
    • /
    • v.16 no.9
    • /
    • pp.1369-1373
    • /
    • 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
    • /
    • v.5 no.2
    • /
    • pp.93-100
    • /
    • 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.

Frequency of the Angiotensin - Converting Enzyme (ACE) Gene Polymorphism in the General Population and the Elite Endurance Students in Korea

  • Choung, Ho-Jin;Yoon, Song-Ro;Choi, Soo-Kyung
    • Journal of Genetic Medicine
    • /
    • v.3 no.1
    • /
    • pp.11-13
    • /
    • 1999
  • Recently it was reported that Insertion/Deletion polymorphism in the gene coding for Angiotensin-Converting Enzyme (ACE) is associated with human capacity for physical performance. This study was performed to genotyping of the ACE gene to determine the correlation between elite endurance performance and ACE I/D gene polymorphism. DNA sample was obtained from peripheral blood, hair roots and mouth epithelial cell in 739 general population and 200 elite athletic performance students. The ACE gene was amplified by polymerase chain reaction (PCR) using allele specific oligonucleotide primers. 155, 525 bp and 237 bp PCR products indicating the presence of insertion(I) and deletion(D) alleles, respectively, were clearly resolved after electrophoresis on a 2% agarose gel with ethidium bromide. Of the 200 elite athletic performance population subjects, 68(34%) showed ACE genotype 11,100(50%) genotype ID and 32(16%) genotype DD. Of the 739 general population subjects, 259(35.1%) showed ACE genotype 11,363(49.1%) genotype ID and 117(15.8%) genotype DD. Therefore ACE I/D gene polymorphism was not associated with human capacity for physical performance.(p>0.05)

  • PDF

Peptide Inhibitors for Angiotensin I Converting Enzyme from Corn Gluten Digests. (옥수수 글루텐 효소 가수분해물의 Angiotensin I Converting Enzyme 활성 저해 펩타이드의 정제)

  • 오광석;이동건;홍정운;성하진
    • Microbiology and Biotechnology Letters
    • /
    • v.31 no.1
    • /
    • pp.51-56
    • /
    • 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).

Angiotensin-I Converting Enzyme Inhibitory Activity of Enzymatic Hydrolysates of Food Proteins (식품단백질 효소가수분해물의 Angiotensin-I 전환효소 저해작용)

  • 염동민;노승배;이태기;김선봉;박영호
    • Journal of the Korean Society of Food Science and Nutrition
    • /
    • v.22 no.2
    • /
    • pp.226-233
    • /
    • 1993
  • Enzymatic hydrolysates of food proteins (defatted soybean cake, egg albumin and casein) were tested for inhibitory activity against angiotensin-I converting enzyme (ACE). Food proteins were hydrolysed with complex enzyme, bromelain, alcalase, $\alpha$-chymotrypsin, trypsin, papain and pepsin by heating method. The hydrolysates obtained from the treatment of complex enzyme and bromelain showed the higher ACE inhibitory activity. ACE inhibitory activity of hydrolysates exhibited a tendency to be increased until 8hrs and increased with increment of concentration. The activity was also stable by heat treatment at 10$0^{\circ}C$ for 20min. Molecular weight of active fraction was about 1, 400 and defatted soybean cake hydrolysate below 1, 400 in case of defatted soybean cake hydrolysate treated with alcalase. Amino acid of the active fractions was abundant in Asp, Glu, Lys, lle, Leu, Ala and Val.

  • PDF

Production and Characterization of Antihypertensive Angiotensin I-Converting Enzyme Inhibitor from Pholiota adiposa

  • Koo Kyo-Chul;Lee Dae-Hyoung;Kim Jae-Ho;Yu Hyung-Eun;Park Jeong-Sik;Lee Jong-Soo
    • Journal of Microbiology and Biotechnology
    • /
    • v.16 no.5
    • /
    • pp.757-763
    • /
    • 2006
  • Angiotensin I-converting enzyme (ACE) inhibitors have generally been very useful to remedy or prevent hypertension. This study describes the extraction and characterization of an ACE inhibitor from the fruiting body of Pholiota adiposa ASI 24012, which can be used as an antihypertensive drug. The maximal ACE inhibitory activity $(IC_{50};0.25mg)$ was obtained when the fruiting body of Pholiota adiposa ASI 24012 was extracted with distilled water at $30^{\circ}C$ for 12 h. After the purification of ACE inhibitor with ultrafiltration, Sephadex G-25 column chromatography, and reverse-phase HPLC, an active fraction with an $IC_{50}$ of 0.044 mg was obtained. The purified ACE inhibitory peptide was a novel pentapeptide, showing very little similarity to other ACE inhibitory peptide sequences. The molecular mass of the purified ACE inhibitor was estimated to be 414 daltons with a sequence of Gly-Glu-Gly-Gly-Pro, and showed a clear antihypertensive effect on spontaneously hypertensive rats (SHR) at a dosage of 1 mg/kg.

Screening of Extracts from Red Algae in Jeju for Potentials MarineAngiotensin - I Converting Enzyme (ACE) Inhibitory Activity

  • Cha, Seon-Heui;Lee, Ki-Wan;Jeon, You-Jin
    • ALGAE
    • /
    • v.21 no.3
    • /
    • pp.343-348
    • /
    • 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.

Association analysis of a polymorphism of the angiotensin I-converting enzyme gene and angiotensin II Type 1 receptor gene in Korean population

  • Yang, Young-Mok;Park, Jong-Hwan;Lee, Hyun-Young;Moon, Eon-Soo
    • Journal of Genetic Medicine
    • /
    • v.2 no.1
    • /
    • pp.27-30
    • /
    • 1998
  • Previously, we made a study report on the genotype distribution and the gene frequency of angiotesin I-converting enzyme (ACE) in Korean population, and on the association between hypertension and genetic variance of ACE. This time, we have investigated a rapid mismatch-PCR/RFLP assays for the variant of the angiotesin II type 1 receptor ($AT_1R$) gene (an $A{\rightarrow}C$ transversion at position 1166 of $AT_1R$ gene), a mutation which may interact with the ACE polymorphism in the determining of risk of myocardial infarction. The genotype distributions of Koreans' angiotensin II type 1 receptor gene were AA (66.3%):AC (28.1%):CC (5.6%), thus the AA genotype was most numerous, and the allele frequency was A:C = 0.803:0.197. Genotype distributions were shown as AA (76.8%):AC (20.9%):CC (2.3%), the allele frequency was A:C = 0.872:0.128 in the male group, and AA (47.4%):AC (41.0%):CC (11.6%), A:C = 0.679:0.321 in the female group. Differences were highly significant between the male and female groups (p<0.0001). Genotype distributions between angiotensin II type 1 receptor gene and angiotensin converting enzyme gene showed that there is no significance between $AT_1R$ genotypes and ACE genotypes in total subjects (p>0.05).

  • PDF

Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity of Elk (Cervus elaphus) Velvet Antler

  • Karawita Rohan;Park, Pyo-Jam;Siriwardhana Nalin;Jeon, Byong-Tae;Moon, Sang-Ho;Ahn, Duk-Kyun;Chos, Somi-K.;Jeon, You-Jin
    • Preventive Nutrition and Food Science
    • /
    • v.10 no.3
    • /
    • pp.239-243
    • /
    • 2005
  • Angiotensin I-converting enzyme (ACE) inhibitory activities of elk antler hydrolysates prepared with three kinds of proteases, pepsin, trypsin and $\alpha-chymotrypsin$, were investigated. The ACE inhibitory activity of the pepsinolytic hydrolysate was the highest with an $IC_{50}$ value of $9.3\mu g/mL.$ In addition, three kinds of pepsinolytic hydrolysates with relatively high molecular weights (over 10,000 Da), medium molecular weights (5,000 to 10,000 Da), and low molecular weights (below 5,000 Da) were fractionated using an ultrafiltration membrane system. The below 5,000 Da hydrolysate exhibited the highest ACE inhibitory activity. These results indicate that the pepsinolytic hydrolysates of elk velvet antler could be a good source of peptides with ACE inhibitory activity.

Angiotensin Converting Enzyme (ACE) Gene Polymorphism and Sasang Constitution in Patients with Cerebral Infarction (뇌경색 환자의 안지오텐신 전환요소 유전자 다형성과 사상체질)

  • Bae, Young-Choon;Kweon, Deog-Yun;Kim, Kyung-Yo;Kim, Il-Hwan;Ju, Jong-Chun
    • Journal of Sasang Constitutional Medicine
    • /
    • v.14 no.1
    • /
    • pp.132-139
    • /
    • 2002
  • The correlation between angiotensin converting enzyme (ACE) polymorphisms and cerebral infarction (CI) has been controversial. Such controversy may be due to different classifications of cerebrovascular diseases and ethnic differences. I studied the correlation between ACE genotypes and CI patients by case-control study in the Korean population. I also classified CI patients and control group into four types according to Sasang constitutional medicine. Furthermore I investigated the correlation among ACE genotypes, CI and Sasang constitutions. The frequencies of D allele were 0.32 in subjects with CI and 0.40 in the control group without CI (X2=0.128, p=0.720). In patients with CI, the frequency of Taeumins, one of four Sasang constitutional types, was significantly higher than that in controls (X2=15.425, p<0.00l). I did not find any correlation between ACE polymorphism and CI in Koreans. However, there were significant differences in allele frequencies between Koreans and Europeans, while similarities were shown to those of Japanese and Chinese populations.

  • PDF