• 제목/요약/키워드: Antihypertensive angiotensin I-converting enzyme inhibitor

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Attenuating Development of Cardiovascular Hypertrophy with Hydrolysate of Chicken Leg Bone Protein in Spontaneously Hypertensive Rats

  • Cheng, Fu-Yuan;Wan, Tien-Chun;Liu, Yu-Tse;Lai, Kung-Ming;Lin, Liang-Chuan;Sakata, Ryoichi
    • Asian-Australasian Journal of Animal Sciences
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    • 제21권5호
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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.

Quality Characteristics and Cardiovascular Activities of Korean Traditional Wines and Liquors

  • Yu, Hyung-Eun;Lee, Dae-Hyoung;Lee, Ju-Hyun;Choi, Sin-Yang;Lee, Jong-Soo
    • Food Science and Biotechnology
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    • 제14권6호
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    • pp.772-777
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    • 2005
  • The goal of this study was to screen and characterize the physiological functions of Korean traditional wines (TW) and liquors (TL). Forty-two TW and TL were collected and evaluated for quality and cardiovascular activities. Ethanol content ranged from $9.0%{\sim}41%$, and pH ranged from $3.0{\sim}7.8$, and they also contained 0.01% to 0.67% of total acid. Samples contained a maximum of 2.0% of crude protein and $0.1%{\sim}14.0%$ of reducing sugar. Commercial CM-wine showed the highest antihypertensive angiotensin I-converting enzyme (ACE) inhibitory activity, 85.9%. The greatest fibrinolytic activity and platelet aggregation inhibitory activity were also found in commercial CM-wine (31.8U) and commercial SS2-wine (38.6 %), respectively. Commercial SHBI-liquor showed the highest HMG-CoA reductase inhibitory activity, 78%. The ACE inhibitor from commercial CM-wine was a peptide compound and also showed an antihypertensive effect in spontaneous hypertensive rats at a dosage of 1.5 mg/kg.

Production of Antihypertensive Angiotensin I-Converting Enzyme Inhibitor-Enriched Edible Yeast Using Gugija (Lycium chinesis Mill)

  • Kim, Ran;Jang, Jeong-Hoon;Park, Won-Jong;Kim, Ha-Kun;Kwak, Hahn-Shik;Lee, Jong-Soo
    • Mycobiology
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    • 제38권3호
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    • pp.206-209
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    • 2010
  • To produce bioactive compound enriched yeast using medicinal Gugiga (Lycium chinensis Mill), several edible Saccharomyces species were cultured in Gugija extracts added yeast extract, peptone and dextrose medium (GE - YEPD medium) at $30^{\circ}C$ for 24 hr, and their growth were determined. Growth of Saccharomyces cerevisiae K-7 and Sacchromyces cerevisiae ACTC 7904 were better than those of the other yeasts. Two yeasts were selected and then determined their some physiological functionalities after cultivated the yeasts in the GE - YEPD medium and compared those grown on YEPD medium. Antihypertensive angiotensin I-converting enzyme (ACE) inhibitory activity of S. cerevisiae K-7 grown on GE - YEPD medium was about 20% higher than that grown on YEPD medium. Superoxide dismutase-like activity of S. cerevisiae ACTC 7904 was also about 12% more high. However, the other physiological functionalities were almost same or lower. Optimal addition concentration of Gugija extract was 10%, and maximally growth and ACE inhibitory activity of S. cerevisiae K-7 were shown when the strain was cultured in 10% Gugija extracts containing YEPD medium at $30^{\circ}C$ for 12 hr.

Angiotensin I-Converting Enzyme Inhibitor Activity on Egg Albumen Fermentation

  • Nahariah, N.;Legowo, A.M.;Abustam, E.;Hintono, A.
    • Asian-Australasian Journal of Animal Sciences
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    • 제28권6호
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    • pp.855-861
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    • 2015
  • Lactobacillus plantarum is used for fermentation of fish products, meat and milk. However, the utilization of these bacteria in egg processing has not been done. This study was designed to evaluate the potential of fermented egg albumen as a functional food that is rich in angiotensin I-converting enzyme inhibitors activity (ACE-inhibitor activity) and is antihypertensive. A completely randomized design was used in this study with six durations of fermentation (6, 12, 18, 24, 30, and 36 h) as treatments. Six hundred eggs obtained from the same chicken farm were used in the experiment as sources of egg albumen. Bacteria L. plantarum FNCC 0027 used in the fermentation was isolated from cow's milk. The parameters measured were the total bacteria, dissolved protein, pH, total acid and the activity of ACE-inhibitors. The results showed that there were significant effects of fermentation time on the parameters tested. Total bacteria increased significantly during fermentation for 6, 12, 18, and 24 h and then decreased with the increasing time of fermentation to 30 and 36 h. Soluble protein increased significantly during fermentation to 18 h and then subsequently decreased during of fermentation to 24, 30, and 36 h. The pH value decreased markedly during fermentation. The activities of ACE-inhibitor in fermented egg albumen increased during fermentation to 18 h and then decreased with the increasing of the duration of fermentation to 24, 30, and 36 h. The egg albumen which was fermented for 18 h resulted in a functional food that was rich in ACE-inhibitor activity.

각종 미강 추출물들의 항고혈압성 엔지오텐신 전환효소 저해 활성 (Antihypertensive Angiotensin I-Converting Enzyme Inhibitiory Activity of Various Extracts from Some Rice Brans)

  • 김형종;김재호;손종록;이종수
    • 자연과학논문집
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    • 제13권1호
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    • pp.65-71
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    • 2003
  • 각종 미강 추출물들의 항고혈압성 엔지오텐신 전환효소 저해 활성을 측정하고 이들의 추출 최적조건을 검토하였다. 각종 미강 추출물들중에서 일품벼 미강의 물 추출물이 77%의 가장 높은 안지오텐신 전환효소 저해활성 보였다. 일품벼 미강중의 안지오텐신 전환효소 저해물질은 물을 1:10(w/v)으로 미강 분말에 첨가한 후 $30^{\circ}C$에서 12시간 추출하였을 때 가장 많이 용출되었다.

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Expression and Purification of an ACE-Inhibitory Peptide Multimer from Synthetic DNA in Escherichia coli

  • OH, KWANG-SEOK;YONG-SUNG PARK;HA-CHIN SUNG
    • Journal of Microbiology and Biotechnology
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    • 제12권1호
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    • pp.59-64
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    • 2002
  • An angiotensin I-converting enzyme (EC 3.4.15.1) (ACE), which can convert inactive angiotensin I into angiotensin II, a vasoconstrictor, is one of the key enzymes in controlling hypertension. It is suggested that the inhibition of ACE prevents hypertension, and many inhibitory peptides have already been reported. In the current study, oligonucleotides encoding ACE inhibitory peptides (IY, VKY) were chemically synthesized and designed to be multimerised due to isoschizomer sites (BamHI, BglII). The cloned gene named AP3 was multimerised up to 6 times in pBluescript and expressed in BL2l containing pGEX-KG. The fusion protein (GST-AP3) was easily purified with a high recovery by an affinity resin, yielding 38 mg of synthetic AP3 from a 1-1 culture. The digestion of AP3 by chymotrypsin exhibited an $IC_50$ value of $18.53{\mu}M$. In conclusion, the present experiment indicated that AP3 could be used as a dietary antihypertensive drug, since the potent ACE inhibitory activity of AP3 could be activated by chymotrypsin in human intestine.

Dipeptide (Tyr-Ile) Acting as an Inhibitor of Angiotensin-I-Converting Enzyme (ACE) from the Hydrolysate of Jellyfish Nemopilema nomurai

  • Kim, Yeon-Kye;Lim, Chi-Won;Yeun, So-Mi;Lee, Moon-Hee;Moon, Ho-Sung;Cho, Hyeon-Ah;Yoon, Na-Young;Yoon, Ho-Dong;Park, Hee-Yeon;Lee, Doo-Seog
    • Fisheries and Aquatic Sciences
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    • 제14권4호
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    • pp.283-288
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    • 2011
  • The jellyfish Nemopilema nomurai was hydrolyzed with papain and a novel dipeptide purified via ultrafiltration, gel filtration chromatography with Sephadex LH-20, and reverse phase chromatography using $C_{18}$ and $C_{12}$ columns. The IR, 1H NMR, 13C NMR, and MS spectrometer analyses showed that the dipeptide comprised tyrosine-isoleucine (Tyr-Ile). The $IC_{50}$ and $K_i$ values were $6.56{\pm}1.12$ and $3.10{\pm}0.28\;{\mu}M$, respectively, indicating competitive inhibition of angiotensin-I-converting enzyme (ACE). As a novel ACE-inhibitory active peptide, Tyr-Ile may have potential for use in antihypertensive therapy.

Expression of Antihypertensive Peptide, His-His-Leu, as Tandem Repeats in Escherichia coli

  • Jeong, Do-Won;Shin, Dong-Seok;Ahn, Chang-Won;Song, In-Sang;Lee, Hyong-Joo
    • Journal of Microbiology and Biotechnology
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    • 제17권6호
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    • pp.952-959
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    • 2007
  • His-His-Leu (HHL), a tripeptide derived from a Korean soybean paste, is an angiotensin-I-converting enzyme (ACE) inhibitor. We report here a method of producing this tripeptide efficiently by expressing tandem multimers of the codons encoding the peptide in E. coli and purifying the HHL after hydrolysis of the peptide multimers. The HHL gene, tandemly multimerized to a 40-mer, was ligated with ubiquitin as a fusion gene (UH40). UH40 was inserted into vector pET29b; the UH40 fusion protein was then produced in E. coli BL21. The recombinant UH40 protein was purified by cation-exchange chromatography with a yield of 17.3mg/l and analyzed by matrixassisted laser desorption ionization (MALDI) time-of-flight (TOF) mass spectrometry and protein N-terminal sequencing. Leucine aminopeptidase was used to cleave a 405-Da HHL monomer from the UH40 fusion protein and the peptide was purified using reverse-phase high-performance liquid chromatography (HPLC) on a C18 HPLC column, with a final yield of 6.2mg/l. The resulting peptide was confirmed to be HHL with the aid of MALDI-TOF mass spectrometry, glutamine-TOF mass spectrometry, N-terminal sequencing, and measurement of ACE inhibiting activity. These results suggest that our production method is useful for obtaining a large quantity of recombinant HHL for functional antihypertensive peptide studies.

Chitosan 올리고당의 안지오텐신 전환효소 활성 억제 및 SHR에서의 고혈압 억제 특성 (ACE Inhibitory and Antihypertensive Effect of Chitosan Oligosaccharides in SHR)

  • 홍상필;김명희;오세욱;한찬규;김용현
    • 한국식품과학회지
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    • 제30권6호
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    • pp.1476-1479
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    • 1998
  • 키토산 올리고당이 ACE 저해활성과 SHR의 혈압에 미치는 영향을 검토하였다. 키토산 올리고당은 모두 ACE 저해활성을 나타내었다. ACE 저해활성$(IC_{50})$은 3량체가 $0.9\;{\mu}mole$로 가장 우수하였고 2량체의 경우에는 $2.4\;{\mu}mole$, 그 외의 올리고당은 모두 $>100\;{\mu}mole$였다. 강력한 ACE 저해제인 Captopril(2-D-mercaptopropanoyl-L-proline)의 인체 투여량을 기준으로 3량체 키토산 올리고당 2.14 mg/kg을 SHR에 강제 경구투여한 바, 4시간 경에 8주령 및 21주령 SHR모두 최저혈압을 보였고 이 때의 혈압 강하는 8주령 SHR $27{\pm}4.8\;mmHg$, 21주령 SHR $36{\pm}4.3\;mmHg$로 나타났다. 따라서 3량체 키토산 올리고당은 2량체 키토산 올리고당과 함께 향후 고혈압 치료제로서 응용가능함이 시사되었다.

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백색 느티만가닥버섯 자실체의 생리기능성 탐색 (Screening and Physiological Functionality of Hypsizygus marmoreus (White Cultivar) Fruiting Body)

  • ;김민경;서건식;이영욱;이종수
    • 한국균학회지
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    • 제39권3호
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    • pp.185-188
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    • 2011
  • 버섯으로부터 생리 기능성이 우수한 건강 소재나 대체의약을 개발하기 위하여 백색 느티만가닥버섯의 자실체의 물추출물과 에탄올추출물을 제조한 후 이들의 생리기능성을 측정하였다. 시료 버섯 자실체의 물 추출물의 ACE 저해활성이 60.5%로 에탄올 추출물의 저해활성 보다 높았다. 또한 SOD 유사활성과 Xanthine oxidase 저해 활성도 물추출물에서 각각 24.1%와 23.0%을 보였다. 백색 느티만가닥버섯 자실체에 함유되어있는 ACE 저해 물질은 자실체 분말을 물에 1 : 40으로 현탁 시킨 후 $50^{\circ}C$에서 12시간 추출했을 때 가장 많이 추출되었고 이때 ACE 저해활성은 80.5% 이었다.