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

검색결과 228건 처리시간 0.022초

Peptic Hydrolysate of Porcine Crude Myosin Has Many Active Fractions Inhibiting Angiotensin I-converting Enzyme

  • Katayama, Kazunori;Fuchu, Hidetaka;Sugiyama, Masaaki;Kawahara, Satoshi;Yamauchi, Kiyoshi;Kawamura, Yukio;Muguruma, Michio
    • Asian-Australasian Journal of Animal Sciences
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    • 제16권9호
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    • pp.1384-1389
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    • 2003
  • In order to clarify one of the biological functions of pork, we investigated whether a peptic hydrolysate of denatured porcine crude myosin showed inhibitory activity against angiotensin I-converting enzyme (ACE), which contributed to hypertension. Our results indicated that this hydrolysate showed relatively strong activity, and we therefore attempted to separate the involved peptides, which were considered to be active substances. To isolate these active peptides, the hydrolysate was separated using a solidphase separation, gel filtration high-performance liquid chromatography (HPLC), and two kinds of reverse phase HPLC. In each stage of separation, many fractions were detected, almost all of which showed ACE inhibitory activity. Thus, we suggested that the activity of the hydrolysate as a whole was a result of the activities of the many individual peptides. Six peaks were distinguished, with yields from 34 to 596 ppm of original crude myosin. In addition to the six peaks, many other active fractions were found throughout the separation steps, strongly suggesting that whole porcine crude myosin itself had ACE inhibitory activity. Moreover, pork as food was considered to function as an ACE inhibitory material in vivo, because pork proteins consist primarily of crude myosin, which included almost all the myofibrillar structural proteins.

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.

담수어 열수추출물 및 효소가수분해물의 Angiotensin I 전환효소 저해작용 (Angiotensin I Converting Enzyme Inhibitory Activity of Hot-Water Extract and Enzymatic Hydrolysate of Fresh Water Fish)

  • 김태진;윤호동;이두석;장영순;서상복;염동민
    • 한국식품영양과학회지
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    • 제25권5호
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    • pp.871-877
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    • 1996
  • 담수산 어류의 고도이용과 이들 추출물의 기능적 특성 해명을 위하여 전통적인 건강보양식품으로 애용되어 온 담수산 어류를 대상으로 열수추출물과 효소 가수분해물을 제조하고 이들의 ACE 저해작용 및 gel 여과에 의한 ACE 저해획분을 분리하고 그 특성을 알아 보았다. 열수추출물과 효소 가수분해물의 ACE 저해활성은 담수어류 중 잉어가 가장 높았으며, 효소가 수분해물이 열수추출물에 비하여 강한 경향을 보였다. Ethanol가용성 획분이 침전획분에 비하여 강한 ACE 저해능을 나타내었으며, 잉어 효소 가수분해물의 70% ethanol 가용성 획분이 가장 높은 ACE 저해율을 나타내었다. ACE 저해효과를 지니는 활성획분의 분자량은 열수추출물에서는 약 1,400이었으며 효소 가수분해물에서는 1,400 보다 다소 큰 것으로 나타났고, 시료 중 잉어 효소 가수분해물이 가장 높은 ACE 저해활성을 나타내었다. 활성회분의 아미노산 조성은 열수추출물에 있어서는 glycine, alanine, leucine, proline등의 합량이 많았으며 효소 가수분해물에 있어서는 aspartic acid, glutamic acid, glycine, alanine, valine, leucine, proline 등의 함량이 많았다. 활성획분의 $IC_{50}$/은 효소가수분해물이 열수추출물에 비하여 낮은 경향이었다.

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Isolation of ACE Inhibiting Peptide from Thermolysin Hydrolysate of Manila clam, Ruditapes philippinarum Proteins

  • Lee, Tae-Gee;Yeum, Dong-Min;Kim, Jin-Soo;Kim, In-Soo;Kim, Seon-Bong
    • 한국어업기술학회:학술대회논문집
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    • 한국어업기술학회 2002년도 추계 수산관련학회 공동학술대회발표요지집
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    • pp.90-91
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    • 2002
  • The angiotensin converting enzyme (ACE) generates the powerful vasoconstrictor angiotensin II by removing the C-terminal dipeptide from the precursor decapeptide angiotensin I (1). The enzyme also inactivates the vasodilator bradykinin (2). There have been many studies on ACE inhibitory substances as functional in food, and ACE inhibitory peptides were isolated (3-5). (omitted)

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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.

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.

멸치 가공선 자숙액 pepsin 가수분해물의 angiotensin 전환효소 저해작용

  • 지청일;이지혜;박덕천;구연숙;박재홍;박영호;김인수;김선봉
    • 한국어업기술학회:학술대회논문집
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    • 한국어업기술학회 2001년도 추계 수산관련학회 공동학술대회발표요지집
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    • pp.171-172
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    • 2001
  • 체내에 널리 분포되어 있는 angiotensin 전환효소(angiotensin converting enzyme, ACE ; peptidyldipeptide hydrolase, EC 3.4.15.1)는 angiotensinogen이 renin의 특이적 분해를 받아서 생성된 불활성형인 angiotensin I의 말단 dipeptide(His-Leu)를 절단하여 octapeptide인 활성형의 angiotensin II로 전환시키며, 이렇게 생성된 angiotensin II는 직접적으로 혈압상승 작용을 하거나 adrenal로부터 sediumretaining steroid hormone인 aldosterone의 유리를 촉진시켜 체내 나트륨을 저류시킨다. (중략)

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Assessment of the Inhibitory Activity of Peptide Extracts from Hanwoo Musculus Longissimus on Angiotensin I-Converting Enzyme

  • Seol, Kuk-Hwan;Song, Ji-Hye;Prayad, Thirawong;Kim, Hyoun-Wook;Jang, Ae-Ra;Ham, Jun-Sang;Oh, Mi-Hwa;Kim, Dong-Hun;Lee, Moo-Ha
    • 한국축산식품학회지
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    • 제31권5호
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    • pp.663-667
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    • 2011
  • This study was performed to measure the angiotensin I-converting enzyme (ACE) inhibitory activity of peptide extracts derived from the enzymatic proteolysis of Hanwoo Musculus longissimus (M. longissimus) during cold storage. Thermolysin (80 ppm, w/w) and protease type XIII (100 ppm, w/w) were injected separately or in combination for the enzymatic proteolysis of sarcoplasmic and myofibrillar proteins prior to storage at $5^{\circ}C$ (T1) or at $-1^{\circ}C$ (T2) in a chilling room for 9 days. Beef injected with thermolysin (E2) and thermolysin+protease type XIII (E3) showed a significantly higher degree of hydrolysis at both storage temperatures (p<0.05). During the storage period, T1E2 at day 6 and T1E3 at day 9 showed the strongest ACE inhibitory activity with sarcoplasmic and myofibrillar protein proteolysates. Macromolecules greater than 10,000 Da were removed by ultra filtration, and the filtrates were separated into fractions using gel filtration. Five and three major fractions were collected from S-T1E2-6 and M-T1E3-9 extracts, respectively, and the $4^{th}$ fraction of the S-T1E2-6 extracts showed the highest ACE inhibitory rate of $61.96{\pm}7.41%$.

구증구포 처리 대두 추출물의 항산화 활성 및 Angiotensin-I Converting Enzyme 저해 효과 (Effect on Angiotensin-I Converting Enzyme Inhibition and Antioxidant Activities of Soybean (Glycine max L.) following Steaming and Drying Nine Times)

  • 김현영;서혜영;서우덕;이미자;최만수;함현미
    • 한국식품영양학회지
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    • 제33권2호
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    • pp.167-173
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    • 2020
  • To increase the functional material content of soybean, a repetitive steaming and drying process was used. We investigated the changes in the total polyphenol content, the antioxidant activity, and the angiotensin-I converting enzyme (ACE) inhibition in soybean following nine rounds of steaming and drying. Soybean was steamed 9 times for 2 h and then dried 9 times from 55℃ to 73℃ for 3 h. The total polyphenol content in the soybean reached a maximum value of 60.47 mg GAE eq./100 g at 73℃ while the total polyphenol content in the raw soybean reached 25.17 mg GAE eq./100 g. In the raw soybean samples, the DPPH radical scavenging activity (5 mg/mL) was 8.04% but it increased by 43.29% after drying 9 times to 73℃. ABTS radical scavenging activity also improved following 9 rounds of steaming and drying. ACE inhibitory activity of the soybean dried 9 times at 73℃ was 58.94% at 10 mg/mL. These results showed that steaming and drying soybean 9 times enhanced the antioxidant activity and the ACE inhibitory activity of soybean. Therefore, more research on the biological and anti-hypertensive activity of soybean using this steaming and drying method is necessary.

γ-Aminobutyric Acid (GABA) Production and Angiotensin-I Converting Enzyme (ACE) Inhibitory Activity of Fermented Soybean Containing Sea Tangle by the Co-Culture of Lactobacillus brevis with Aspergillus oryzae

  • Jang, Eun Kyeong;Kim, Nam Yeun;Ahn, Hyung Jin;Ji, Geun Eog
    • Journal of Microbiology and Biotechnology
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    • 제25권8호
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    • pp.1315-1320
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    • 2015
  • To enhance the γ-aminobutyric acid (GABA) content, the optimized fermentation of soybean with added sea tangle extract was evaluated at 30℃ and pH 5.0. The medium was first inoculated with Aspergillus oryzae strain FMB S46471 and fermented for 3 days, followed by the subsequent inoculation with Lactobacillus brevis GABA 100. After fermentation for 7 days, the fermented soybean showed approximately 1.9 g/kg GABA and exhibited higher ACE inhibitory activity than the traditional soybean product. Furthermore, several peptides in the fraction containing the highest ACE inhibitory activity were identified. The novel fermented soybean enriched with GABA and ACE inhibitory components has great pharmaceutical and functional food values.