• Title/Summary/Keyword: ACE Inhibitor

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Purification of Angiotensin I-Converting Enzyme Inhibitory Peptide from Squid Todarodes pacificus Skin (오징어(Todarodes pacificus) 껍질로부터 Angiotensin I 전환효소 저해 펩티드의 분리 정제)

  • Lee, Jung-Kwon;Jeon, Joong-Kyun;Byun, Hee-Guk
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.44 no.2
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    • pp.118-125
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    • 2011
  • In this study, an angiotensin I-converting enzyme (ACE) inhibitor from squid skin was purified and characterized. Squid (Todarodes pacificus) skin protein isolates were hydrolyzed using six commercial proteases: alcalase, ${\alpha}$-chymotrypsin, neutrase, papain, pepsin, and trypsin. The peptic hydrolysate had the highest ACE inhibitory activity. The ACE inhibitory peptide was purified using Sephadex G-25 column chromatography and reverse phase high-performance liquid chromatography (HPLC) with a $C_{18}$ column. The purified ACE inhibitory peptide was identified and sequenced, and found to consist of seven amino acid residues: Ser-Ala-Gly-Ser-Leu-Val-Pro (657Da). The $IC_{50}$ value of the purified ACE inhibitory peptide was 766.2 ${\mu}M$, and Lineweaver-Burk plots suggested that the purified peptide acts as a noncompetitive ACE inhibitor. These results suggest that the ACE inhibitory peptide purified from the peptic hydrolysate of squid skin may be of benefit in developing antihypertensive drugs and functional foods.

Partial Purification of Angiotensin Converting Enzyme Inhibitory Peptide Isolated form Supernatant of Bovine Plasma Treated by Trichloroscetic Acid

  • Park, Eun-Hee;Song, Kyung-Bin
    • Preventive Nutrition and Food Science
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    • v.3 no.4
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    • pp.379-381
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    • 1998
  • An angiotensin converting enzyme (ACE) inhibitor was isolated and partially purified from bovine blood plasma. Bovine blood plasma was obtained after removing blood cells by centrifugation, followed by the addition of anticoagulant to whole bovine blood. To precipitate plasma proteins, bovine blood plasma was treated with 4% trichloroacetic acid (TCA) as a final concentration .An ACE inhibitor was isolated from TCA supernatnat, using ultrafiltration, gel permeation chormatography, and reverse-phase high pressure liquid chromatogrpahy. The ACE inhibitor purified from TCA supernatant had IC50 values of 9.4$\mu$M.

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

  • Hong, Sang-Pill;Kim, Myung-Hee;Oh, Se-Wook;Han, Chan-Kyu;Kim, Yong-Hyun
    • Korean Journal of Food Science and Technology
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    • v.30 no.6
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    • pp.1476-1479
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    • 1998
  • Effect of chitosan oligosaccharides on the ACE (angiotensin I converting enzyme) inhibition and antihypertension in SHR (Spontaneously hypertensive rat) was examined. The ACE inhibition activity was observed in all the chitosan oligosaccharides used in this study, and chitosan trimer exhibited the highest inhibitory activity $(IC_{50}=0.9{\mu}M)$ compared with other chitosan oligosaccharides $(IC_{50}\;:\;2.4{\sim}100\;{\mu}M)$. The results suggested that chitosan trimer was a good inhibitor of ACE in molecular level. When the single oral dose (2.14 mg/kg, similar to dose level of Captopril, known as strong ACE inhibitor) of chitosan trimer was given to 8 or 21 week aged SHR, the blood pressure reduction of both SHRs in 4hrs were $27{\pm}4.8\;mmHg\;and\;36{\pm}4.3\;mmHg$, respectively. Therefore, it was suggested that chitosan trimer could be applicable as natural ACE inhibitor related to antihypertension.

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Identification and Culture Conditon of an Actionomycetes Stranin Producing an Angiotensin Converting Enzyme Inhibitor (Angiotensin Converting Enzyme(ACE) 저해제를 생성하는 방선균 분리주의 동정 및 최적 발효조건)

  • Moon, Seong-Hoon;Ha, Sang-Chul;Lee, Dong-Sun;Kim, Jong-Guk;Hong, Soon-Duck
    • Microbiology and Biotechnology Letters
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    • v.23 no.4
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    • pp.439-445
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    • 1995
  • Identification of Actinomycetes isolate strain SH-8002, a producer of ACE inhibitor, based on procedures employed in the international Streptomyces project. The strain, designated as SH-8002, was identified as Streptomyces zoamyceticus SH-8002 based on its morphological, physiological, biochemical and chemotaxonomic characteristics. The ACE inhibitor produced by the strain was highly achieved in fermentation medium condition that was 1% soluble starch, 0.5% tryptone, 0.2% K$_{2}$HPO$_{4}$, 0.2% CaCO$_{3}$, 0.1% NaCl, pH 8.0 at 30$\circ$C for 144 hrs.

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Isolation of Angiotensin Converting enzyme inhibitors from Ripe Cucurbita moschata Duch

  • Hyeyoung Jung;Song, Kyung-Bin
    • Preventive Nutrition and Food Science
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    • v.6 no.4
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    • pp.244-246
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    • 2001
  • Angiotensin converting enzyme (ACE) inhibitor acts on the inhibition of ACE and causes a decrease in blood pressure. There have been several reports on screening of ACE inhibitors from natural food products and protein hydrolysates of various food sources. Ripe Cucurbita moschata Duch has been used as an oriental medicine in Korea. To isolate ACE inhibitors, crude water extracts of the edible portion of ripe Cucurbita moschata Duch were obtained after heating in water at 95$^{\circ}C$ for 2 h. Crude extracts were then filtered using PM-10 and YM-1 membranes. The membrane-filtered solution was loaded onto Sephadex G-15 column equlibrated with a phosphate buffer. Among the four major fractions of gel permeation chromatography, the second fraction had the highest inhibitory activity of 65%. Further purification of the fraction using reversed-phase HPLC with a $C_{18}$ column produced ACE inhibitors, which were identified as a mixture having molecular mass of 222 and 273 by Tandem mass spectrometry.

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Isolation of Angiotensin Converting Enzyme Inhibitory Peptide from Beef Bone Extract Hydrolysate

  • Park, Eun-Hee;Cho, Yong-Sik;Song, Kyung-Bin
    • Applied Biological Chemistry
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    • v.41 no.4
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    • pp.270-272
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    • 1998
  • Angiotensin converting enzyme (ACE) inhibitor was isolated from beef bone extract hydrolysate. After hydrolysis of beef bone extract with a commercial protease, ACE inhibitory peptide was purified by using ultrafiltration, gel permeation chromatography, and reverse-phase high pressure liquid chromatography. The purified ACE inhibitor was a pentapeptide, Gly-Pro-X-Gly-Pro.

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Isolation of Angiotensin I Converting Enzyme (ACE) Inhibitor from fermented oyster, Crassostrea gigas

  • Park, Ji-Young;Je, Jae-Young;Park, Pyo-Jam;Kim, Se-Kwon
    • Proceedings of the Korean Society of Fisheries Technology Conference
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    • 2002.10a
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    • pp.193-194
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    • 2002
  • Angiotensin I converting enzyme (ACE) inhibitor was purified from Crassostrea gigas. The ACE belongs to the class of metalloprotease. This enzyme plays an important physiological role in regulating blood pressure of the rennin-angiotensin system by converting from angiotensin I to octapeptide angiotensin II, a potent vasoconstrictor and by inactivating bradykinin, which has depressor action. (omitted)

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Physiological Functionality of Various Extracts from Danmemil and Legumes (단메밀과 콩 추출물들의 생리 기능성)

  • 김동희;이국영;김나미;이종수
    • The Korean Journal of Food And Nutrition
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    • v.16 no.4
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    • pp.347-352
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    • 2003
  • Physiological functionalities of various extracts from Danmemil and legumes were determined and its optimal extraction conditions were also investigated. Angiotensin I-converting enzyme (ACE) inhibitory activity and tyrosinase inhibitory activity of Danmemil were higher in water extracts (53%, 58%) than those of ethanol extracts. However, its electron-donating ability was the highest in ethanol extracts (72%). ACE inhibitory activity and electron-donating ability of Black bean No. 1 and Taekwangkong(one of bean) were higher in water extracts than those of ethanol extracts, whereas SOD-like activity was the highest in ethanol extracts. ACE inhibitor and tyrosinase inhibitor of Danmemil were maximally extracted when it were treated with 20 times of distilled water at 35$^{\circ}C$ for 24 h and 36 h, respectively. Its electron donating compound was maximally extracted by treatment of 50$^{\circ}C$ for 18 h. ACE inhibitor of Black bean No. 1 was extracted maximally when it was treated with distilled water (1 :20) at 20$^{\circ}C$ for 24 h, whereas the other functional compounds were maximally extracted at 20$^{\circ}C$ for 18 h.

ACE inhibitory activity of Peptide from krill(Euphausia superba) Hydrolysate

  • Kim, Dong-Soo;Kim, Young-Myoung;Park, Douck-Choun;Do, Jeong-Ryong
    • Proceedings of the Korean Society of Fisheries Technology Conference
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    • 2001.10a
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    • pp.183-184
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    • 2001
  • Angiotensin I converting enzyme (ACE) in renin-angiotensin system is a cause of essential hypertension, which covers most hypertension, one of the major adult diseases. Thus, the inhibition of ACE would be indispensable for the prevention and cure of hypertension. Therefore, a lot of studies on the ACE inhibitor have been conducted. Peptides from the protein hydrolysate have been reported as an remarkable inhibitor. Especially, various ACE inhibitory peptides were isolated and identified from marine products for their utilization as value added products. (omitted)

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Antihypertensive Angiotensin I-Converting Enzyme Inhibitory Activity and Antioxidant Activity of Vitis hybrid-Vitis coignetiae Red Wine Made with Saccharomyces cerevisiae

  • Jang, Jeong-Hoon;Lee, Jong-Soo
    • Mycobiology
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    • v.39 no.2
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    • pp.137-139
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    • 2011
  • A Vitis hybrid-Vitis coignetiae red wine was vinified by fermentation of a mixture of a Vitis hybrid.Vitis coignetiae must with Saccharomyces cerevisiae KCTC 7904 at $25^{\circ}C$ for 10 days. The Vitis hybrid-Vitis coignetiae red wine showed high antihypertensive angiotensin I-converting enzyme (ACE) inhibitory activity (67.8%) and antioxidant activity (76.7%). The antihypertensive ACE inhibitor in the Vitis hybrid-Vitis coignetiae red wine was partially purified by solid phase extraction chromatography, and its ACE inhibitory activity yielded an $IC_{50}$ of 1.8 mg/mL. Six kinds of oligopeptides, including five new kinds, were contained in the partially purified ACE inhibitor fraction from the red wine after 10 days of fermentation. Antioxidant activity decreased significantly from 76.7% to 40.5% when the post-fermentation period was prolonged to 30 days.