• Title/Summary/Keyword: enzyme inhibitory

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Characterization of Antihypertensive Angiotensin I-Converting Enzyme Inhibitor from Saccharomyces cerevisiae

  • KIM, JAE-HO;LEE, DAE-HYOUNG;JEONG, SEOUNG-CHAN;CHUNG, KUN-SUB;LEE, JONG-SOO
    • Journal of Microbiology and Biotechnology
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    • v.14 no.6
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    • pp.1318-1323
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    • 2004
  • This study describes the purification and characterization of a novel antihypertensive angiotensin 1­converting enzyme (ACE) inhibitory peptide from Saccharomyces cerevisiae. Maximal production of the ACE inhibitor from Saccharomyces cerevisiae was obtained from 24 h of cultivation at $30^{\circ}C$ and its ACE inhibitory activity was increased by about 1.5 times after treatment of the cell-free extract with pepsin. After the purification of ACE inhibitory peptides with ultrafiltration, Sephadex G-25 column chromatography, and reverse-phase HPLC, an active fraction with an $IC_{50}$ of 0.07 mg and $3.5\%$ yield was obtained. The purified peptide was a novel decapeptide, showing very low similarity to other ACE inhibitory peptide sequences, and its amino acid sequence was Tyr-Asp-Gly-Gly-Val-Phe-Arg-Val-Tyr-Thr. The purified inhibitor competitively inhibited ACE and also showed a clear antihypertensive effect in spontaneously hypertensive rats (SHR) at a dosage of 1 mg/kg body weight.

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.

Antioxidant and Angiotensin I Converting Enzyme Inhibitory Activities of Red Snow Crab Chionoecetes japonicas Shell Hydrolysate by Enzymatic Hydrolysis

  • Yoon, Na Young;Shim, Kil-Bo;Lim, Chi-Won;Kim, Sang-Bo
    • Fisheries and Aquatic Sciences
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    • v.16 no.4
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    • pp.237-242
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    • 2013
  • We investigated the antioxidant and angiotensin I converting enzyme (ACE) inhibitory activities of red snow crab Chionoecetes japonicas shell (RSCS) hydrolysate by enzymatic hydrolysis and its molecular weight cut-off fractions. The RSCS hydrolysate was fractionated through two ultrafiltration membranes of 3 and 10 kDa cut-offs. Three fractions (<3 kDa, 3-10 kDa, and >10 kDa) were evaluated for total amino acid composition, antioxidant activities using 2'-azino-bis[3-ethylbenzthiazoline-6-sulfonic acid] ($ABTS^+$) radical scavenging and superoxide dismutase (SOD)-like activities and reducing power assays, and ACE inhibitory activity using Hou's method. Although all fractions showed activity, the <3 kDa fraction of RSCS hydrolysate exhibited the greatest $ABTS^+$ radical scavenging, SOD-like and ACE inhibitory activities. However, these fractions exhibited low reducing power. These results suggest that the low-molecular-weight enzymatic hydrolysate of RSCS could be used as a functional ingredient to control oxidative stress and ACE activity.

Characterization of New Antihypertensive Angiotensin I-Converting Enzyme Inhibitory Peptides from Korean Traditional Rice Wine

  • Kang, Min-Gu;Kim, Jae-Ho;Ahn, Byung-Hak;Lee, Jong-Soo
    • Journal of Microbiology and Biotechnology
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    • v.22 no.3
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    • pp.339-342
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    • 2012
  • This study describes the characterization of a new angiotensin I-converting enzyme (ACE) inhibitory peptide from a Korean traditional rice wine. After purification of the ACE inhibitor peptides with ultrafiltration, Sephadex G-25 column chromatography, and successively $C_{18}$ and SCX solid-phase extraction, reverse-phase HPLC, and size exculsion chromatography, two types of the purified ACE inhibitors with $IC_{50}$ values of 0.34 mg/ml and 1.23 mg/ml were finally obtained. The two purified ACE inhibitors (F-1 and F-2) were found to have two kinds of novel oligopeptides, showing very little similarity to other ACE inhibitory peptide sequences. The amino acid sequences of the two purified oligopeptides were found to be Gln-Phe-Tyr-Ala-Val (F-1) and Ala-Gly-Pro-Val-Leu-Leu (F-2), and their molecular masses were estimated to be 468.7 Da (F-1) and 357.7 Da (F-2), respectively. They all showed a clear antihypertensive effect on spontaneously hypertensive rats at a dosage of 500 mg/kg.

Isolation of Angiotensin Converting Enzyme Inhibitory Component from the Seeds of Xanthium strumarium (창이자(蒼耳子)로부터 안지오텐신 전환효소 억제 유효 성분의 분리)

  • Lee, Yun-Mi;Kang, Dae-Gill;Kim, Myung-Gyu;Jang, Ji-Yeon;Lee, Ho-Sub
    • Journal of Physiology & Pathology in Korean Medicine
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    • v.19 no.1
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    • pp.119-123
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    • 2005
  • In the courses of in vitro screening for the angiotensin converting enzyme (ACE) inhibitory activity of the various extracts from medicinal plants, n-BuOH soluble extract of the seeds of Xanthium strumarium was found to exhibit distinctive angiotensin converting enzyme (ACE) inhibitory activity. Bioassay-guided fractionation and purification of the n-BuOH soluble extract of the seeds of Xanthium strumarium afforded a new $xanthiazone-11-{\beta}-glucopyranoside$. The ACE activity was significantly inhibited by the addition of a new $xanthiazone-11-{\beta}-glucopyranosidein$ a dose-dependent manner of which $IC_{50}$ value was $21.8\;{\mu}g/ml$.

Fractionation and Angiotensin I-converting Enzyme (ACE) Inhibitory Activity of Gelatin Hydrolysates from by-products of Alaska Pollock Surimi

  • Park, Chan-Ho;Kim, Hyung-Jun;Kang, Kyung-Tae;Park, Jae-W.;Kim, Jin-Soo
    • Fisheries and Aquatic Sciences
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    • v.12 no.2
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    • pp.79-85
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    • 2009
  • Gelatin hydrolysates with a high inhibitory activity against angiotensin I-converting enzyme (ACE) were fractionated from Alaska pollock surimi refiner discharge. The ACE-inhibitory activity, expressed as $IC_{50}$ (mg/mL), was highest (0.49 mg/mL) in gelatin hydrolysates formed by sequential 2-hr treatments of Pronase and Flavourzyme. After fractionation through four different membrane filters with molecular weight cut-offs of 3, 5, 10, and 30 kDa, the highest ACE-inhibitory activity (0.21 mg/mL) was observed with the 3-kDa filtrate.

Enzyme Inhibitory and Antioxidant Activities of Fruit and Stem of Opuntia ficus india var. saboten

  • Han, Yong-Nam;Jun, Jae-Suk;Choo, Yeun-Su
    • Proceedings of the Korean Society of Applied Pharmacology
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    • 1998.11a
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    • pp.187-187
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    • 1998
  • The objective was to verify biological activities of fruit and stem of prickly pear(Opuntia ficus indica L. var, saboten Makino). We have determined inhibitory activities on enzymes, such as dopamine ${\beta}$-hydroxylase(DBH), monoamme oxidase A and B(MAO-A, B), and antioxidant activity, in vitro. We purchased dried stem powder and lyophilized fruit powder of prickly pear from CheJu Island, and prepared the extracts with 80% of methanol. The fruit extract showed stronger inhibitory effects on MAO-A and -B and antioxidant activity compared. to the stem extract, on fractionation with hexane, ethyl acetate, butanol and water. Both the stem and the fruit extracts with ethyl acetate showed stronger enzyme inhibitory and antioxidant activities than other extracts. Now we are isolating active principles from both ethyl acetate extracts.

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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.

Inhibitory Effects of Water and 80% Ethanol extracts from Mulberry Leaves (Morus alba L.) on Angiotensin Converting Enzyme and Xanthine Oxidase (뽕잎(Morus alba L.)의 물과 80% Ethanol 추출물의 Angiotensin Converting Enzyme과 Xanthine Oxidase에 대한 활성억제효과 탐색)

  • Cho, Young-Je;Chun, Sung-Sook;Kwon, Hyo-Jung;Kim, Jeung-Hoan;Lee, Kyoung-Hwan;An, Bong-Jeon;Choo, Jai-Weon
    • Applied Biological Chemistry
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    • v.49 no.2
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    • pp.114-124
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    • 2006
  • The objective of this research was to evaluate the ability of water and 80% ethanol extracts from one hundred eight mulberry leaves (Morus alba L.) to influence the inhibitory activity of angiotensin converting enzyme (ACE) and xanthine oxidase (XOase). The total phenol contents were that water extracts of ten species (Kakjayongsan (Morus alba L.), Daejungsun (Morus alba L.) etc.) and 80% ethanol extracts of twenty three species (Waryoung (Morus alba L.), Hasusang (Morus alba L.) etc.) showed more than 15 mg/g. The inhibitory activity on angiotensin converting enzyme (ACE) were that ten species (YamanakkadakKaskke (Morus alba L.), Mijiro (Morus alba L.) etc.) showed 100% inhibition rate both of water extracts and 80% ethanol extracts. The rest, water extracts of thirty four species (Cheongilppong (Morus alba L.) etc.) and 80% ethanol extracts of thirty four species (Wonjukojo (Morus alba L.) etc.) showed inhibitory activity (above 90%) on ACE. Also, to search of xanthine oxidase (XOase) inhibition were that water extracts of five species (Cheongsipjosaeng (Morus alba L.), Suwon 3 (Morus alba L.) etc.) and 80% ethanol extracts of Jeokmok (Morus alba L.) showed inhibitory activity (above 50%) on XOase. This result revealed, strong biological activity in spite of has a little total phenol contents. These water and 80% ethanol extracts from mulberry leaves (Morus alba L.) are expected good candidate for development into anti-hypertentive and anti-gout sources.

The Response of Nitrogen Deposition to Methane Oxidation Availability and Microbial Enzyme Activities in Forest Soils

  • Jang, In-Young;Lee, Hyoung-Min;Kang, Ho-Jeong
    • Environmental Engineering Research
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    • v.15 no.3
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    • pp.157-161
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    • 2010
  • Forest soils are often nitrogen-limited, and nitrogen input to forest soils can cause substantial changes in the structure and functions of a soil ecosystem. To determine the effects of nitrogen input on methane oxidation and the microbial enzyme activities, manipulation experiments were conducted using nitrogen addition to soil samples from Mt. Jumbong. Our findings suggested that the addition of nitrogen to the soil system of Mt. Jumbong did not affect the microbial enzyme activities. Conversely, the addition of nitrogen affected the rate of methane oxidation. Inorganic nitrogen in soils can inhibit methane oxidation via several mechanisms, such as substrate competition, toxic effects, and competition with other microbes, but the inhibitory effects are not always the same. In this research, seasonal changes were found to produce different inhibitory factors, and these different responses may be caused from differences in the methantrophic bacteria community structure.