• Title/Summary/Keyword: enzyme inhibitory activity

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Effects of Polyacetylenes from Panax ginseng on Some Microsomal and Mitochondrial Enzymes

  • Kim, Young-Sook;Kim, Shin-Il;Hahn, Dug-Ryong
    • Korean Journal of Pharmacognosy
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    • v.20 no.3
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    • pp.154-161
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    • 1989
  • Effects of panaxydol, panaxynol and panaxytriol isolated from Panax ginseng C.A. Meyer on some enzyme activities were determined. Activities of ATPase, membrane-bound enzyme from Sarcoma 180 and rat liver were slightly inhibited by panaxydol. Activities of 5'-nucleotidase, membrane-bound enzyme and succinate cytochrome c reductase in mitochonidria from sarcoma 180 and rat livers were significantly inhibited in a dose-dependent manner by panaxynol. The inhibitory effects of panaxydol and panaxynol on succinate cytochrome c reductase activities were more potent than those on 5'-nucleotidase activities and panaxynol was found to be a very potent inhibitor of succinate cytochrome c reductase. Activities of glucose-6-phosphatase in endoplasmic reticulum from Sarcoma 180 and rat livers were not affected by all three polyacetylenes. These results suggested that the inhibitory effects of panaxydol and panaxynol on enzyme activities might contribute to their biological activities.

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Inhibitory Effects of Angiotensin Converting Enzyme and α-Glucosidase, and Alcohol Metabolizing Activity of Fermented Omija (Schizandra chinensis Baillon) Beverage (오미자 발효음료의 알코올 분해능과 Angiotensin Converting Enzyme 및 α-Glucosidase 저해효과)

  • Cho, Eun-Kyung;Cho, Hea-Eun;Choi, Young-Ju
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.39 no.5
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    • pp.655-661
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    • 2010
  • The nutraceutical role of fermented omija (Schizandra chinensis) beverage (FOB) was determined through the analysis of fibrinolytic and alcohol metabolizing activities, nitrite scavenging activity, and angiotensin converting enzyme and $\alpha$-glucosidase inhibitory effects. Firstly, FOB increased fibrinolytic activity in a dose-dependent manner and indicated angiotensin converting enzyme inhibitory activity of 94.8% at 20% FOB (0.6 mg/mL). In addition, the inhibitory activities of FOB on $\alpha$-amylase and $\alpha$-glucosidase were determined to be 100% at 100% FOB (3 mg/mL) and 49% at 60% FOB (1.8 mg/mL), respectively. Nitrite scavenging activity of FOB was about 96.1%, 72.3%, and 68.3% on pH 1.2, 3.0, and 6.0 at 100% FOB, respectively. To determine influence of FOB on alcohol metabolism, the generating activities of reduced-nicotinamide adenine dinucleotide (NADH) by alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase (ALDH) were measured. Facilitating rate of ADH activity was 70.3% at 50% FOB, but ALDH activity was not affected. These results revealed that FOB has a strong alcohol metabolizing activity, and fibrinolytic and nitrite scavenging activities and exhibits the angiotensin converting enzyme, $\alpha$-amylase, and $\alpha$-glucosidase inhibitory activities.

Effect of Alum on the Activity of Raw Starch-Digesting Enzyme Produced by Bacillus sp. (Bacillus sp.가 생산하는 전분 분해효소의 활성에 미치는 Alum첨가의 영향)

  • Lee, Shin-Young;Lee, Sang-Gui;Kang, Tae-Su;Lee, Myong-Yul
    • Korean Journal of Food Science and Technology
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    • v.27 no.5
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    • pp.773-775
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    • 1995
  • The effect of alum$(Al{\cdot}K(SO_4)_2{\cdot}12H_{2}O)$ on the activity of raw starch-digesting enzyme produced by alkali-tolerant Bacillus sp. was investigated. In adding alum of 0.5%(w/w), activities of raw starch-digesting enzyme on the gelatinized and raw rice starches have not been inhibited. In case of adding alum of 5%(w/w), competitive and uncompetitive inhibition were observed for the gelatinized and raw rice starches, respectively. The inhibitory effect on the raw starch was much higher than that on the gelatinized starch.

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Peptide Inhibitor for Angiotensin-Converting Enzyme from Thermolysin Hydrolysate of Manila Clam Proteins

  • Lee Tae-Gee;Yeum Dong-Min;Kim Young-Sook;Yeo Saeng-Gyu;Lee Yong-Woo;Kim Jin-Soo;Kim In-Soo;Kim Seon-Bong
    • Fisheries and Aquatic Sciences
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    • v.8 no.2
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    • pp.109-112
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    • 2005
  • A peptide that inhibits angiotensin-converting enzyme (ACE) was isolated from a hydrolysate of Manila clam (Ruditapes philippinarum) proteins prepared with thermolysin. Amino acid sequence of the peptide was determined to be Leu-Leu-Pro. Chemically synthesized Leu-Leu-Pro had an $IC_{50}\;value\;of\;158\;\mu{M}$. Peptides related to the Manila clam-derived peptide were synthesized to study the structure-activity relationships. The tetrapeptide, Leu-Leu-Pro-Pro, had a very weak effect on the enzyme. However, Leu-Leu-Pro-Asn showed no inhibitory activity.

Antioxidative Activity and Inhibition of Angiotensin Converting Enzyme by Lycii fructus Extracts Prepared by Adding White Ginseng and Red Ginseng (구기자 추출물 제조 시 백삼 및 홍삼 첨가에 의한 항산화활성 및 안지오텐신 전환효소에 대한 저해활성 효과)

  • Seong, Bong Jae;Kim, Sun Ick;Jee, Moo Geun;Kim, Soo Dong;Kwon, A Reum;Kim, Hyun Ho;Won, Jun Yeon;Lee, Ka Soon
    • Korean Journal of Medicinal Crop Science
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    • v.26 no.5
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    • pp.370-381
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    • 2018
  • Background: To enhance the taste and physiological characteristics of Lycii fructus (Gugija) extracts, we investigated the changes in the physiological characteristics of Gugija extracts caused by adding white ginseng (WG) and red ginseng (RG) Methods and Results: Gugija extracts, including 10G10, 10GW-G8 : 2, -G6 : 4, -G4 : 6, -G2 : 8, and -G0 (mixtures made by replacing 0, 20, 40, 60, 80, and 100% of Gugija with WG), as well as 10G10, 10GR-G8 : 2, -G6 : 4, -G4 : 6, -G2 : 8, and -G0 (mixture made by replacing 0, 20, 40, 60, 80, and 100% of Gugija with RG) were extracted with water at 10 times the respective mixture's volume. The antioxidant activities of Gugija extracts were investigated by assessing their 1,1-diphenyl-2-picrydrazyl (DPPH) and 2,2'-azinobis(3ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activity, ferric reducing antioxidant potential (FRAP) activity, nitrite scavenging activity, and angiotensin converting enzyme (ACE) inhibitory activity. As the amount of WG added increased, the DPPH, and, ABTS radical scavenging activity, and FRAP activity of the Gugija extract decreased. The half maximal inhibitory concentration ($IC_{50}$) value of 10G10, 10GW-G6 : 4, 10GR-G6 : 4, and 10GR-G0 for DPPH radical scavenging activity were $25.50{\pm}1.04$, $52.06{\pm}1.46$, $16.87{\pm}1.24$, and $9.50{\pm}0.16{\mu}{\ell}/m{\ell}$, respectively. On the other hand, the physiological activity of Gugija extract increased with the addition of increasing amounts of RG. However, ACE inhibitory activity was the highest ($50.25{\pm}2.58%$) in the Gugija 10-fold extract without any added RG. Conclusions: From the above results, we suggest that adding RG to Gugija extracts increase their antioxidant, FRAP, and nitrite scavenging activities.

Antidiabetes and Angiotensin Converting Enzyme Inhibitory Activity of Sonchus asper (L) Hill Extract (큰방가지똥 추출물의 항당뇨 및 항고혈압효과)

  • Xu, Ming-Lu;Wang, Lan;Xu, Gui-Fang;Wang, Myeong-Hyeon
    • Korean Journal of Pharmacognosy
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    • v.42 no.1
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    • pp.61-67
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    • 2011
  • In this study, we evaluated the bioactivities of methanol extract and its solvent fractions of Sonchus asper (L.) Hill. The EtOAc fraction of S. asper exhibited more strong antioxidant activity than other extracts as evidenced by the strongest 1,1-diphenyl-2-picryl hydrazyl (DPPH) radical scavenging activity with a $EC_{50}$ value at $33.55\;{\mu}g/mL$ and reducing power, the total polyphenol (180.71 mg GAE/g) and flavonoid contents (145.86 mg QE/g) of S. asper extract were higher than other extracts. The EtOAc fraction of the S. asper also showed 47.38% mushroom tyrosinase inhibition activity, 56.22% ${\alpha}$-glucosidase inhibition and 46.58% ${\alpha}$-amylase inhibition ratio at 1 mg/mL. Both methylene chloride and EtOAc fractions of methanol extract of S. asper effectively reduced of the 86.34% and 62.03% angiotensin I converting enzyme (ACE) activity at 2 mg/mL, respectively. These findings suggest that the EtOAc fraction of the S. asper could be a potential antioxidant in food additive, medicinal, and industry product.

Inhibitory Effect of Trans-N-p-Coumaroyl Tryamine from the Twigs of Celtis chinensis on the Acetylcholinesterase

  • Kim, Dae-Keun;Lee, Kie-Seung
    • Archives of Pharmacal Research
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    • v.26 no.9
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    • pp.735-738
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    • 2003
  • The methanolic extract of the twigs of Celtis chinensis was found to show inhibitory activity on acetylcholinesterase (AChE), an enzyme that plays a role in the metabolic hydrolysis of ACh. Bioassay-guided fractionation of the methanolic extract resulted in the isolation of N-p-coumaroyl tyramine. as an inhibitor on AChE. This compound inhibited AChE activity in a dose-dependent manner, and the $IC_50$ value of trans-N-p-coumaroyl tyramine was 34.5 $\mu$g/mL (122 $\mu$M).

ACE Inhibitory and Antioxidative Activities of Silkworm Larvae (Bombyx mori) Hydrolysate (번데기 가수분해물의 ACE 저해활성과 항산화활성)

  • Yu, Jung-Sik;Woo, Koan-Sik;Hwang, In-Guk;Lee, Youn-Ri;Kang, Tae-Su;Jeong, Heon-Sang
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.37 no.2
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    • pp.136-140
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    • 2008
  • In order to utilize the silkworm larvae (Bombyx mori) protein, defatted silkworm protein was hydrolysed by four enzymes (pepsin, trypsin, neutrase and alcalase) at various hydrolysis times (6, 12, 18, 24 and 30 hr) and suspension concentrations (2, 5, 10, 15 and 20%). Protein solubility index, ACE (angiotensin converting enzyme) inhibitory activity and antioxidative activity of silkworm protein hydrolysates were investigated. The optimum condition of hydrolysis was 10% suspension concentration and 18 hr. Protein solubility index of trypsin treatment was higher than other enzyme treatments. ACE inhibitory activity and $IC_{50}$ value of antioxidative activity of neutrase treatment were 86.16% at $100\;{\mu}g/mL$ and $352.75\;{\mu}g/mL$, respectively; also, these values were higher than other enzyme treatments.

Angiotensin I-Converting Enzyme Inhibitory Activity of the ${\kappa}-Casein$ Fragments Hydrolysated by Chymosin, Pepsin, and Trypsin (${\kappa}-Casein$의 Chymosin, Pepsin 및 Trypsin 가수분해물에 대한 안지오텐신 변환효소 저해효과의 탐색)

  • Oh, Se-Jong;Kim, Sae-Hun;Kim, Sang-Kyo;Baek, Young-Jin;Cho, Kyung-Hyun
    • Korean Journal of Food Science and Technology
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    • v.29 no.6
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    • pp.1316-1318
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    • 1997
  • The isolated ${\kappa}-Casein$ on gel permeation chromatography was hydrolyzed by chymosin, trypsin, and pepsin. The 3% TCA soluble portion of the hydrolysates were dialyzed on the angiotensin-I converting enzyme (ACE) inhibition rate (%,) and inhibitory activity $(IC_{50})$ were determined. The trypsin hydrolysate exhibited the highest ACE inhibition rate while the chymosin hydrolysation showed the lowest activity. The hydrolysate was dialyzed using dialysis membrane with various molecular cut-offs, and $IC_{50}$ was determined. As the pore size of the dialysis tubing increased, the ACE inhibitory activity decreased.

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Angiotensin-I Converting Enzyme Inhibitory Activity of Algae (해조류의 Angiotensin-I 전환효소 저해작용)

  • LEE Heon-Ok;KIM Dong-Soo;DO Jeong-Ryong;KO Young-Su
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.32 no.4
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    • pp.427-431
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    • 1999
  • This study was conducted to investigate the inhibitory activity of water extracts and its enzymatic hydrolysates from algae against angiotensin-I converting enzyme (ACE). The 7 kinds of algae were extracted with water at $50^{\circ}C,\;70^{\circ}C$ and $98^{\circ}C$. ACE inhibitory activities of water extracts were the highest at $70^{\circ}C$, and those of ceylon moss, layer, green layer, sea mustard, seaweed fusiforme sea tangle and sea staghorn were $10.9\%,\;9.3\%,\;8.9\%,\;8.2\%,\;7.5\%,\;7.1\%$ and $7.0\%$, respectively. Layer, green laver sea mustard and ceylon moss of high ACE inhibitory activities among the 7 kinds of water extracts were hydrolyzed by maxazyme and papain during 24hrs. ACE inhibitory activity of enzymatic hydrolysates was higher than that of water extracts, and was the highest in enzymatic hydrolysates of laver among the tested samples. In laver hydrolysates by proteases, the highest ACE inhibitory activity and peptide-nitrogen contents were observed at 8 hours hydrolysis and the hydrolysates by maxazyme showed relatively higher activity than those by papain(31.3 and $27.9\%$, respectively). But peptide-nitrogen contents were greater in papain hydrolysates than in maxazyme.

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