• BMB Reports
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• v.31 no.5
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• pp.459-467
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• 1998

A new set of functional group interaction energy descriptors relevant to the ACE (Angiotensin-Converting Enzyme) inhibitory peptide, QSAR (Quantitative Structure Activity Relationships), is presented. The functional group interaction energies approximate the charged interactions and distances between functional groups in molecules. The effective energies of the computationally derived geometries are useful parameters for deriving 3D-QSAR models, especially in the absence of experimentally known active site conformation. ACE is a regulatory zinc protease in the renin-angiotensin system. Therapeutic inhibition of this enzyme has proven to be a very effective treatment for the management of hypertension. The non bond interaction energy values among functional groups of six-feature of ACE inhibitory peptides were used as descriptor terms and analyzed for multivariate correlation with ACE inhibition activity. The functional group interaction energy descriptors used in the regression analysis were obtained by a series of inhibitor structures derived from molecular mechanics and semi-empirical calculations. The descriptors calculated using electrostatic and steric fields from the precisely defined functional group were sufficient to explain the biological activity of inhibitor. Application of the descriptors to the inhibition of ACE indicates that the derived QSAR has good predicting ability and provides insight into the mechanism of enzyme inhibition. The method, functional group interaction energy analysis, is expected to be applicable to predict enzyme inhibitory activity of the rationally designed inhibitors.

• Korean Journal of Food Science and Technology
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• v.32 no.4
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• pp.920-927
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• 2000

Angiotensin converting enzyme(ACE) inhibitory activity of Kimchi added with salted-fermented fish products(SFFP), such as salted-fermented anchovy(SFA), salted-fermented anchovy sauce(SFAS), low salt-fermented anchovy sauce(LSFAS), salted-fermented small shrimp(SFS), low salt-fermented sandlance sauce(LSFSS) and their alternatives, such as oyster hydrolysate(OH), Alaska pollack hydrolysate(APH) and sea-staghorn extract(SSE) were studied during fermentation at $20^{\circ}C,\;10^{\circ}C\;and\;4^{\circ}C$. ACE inhibitory activities of Kimchi samples added with SFFP were increased until some fermentation period and then kept similarly constant levels at every fermentation temperature. Similar tendencies were occurred in amino nitrogen (AN) content. ACE inhibitory activities of Kimchi samples added with SFFP alternatives rapidly increased in 1st or 2nd day fermentation and then very slowly increased but AN contents showed roughly constant levels $(400{\sim}600\;mg/100\;g)$ in every fermentation temperature. Kimchi added with LSFAS had higher ACE inhibitory activity (>80%) with elevated level of AN (>600 mg/100 g) among the tested Kimchi samples. Kimchi samples added with SFFP alternatives also showed comparable activity to Kimchi added with SFFP This study shows that Kimchi added with SFFP and their alternatives is a good source as a functional food.

• Journal of the Korean Society of Food Science and Nutrition
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• v.32 no.8
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• pp.1318-1322
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• 2003

This study was carried out to identify the biophysical utility of bioflavonoids by the determination of their antioxidative activities, radical scavenging activity and inhibitory effect on the ACE activity. The results obtained were as follows; All flavonoids experimented greatly inhibited the linoleic acid oxidation from the early period of oxidation, and the radical scavenging ability was also greater in genistein and daidzein than other flavonoids, generally showing donating ability. Rutin has the metal-chelating ability with C $u^{2+}$ and $Mg^{2+}$, which means to have the inhibitory effect on the promotive oxidation of lipid by metal ion. All flavonoids experimented inhibited the angiotensin converting enzyme (ACE) activity, which was greater in genistein and daidzein than other flavonoids.s.

• Journal of the Korean Society of Food Science and Nutrition
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• v.38 no.12
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• pp.1672-1678
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• 2009

This study was carried out to investigate the total polyphenol, total flavonoid content, antioxidant activity, angiotensin I-converting enzyme (ACE) inhibitory activity, $\alpha$-glucosidase inhibitory activity, and antiproliferation activity of the citron seed. The citron seed were separated to hull and embryo, and extracted with n-hexane and 70% ethanol. Antioxidant activity of ethanol extract was higher than that of n-hexane extract. IC50 value for DPPH radical scavenging activity of ethanol extract of hull (CSE1) and embryo (CSE2) were 3.18 and 8.43 mg/mL, and those of total antioxidant activity were 19.96 and 11.28 mg AA eq/g, respectively. ACE inhibitory activity and $\alpha$-glucosidase inhibitory activity on CSE1 showed the highest values of 31.61 and 45.17%, respectively. Antiproliferation effects on the MCF7, HepG2, H460, HCT-116, and PC3 cell line showed the highest values of 14.09, 19.12, 12.29, 9.78, and 9.12% in extract concentration of 5 mg/mL, respectively. These results suggested that citron seed can be used for development of functional food material which have biological activities.

• Journal of Life Science
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• v.8 no.3
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• pp.312-317
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• 1998

This study was designed to investigate the angiotensin convertin enzyme (ACE) inhibitory activity of skipjack/yellowpin tuna cooking broth. The cooking broth was pretreated with membrane filter (MW cut-off 5,000) to obtain the peptide fraction with ACE inhibition. the crude peptides fractionated with Amberlite IR-120 ($H^{+}$ form and followed by Bio-gel P-2, were separated into nine fractions (T-1 to T-9). The maximum inhibitory activity was observed in the fraction T-4 ($IC_{50}$ value, 0.619mg/ml). The abundant amino acids obtained from active fraction T-4 were phenylaanine, leucine and glutamic acid.

• Journal of Applied Biological Chemistry
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• v.49 no.3
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• pp.82-85
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• 2006

Eucommia ulmoides bark extracts by cold water, boiling water, 100% EtOH, 70% EtOH, 100% MeOH, 70% MeOH and $CHCl_3$ were assayed for their medicinal effects. The antioxidant activity of the extracts ranged from $IC_{50}$ 125.2 to $IC_{50}\;872.7{\mu}g/ml$ in the 1,1-diphenyl-2-picrylhydrazyl (DDPH) free radical-scavenging assay, and cold water extracts had the highest antioxidant activity. $CHCl_3$ extracts had the highest inhibitory effect on angiotensin I-converting enzyme (ACE) giving inhibition of up to 56.4% at a concentration of 1 mg/ml. Extracts in 100% EtOH had the greatest inhibitory effect on $\acute{a}-amylase$ activity ($IC_{50}=174.6{\mu}g/ml$), and 70% MeOH extracts had the greatest inhibitory effect on ${\alpha}-glucosidase$ activity ($IC_{50}=14.0{\mu}g/ml$). Taken together, these results provided the in vitro evidence on the ACE, amylase and glucosidase inhibitory actions of E. ulmoides bark that form the pharmacological basis for its antihypertensive and antidiabetic action.

• The Korean Journal of Food And Nutrition
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• v.18 no.1
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• pp.11-18
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• 2005

Angiotensin Ⅰ converting enzyme(ACE) inhibitory activities of laver(Porphyra tenera) protein hydrolysates were investigated by enzymes used for hydrolysis, molecular fractions and drying methods. For the enzymatic hydrolysis, crude laver protein, separated by filtration of water extract of dried laver extracted with 20 times(w/v) water for 3 hours at boiling temperature, were hydrolyzed with three commercial protease, Pepsin, alcalase and maxazyme NNP at optimal conditions. The yield of hydrolysis and ACE inhibitory activities of which were high in order of pepsin, alcalase and maxazyme NNP. ACE inhibitory activities of laver hydrolysates by molecular levels were high in order of 3 kDa > 10 kDa > 3∼10 kDa, and the IC/sub 50/ ACE inhibitory activities by molecular lebels were 4 mg/mL(3 kDa), 5 mg/mL(total hydrolysate), and 20 mg/mL(10 kDa), respectively. The storage stability of dried laver hydrolysates at 20℃ were strongly affected by drying methods, hot air dried of which were much stabler than freeze-dried one.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.34 no.2
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• pp.164-172
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• 2001

The angiotensin-I converting enzyme (ACE) inhibitors from laver hydrolysate was isolated. Among the 13 kinds of proteases, Maxazyme NNP was most effective for preparing the high ACE inhibitory compound. In extraction conditions of ACE inhibitory peptide from laver hydrolysate, ACE inhibitory activity of hydrolysate treated with diethylether for decolorization and that of $70\%$ ethanol soluble fraction among the different ethanol concentrations were higher than other preparations. Low molecular fraction less than 3,000 dalton of layer hydrolysate separated by ultrafiltration had the highest ACE inhibitory activity, for further separation of ACE inhibitory peptide from laver hydrolysate, gel filtration chromatography (Sephadex G-25), reverse-phase HPLC (ODS & Vydac C-18) and gel permeation chromatography (Superdex Peptide HR) were performed. The molecular mass of the ACE inhibitory peptide fractions of gel permeation chromatography determined by electrospray-mass spectrometer were 413.48 (S1O2V2V1P),346.86 (S1O2V2V2P) and 320.32 (S2O6V3V1P) dalton and their amino acid sequence were Val-Gln-Gly-Asn, Thr-Glu-Thr and Phe-Arg, respectively.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.31 no.6
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• pp.875-881
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• 1998

To develop functional food material with angiotensin converting enzyme (ACE) inhibitory peptides, muscle protein of anchovy, Engraulis japonica was hydrolyzed during 48 hrs by digestive pretenses such as pepsin, trypsin, $\alpha$-chymotrypsin, and commercial proteases such as papain, bromelain, complex enzyme, Elavourzyme, Novozym, Neutrase, Protamex and Alcalase. The only $50\%$ ethanol soluble hydrolysates were tested for inhibitory activity against ACE and yield of $50\%$ ethanol soluble peptide-nitrogen ($ESPN_{50}$). ACE inhibition effects and yield of $ESPN_{50}$ occurred as hydrolysis time increased to 8 hrs, Among those pretenses tested, hydrolysates by Alcalase and $\alpha$-chymohypsin had greater ACE inhibitory activity (80 and $74\%$, reipectively) with eletated levels of $ESPN_{50}$ (48 and 58 mg/ml, respectively), while Protamex hydrolysates had greater ACE inhibitory activities ($73\%$) with reduced levels of $ESPN_{50}$ (7.2mg/ml) than others. Amino acid compositions of $50\%$ ethanol solubles obtained from those hydrolysates were rich in glutamic acid, aspartic acid, cysteine and leucine.

• Horticultural Science & Technology
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• v.28 no.5
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• pp.857-863
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• 2010

This study was conducted to evaluate the antioxidant activity, Angiotensin I Converting Enzyme (ACE) inhibitory activity, ${\alpha}$-glucosidase inhibitory activity, nitrate synthesis inhibitory activity, and antiproliferation inhibitory effect on ethanol extract and its solvent fractions of $Coreopsis$ $tinctoria$ Nutt. Ethyl acetate fraction was the strongest at 1,1-diphenyl-2-picryl hydrazyl (DPPH) ($IC_{50}=0.100mg{\cdot}mL^{-1}$) and 2,2'-Azino-bis-(3-ethylbenozothiazoline-6-sulfonic acid) (ABTS) (15.785 mg AA $eq{\cdot}10mg^{-1}$) radical scavenging activity, ACE (40.96% at $1mg{\cdot}mL^{-1}$), and ${\alpha}$-glucosidase ($IC_{50}=0.125mg{\cdot}mL^{-1}$) inhibitory effect among the solvent fractions. Nitrate synthesis inhibitory activity of ethanol extract, chloroform fraction, and ethyl acetate fraction effectively inhibited NO formation in a dose-dependent manner without the cytotoxic effect. Ethanol extract and its solvent fractions inhibited growth of HCT-116 colon cancer cells in a dose-dependent manner. n-Hexane fraction showed the highest antiproliferation inhibitory effect of $0.041mg{\cdot}mL^{-1}$ among fractions.