• KSBB Journal
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• v.28 no.2
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• pp.131-136
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• 2013

The hydrolysates prepared with various enzyme digestion of Capsosiphon fulvescens were used to measure the inhibitory effects against angiotensin I converting enzyme (ACE). The commercially available enzymes such as Celluclast, Viscozyme, Lysing enzyme, Flavourzyme, Alcalase and Pectinex were used to digest C. fulvescens and produce hydrolysates. The maximum ACE inhibitory activity was observed using Alcalase hydrolysis (72.9%). The optimal conditions of Alcalase extraction were pH 8.0 and extraction time for 12 hr. The hydrolysates were fractionated using preparative-LC and anion-exchange chromatography on DEAE-cellulose and the fraction B and B-2 were isolated. The ACE inhibitory activity of fraction B-2 by anion-exchange chromatography was 82.6%. The molecular weight of fraction B-2 estimated using size exclusion chromatography was about 1 kDa. The monosaccharide composition of the fraction B-2 was determined to be mannose (1.1%), glucuronic acid (1.3%), galactose (1.3%) and glucose (96.3%).

• Fisheries and Aquatic Sciences
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• v.5 no.1
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• pp.21-27
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• 2002

Angiotensin I converting enzyme inhibitory activities of shelled krill (Euphausia superba) hydrolysates by autolysis and by hydrolysis with commercial proteases were analyzed. Among the proteases, Alcalase was the most effective protease for the hydrolysis of krill considering the degree of hydrolysis $(87.5\%)$ and the ACE inhibitory activity $(60\%)$. Four hour hydrolysis suggested as the most suitable and economic. In order to establish the optimum hydrolysis condition of krill, degree of hydrolysis and ACE inhibitory activity as affected by Alcalase concentration and water amount added were statistically analyzed by response surface methodology (RSM). The optimum hydrolysis condition was $2.0\%$ Alcalase hydrolysis in 2 volumes (v/w) of water at $55\% for 4 hr. The hydrolysate prepared from the optimum hydrolysis condition was fractionated by molecular weight. The lower molecular weight fraction showed the higher ACE inhibitory activity. $IC_{50}$ of the fraction under 500 Da was 0.57mg protein/mL.

• Natural Product Sciences
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• v.17 no.4
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• pp.363-366
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• 2011

Guibi-tang is a traditional medicine used for the treatment of colds. We investigated the levels of several compounds in Guibi-tang before and after fermentation with Lactobacillus and tested their ability to inhibit angiotensin-converting enzyme. Six known compounds (decursin, decursinol angelate, nodakenin, liquiritin, formononetin, and 6-gingerol) and 2 unidentified compounds were detected in Guibi-tang (GB) and fermented Guibi-tang (FGB) by an established HPLC-DAD method. The levels of the 6 known compounds were decreased after fermentation. FGB showed more potent inhibition of angiotensin-converting enzyme activity than GB. In conclusion, fermentation with Lactobacillus affects the content of several compounds in GB and improves its angiotensin-converting enzyme inhibitory activity.

• 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.

• 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 $21.8\;{\mu}g/ml$.

• KSBB Journal
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• v.14 no.5
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• pp.600-605
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• 1999

For the production of angiotensin I converting enzyme inhibitory peptides as a material for antihypertensive functional foods from animal blood produced in slaughterhouse, the optimum condition for enzymatic hydrolysis to yield a peptide fraction of the highest activity were investigated with a respect of industrial production. Among several industrially-usable enzymes tested, $Alcalase^？$ produced hydrolysates of the highest activity from total plasma and purified albumin. $IC_50$ values of albumin hydrolysate and its third fraction separated by gel chromatography were 0.5 and 0.02 mg/mL, respectively. The fraction was found to be obtained by a simple ultrafiltration using a membrane of MW cutoff 1,000. The possibility for the industrial production of antihypertensive peptides from animal blood plasma protein was suggested.

• 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.

• The Korean Journal of Food And Nutrition
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• v.31 no.6
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• pp.926-932
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• 2018

This research was conducted to investigate the changes in quality characteristics of cheonggukjang fermented with the addition of hazelnut (10, 20, 30 and 40%) including; water content, pH, hydrophilic and lipophilic substances, color, viscosity and angiotensin converting enzyme inhibition activity. There was no significant change in pH with the addition of hazelnut. The water content significantly decreased with the addition of hazelnut. Hazelnut was also found to brighten the color of cheonggukjang. L-value and b-value increased with the addition of cheonggjuang. There was an insignificant change in the a-value. There was a slight decrease in the content of hydrophilic with addition of hazelnuts. Where there was more than 20% addition of hazelnut to soybean, the viscous substance content in cheonggukjang decreased significantly. Angiotensin converting enzyme inhibitory activity increased proportionally to the amount of hazelnut added. It was identified that the addition of 40% of hazelnut made its angiotensin converting enzyme inhibitory activity 10% point higher than that of control. These results suggests that the addition of hazelnut makes it possible to produce cheongkukjang of excellent angiotensin converting enzyme inhibitory activity.

• ALGAE
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• v.21 no.3
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• pp.343-348
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• 2006

This study was conducted to screen in vitro angiotensin - I converting enzyme (ACE) inhibitory activities of methanol (MeOH) and aqueous extracts at 20°C and 70°C, respectively, prepared from twenty-six red algae obtained from the coast of Jeju Island in Korea. Among aqueous extracts at 20°C (20AE) from red algae Lomentaria catenata showed the strongest ACE inhibitory activity and Lithophyllum okamurae recorded the second highest activity. From MeOH extract at 20°C (20ME) Ahnfeltiopsis flabelliformis possessed the strongest ACE inhibitory activity. Remarkable activities from MeOH extracts at 70°C (70ME) were observed in Grateloupia filicina, Sinkoraena lancifolia and Grateloupia lanceolata. However, no significant activity was found in aqueous extracts at 70°C (70AE). The IC50 values, which are concentrations required to inhibit 50% activity of ACE, for ACE inhibitory activities of 20AE from Lithophyllum okamurae and L. catenata were 13.78 and 12.21 μg mL–1, respectively. The IC50 values of 20ME from A. flabelliformis and Laurencia okamurae were 13.84 and 106.15 μg mL–1. Those of the 70ME from Bonnemaisonia hamifera, Grateloupia filicina, Sinkoraena lancifolia, G. lanceolata, Gracilaria vermiculophylla and L. okamurae ranged from 25.82 to 124.69 μg mL–1.

• Journal of Animal Science and Technology
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• v.49 no.1
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• pp.129-136
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• 2007

This study was performed to determine the protein profiles using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Angiotensin-I-converting enzyme(ACE) inhibitory activity (IC50) as affected by the various meat cuts, digestion times with pepsin. Hydrolysates having the protein concentration of 10 ug/mL had approximately 36∼39% ACE inhibitory activities, regardless of meat cut and digestion time. Protein concentration and ACE inhibitory activity of the diluted hydrolysate increased after 1-hr digestion. In original hydrolysates, ACE inhibitory activities of loin had higher than those of round (P<0.05). In addition, non-heated hydrolysates had higher ACE inhibitory activities than heated counterparts. When myosin B was digested by pepsin more than 1 hr, improved ACE inhibitory activities were observed as compared to the non-digested control.