• Applied Biological Chemistry
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• v.41 no.1
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• pp.110-117
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• 1998

Seven kinds of polyphenol compounds having ACE activities were isolated and purified by Sephadex LH-20, MCI-gel CHP-20, ${\um}-Bondapak\;C_{18}$ and Fuji-gel ODS $G_3$ sucessively from cacao bean(Ghana). The chemical structures of each compound were determined and identified using analyzers such as $^1H-NMR$, $^{13}C-NMR$, IR, MS, polarimeter and Elemental Analysis. Inhibition effects of isolated polyphenols on angiotensin converting enzyme (concerned with hypertension) were also observed. The results obtained were as follows,; The compounds isolated and identified were confirmed and determined as compound 1 [(+)-catechin], compound 2 [(-)-epicatechin], compound 3 [procyanidin B-1 : (-)-epicatechin-$(4{\beta}{\rightarrow}8)$-(+)catechin], compound 4 [procyanidin B-2 : (-)-epicatechin-$(4{\beta}{\rightarrow}8)$-(-)-epicatechin], compound 5 [procyanidin B-7 : (-)-epicatechin-$(4{\beta}{\rightarrow}6)$-(+)-catechin], campound 6 (procyanidin B-2,3,3'-O -digallate), compound 7 [cinnamtannin A-2 : (-)-epicatechin-$(4{\beta}{\rightarrow}8)$-(-)-epicatechin-$(4{\beta}{\rightarrow}8)$-(-)-epicatechin-$(4{\beta}{\rightarrow}8)$-(-)-epicatechin]. In the inhibition effect on ACE, procyanidin B-2,3,3'-O-digallate (compound 6) showed a higher value of 94.6% for ACE in $100\;{\um}M$ than other compounds such as (+)-catechin (compound 1), (-)-epicatechin (compound 2), procyanidin B-1 (compound 3), procyanidin B-2 (compound 4), procyanidin B-7 (compound 5) and cinnamtannin A-2 (compound 7) showing 67.9%, 61.9%, 88.6%, 82.5%, 72.2% and 82.3% for ACE, respectively. Inhibition of $4{\beta}{\rightarrow}8$ in coupling bond on the ACE enzyme was more effective than that of $4{\beta}{\rightarrow}6$. Procyanidin containing gallate inhibited more effectively than those containing not any. It was also observed that a lot of hydroxy group in the compounds increased the inhibitory effect.

• Korean Journal of Clinical Laboratory Science
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• v.52 no.4
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• pp.398-407
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• 2020

The inhibitory effect on α-glucosidase, a marker of postprandial hyperglycemia, and angiotensinconverting enzyme (ACE), a marker of hypertension, was analyzed using non-fermented green tea and three different types of fermented tea, which are popular beverages in modern life. Green tea was mixed with trace amounts of vanadate (50 ㎍/mL), which has insulin-mimetic effects, to investigate the synergistic effect of vanadate on the inhibition of α-glucosidase. The concentration of epigallocatechin gallate (EGCG) and caffeine was also checked. The extracts of green tea and fermented teas showed clear inhibition on α-glucosidase, which caused a decrease in the postprandial glucose levels. The inhibitory effect was most prominent in the 20% fermented tea. Trace amounts of vanadate (50 ㎍/mL)-mixed green tea extract had twice the inhibitory effect on α-glucosidase than the pure tea extract. All teas showed inhibitory effects on ACE. Among those, the effect was most prominent in green tea, which had higher concentrations of EGCG. In contrast, the postprandial glucose-lowering effect and ACE inhibition of the fermented teas, which have a lower level of EGCG, was attributed to some other different functional substances.

• Applied Biological Chemistry
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• v.44 no.3
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• pp.137-142
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• 2001

In order to prove physiological function of biopolymer from Bacillus coagulans CE-74, in vitro experiments simulating the passive membrane transport of gastrointestinal tract were carried out using dialysis membrane. And inhibition effect of isolated biopolymer on tyrosinase and angiotensin converting enzyme (ACE) were observed. The glucose retardation index after 30 min dialysis was 43.5% in the presence of 2% biopolymer. As the dialysis period became longer, the retarding effect toward glucose absorption decreased and the effect was close to zero after 5 hr dialysis. The bile acid retardation index after 30 min dialysis was 34% and 44.2% in the presence of 1% and 2% biopolymer, respectively. The effect decreased as the dialysis time elapsed. It was measured by arosinase inhibition activity of biopolymer that inhibition effect was 48.5% in $20\;{\mu}g/{\mu}l$. In a ACE inhibition activity, biopolymer showed inhibition activity as 97% in $10\;{\mu}g/{\mu}l$.

• The Korean Journal of Mycology
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• v.39 no.2
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• pp.111-116
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• 2011

This study was carried out to examine Electron donating ability (EDA), nitrite scavenging, tyrosinase inhibition, ACE inhibition activity and fibrinolytic activity of culture extracts from Phellinus linteus which was grown added rice bran, pine needles and turmeric in brown rice. Electron donating ability of Phellinus linteus extract (PLE) was lower in the water extract than the ethanol extract. Nitrite scavenging activity was the highest in PLE from ethanol extract than water extract. Especially, when the pine needles was addition treatment, the nitrite scavenging activity was about 70% at pH 1.2 by ethanol extract. Tyrosinase inhibition activity of PLE was highest in the water extract than ethanol extract, and inhibition rate was the most higher in the extract by hot water added pine needles. ACE inhibition activity were very low effective at water and ethanol extract. Fibrinolytic activities were similarly strong in rice bran, pine needles and turmeric powder. Especially, when rice bran was added, showed the activity was increased about 5% than plasmin. Therefore, It may be used for the food industry as natural source of bioactive compound after further investigation, such as in vivo experiment.

• The Korean Journal of Mycology
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• v.39 no.2
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• pp.105-110
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• 2011

This study was carried out to examine the electron donating ability (EDA), nitrite scavenging, tyrosinase inhibition, ACE inhibition and fibrinolytic activity of culture extracts from Fomitella fraxinea which was grown added rice bran, pine needles and turmeric in brown rice. Electron donating ability was higher in the extract by hot water than ethanol. Nitrite scavenging activity was the highest from ethanol extract of culture products added to the pine needles, showed the scavenging activity was approximately 50%. Tyrosinase inhibition activity was highest in the extract by hot water, showed inhibition rate of rice bran was 72.49%, pine needles 87.34% and turmeric powder 82.75%, respectively. ACE inhibition activity were very low effective at all water and ethanol extracts. Fibrinolytic activities were similarly strong in the rice bran, pine needles and turmeric powder. Especially, when the rice bran and turmeric powder were added, showed the activities were increased about 10% than plasmin. Therefore, it may be used for the food and cosmetic industry as natural source of bioactive compound after further investigation such as in vivo experiment.

• 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.

• The Journal of Korean Medicine
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• v.22 no.2
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• pp.3-9
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• 2001

Objective : Oriental medicinal plants reported to be used as anti-hypertensive drugs have been in vitro screened for inhibitory effects on angiotensin-converting enzyme (ACE). Methods : The bioassay is based on inhibition of plasma angiotensin-converting enzyme, as measured from the enzymatic cleavage of the Hip-His-Leu substrate into His-Leu. The plant material is extracted with hexane, ethylacetate, n-buthanol and water separately. Results : In total, 51 species (202 extracts) have been investigated and $400{\;}\mu\textrm{g}/ml$ of the solvent extracts from 26 extracts inhibit the enzyme activities by more than 50%. Among them, four samples of two plant species (buthanol and ethylacetate extracts of Salvia miltiorrhiza and buthanol and water extracts of Jeffersonia dubia) were found to posses a high ACE inhibition ability more than 90%. Conclusion : These results suggested that many Oriental medicinal plants have a antihypertensive effects by inhibition of ACE.

• Journal of Microbiology and Biotechnology
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• v.12 no.1
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• pp.59-64
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• 2002

An angiotensin I-converting enzyme (EC 3.4.15.1) (ACE), which can convert inactive angiotensin I into angiotensin II, a vasoconstrictor, is one of the key enzymes in controlling hypertension. It is suggested that the inhibition of ACE prevents hypertension, and many inhibitory peptides have already been reported. In the current study, oligonucleotides encoding ACE inhibitory peptides (IY, VKY) were chemically synthesized and designed to be multimerised due to isoschizomer sites (BamHI, BglII). The cloned gene named AP3 was multimerised up to 6 times in pBluescript and expressed in BL2l containing pGEX-KG. The fusion protein (GST-AP3) was easily purified with a high recovery by an affinity resin, yielding 38 mg of synthetic AP3 from a 1-1 culture. The digestion of AP3 by chymotrypsin exhibited an $IC_50$ value of $18.53{\mu}M$. In conclusion, the present experiment indicated that AP3 could be used as a dietary antihypertensive drug, since the potent ACE inhibitory activity of AP3 could be activated by chymotrypsin in human intestine.

• Preventive Nutrition and Food Science
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• v.10 no.2
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• pp.134-139
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• 2005

Seven brown algal species (Ecklonia cava, Ishige okamurae, Sargassum fulvellum, Sargassum horneri, Sargassum coreanum, Sargassum thunbergii and Scytosiphon lomentaria) were hydrolyzed using five proteases (Protamex, Kojizyme, Neutrase, Flavourzyme and Alcalase) and screened for angiotensin 1-converting enzyme (ACE) inhibitory activities. Most algal species examined showed good ACE inhibitory activities after the enzymatic hydrolysis. However, E. cava was the most potent ACE inhibitor of the seven species. Flavourzyme digest of E. cava exhibited an $IC_{50}$ of around $0.3\;{\mu}g/mL$ for ACE; captopril has an $IC_{50}$ of $\~0.05\;{\mu}g/mL$. The Flavourzyme digest was separated to three fractions by an ultrafiltration membrane (5, 10, 30 kDa MWCO) system according to the molecular weights. The active components were mainly concentrated in >30 kD fraction which are composed of the highest protein content $(27\%)$ and phenolic content (261 mg/100 mL) compared to the other two smaller molecular weight fractions. Therefore, the active compounds appear to be relatively high molecular weight complex molecules associated with protein (glycoprotein) and polyphenols. Therefore, E. cave is a potential source of antihypertensive compound.

• Food Science and Biotechnology
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• v.17 no.4
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• pp.873-877
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• 2008

Native soy protein isolate (SPI) was hydrolyzed with 4 different proteolytic enzymes, including bromelain, papain, Neutrase, and Flavourzyme. SPI hydrolysates with the degree of hydrolysis (DH) in range of 6 to 15% were prepared by each enzyme. The angiotensin 1 converting enzyme (ACE) inhibitory and the antioxidant activities of the SPI hydrolysates, such as superoxide dismutase-like activity and inhibition of the linoleic acid autoxidation, were evaluated. Overall, as the DH increased, all evaluated bioactivities of the SPI hydrolysates significantly increased. The significantly highest ACE inhibitory and antioxidant activities were found in hydrolysates made with papain and bromelain, respectively. SPI hydrolysates by Flavourzyme showed the significantly lowest activity in all tested bioactivities. The results suggested that ACE inhibitory and antioxidant activities of SPI hydrolysates were determined by the DH and by the enzyme used.