• The Korean Journal of Food And Nutrition
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• v.32 no.5
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• pp.511-521
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• 2019

The purpose of this study was to investigate the inhibitory effect of enzyme activity and anti-proliferation of human cancer cell lines (HCT 116, NCI-H460 and MCF-7) of peanut skin depending on cultivars (Arachis hypogaea L. cv. K-Ol, cv. Sinpalkwang, cv. Daan, cv. Heuksaeng) and extraction solvent. Peanut skin was extracted with 80% ethanol, 80% methanol, 80% acetone, and distilled water, followed by analysis of the enzyme inhibitory activity and anticancer activity. Methanol extract of Daan cultivar most effectively inhibited ${\alpha}$-gluosidase (65.08%, 0.025 mg/mL), tyrosinase (82.49%, 2 mg/mL) and ACE (73.61%, 10 mg/mL). The inhibitory effect of peanut skin extracts on colon cancer cell (HCT-116), lung cancer cell (NCI-H460) and breast cancer cell (MCF-7) growth were investigate using MTT assay. The highest anti-proliferation of cancer cell line of peanut skin extracts was observed in the methanol extract of Daan cultivar. The cell viability on HCT 116, NCI-H460 and MCF-7 cell lines of methanol extracts from peanut skin of Daan cultivar was 48.13%, 41.03%, and 36.02% at $200{\mu}g/mL$, respectively. These results suggest that peanut skin extracts may mediate physiological activity, and provide valuable information for the use of peanut byproduct as a functional food material.

• Korean Journal of Medicinal Crop Science
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• v.11 no.3
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• pp.236-245
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• 2003

The study was performed for elucidating angiotensin converting enzyme (ACE) inhibitory activity and comparing antioxidative activity of Panax ginseng extracts prepared at different conditions. Total phenolic content, inhibitory activity on ACE and antioxidative effects were tested on 10 ethanolic extracts and correlation coefficient between total phenolic content and physiological activity was calculated. Yield and total phenolic content of 50% ethanolic extract prepared at $85^{\circ}C$ exhibited the highest value as 42.52% and 0.82%, respectively. Among the fractions obtained from 50% ethanolic extract prepared at room temperature, water fraction showed the highest value in yield as 72.08% and ethyl acetate fraction did in total phenolic content as 6.59%. In the test on ACE inhibitory activity, 50% ethanolic extract obtained at room temperature indicated the strongest effect of 93.8% which was higher than 85.2% of commercialized ACE inhibitor and solvent fractions showed potent inhibitory activity in order of hexane fraction, diethyl ether fraction, ethyl acetate fraction, butanol fraction and water fraction at concentration of $4000{\mu}g/ml$. 50% Ethanolic extract prepared at $85^{\circ}C$ had the most potent inhibition effect on human LDL oxidation as 78.2% at $200{\mu}g/ml$ and the other extracts also did above 60%. Diethyl ether fraction and ethyl acetate fraction showed strong inhibition activity $(34.38%{\sim}78.13%)$ on LDL oxidation at concentration of $10{\sim}200\;{\mu}g/ml$. From the statistical analysis via SAS program, correlation coefficient between total phenolic content and ACE inhibitory effect was 0.6353 at P<0.05. Conclusively, this report showed that the most efficient extraction condition for elevating inhibitory activity on ACE and LDL oxidation, phenolic content and yield from Panax ginseng was 50% ethanol extraction at room temperature or high temperature condition. And Panax ginseng would be used for preventing hypertension or atheroscrelosis for man via inhibitory action on ACE and LDL oxidation.

• Archives of Pharmacal Research
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• v.19 no.6
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• pp.480-485
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• 1996

Brain GABA transaminase is inactivated by preincubation with antidepressant/antipanic drug pheneizine (${\beta}$ethylphenylhydrazine) (mixing molar ratio 10:1) at pH 7.4. The reaction of enzyme with phenelzine was monitored by absorption and fluorescence spectroscopic methods. The inactive enzyme was fully reconstituted by addition of cofactor pyridoxal-5-phosphate. This result implies that the blocking of 1 mol of pyridoxal-5-phosphate per enzyme dimer is needed for inactivation of the enzyme. The time course of the reaction is significantly affected by the substrate .alpha.-ketoglutarate, which afforded complete protection against the loss of catalytic activity. The kinetic studies shows that phenelzine reacts with the cofactor of enzyme with a second-order rate constant of $2.1{\times}10^3M^{-1}s^{-1}$. It is postulated that the antidepressant/antipanic drug phenelzine is able to elevate the neurotransmitter GABA levels in central nervous system by inhibitory action on GABA degradative enzyme GABA transaminase.

• Journal of Life Science
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• v.20 no.5
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• pp.768-774
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• 2010

In this study, we investigated the antioxidant activities, alcohol metabolizing activities, nitrite scavenging ability, angiotensin converting enzyme (ACE), and elastase inhibitory effects of hot water extract from Makgeoly (HWM). Antioxidant activities were measured by using 2,2.diphenyl.1.picryl.hydrazyl (DPPH) free radical scavenging activity and SOD (superoxide dismutase).like activity. The DPPH radical scavenging activity and SOD.like activity of HWM were remarkably increased in a dose.dependent manner and were 48.0% and 98.7% at 10 mg/ml, respectively. To determine the influence of HWM on alcohol metabolizing activity, the generating activities of reduced.nicotinamide adenine dinucleotide (NADH) by alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) were measured. The facilitating rates of ADH and ALDH activity by HWM were remarkably increased in a dose.dependent manner and were 70.2% and 64.1% at 10 mg/ml, respectively. The inhibitory activity against angiotensin converting enzyme (ACE) of HWM was increased in a dose.dependent manner and was 74.2% at 10 mg/ml. The nitrite scavenging ability of HWM showed the most remarkable effect at pH 1.2 and 2 mg/ml. These results indicated that HWM may have valuable biological properties owing to their antioxidant activities, ADH and ALDH activity, nitrite scavenging ability, and ACE inhibitory activity.

• Journal of the Korean Society of Food Science and Nutrition
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• v.29 no.4
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• pp.737-742
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• 2000

As functionality investigation of a soybean fermentation food, a angiotensin converting enzyme inhibitory peptide was separated during natto fermentation by Bacillus natto and inhibitory effect was investigated. After incubation at each 2$0^{\circ}C$, 3$0^{\circ}C$, 4$0^{\circ}C$, 5$0^{\circ}C$, 6$0^{\circ}C$ for the 0~72 hr, protein content, protease activity and angiotensin converting enzyme inhibition were determined. The protein content and protease activity were increased and reached maximum at 60 hr fermentation with 4$0^{\circ}C$ and decreased after the 60 hr fermentation during natto fermentation. The optimum condition for angiotensin converting enzyme inhibitors was appeared at fermentation for 60 hr at 4$0^{\circ}C$. Crude extract of natto was partially purified by Amicon membrane YM-3 and Sephadex G-10, G-25 gel filtration, stepwise. The inhibitory rate was increased in a concentration dependent manner, espcially the most potent activity about 74.74% at 1.0 mg peptide content. The most prominent amino acid of the peptide from natto was alanine, followed by phenylalnine, histidine.

• The Korean Journal of Physiology
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• v.10 no.2
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• pp.1-10
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• 1976

The action of acetylcholine on the sodium plus potassium activated ATPase activity in the rabbit red cell membrane has been investigated and the experiments were also designed to determine the mechanism of action of acetylcholine on the ATPase activity. The following results were observed. 1. The activity of the NaK ATPase from red cell membrane is inhibited by acetylcholine. 2. The ratio of inhibition of NaK ATPase by acetylcholine is decreased by raising the potassium concentration, and is increased by raising the sodium concentration. 3. The ATPase activity is increased by small amounts of calcium but inhibited by larger amounts. The ratio of inhibition of the enzyme by acetylcholine is increased by raising the calcium concentration. 4. The inhibitory action of acetylcholine on the NaK ATPase activity was not related to the sulfhydryl group of cysteine, the hydroxyl group of threonine, or the carboxyl group of aspartic acid. 5. The inhibitory action of acetylcholine on the ATPase activity is due to amino group of the enzyme of NaK ATPase.

• The Journal of Natural Sciences
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• v.13 no.1
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• pp.65-71
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• 2003

Angiotensive I-converting enzyme inhibitory activity of various extracts from some rice brans were investigated with its optimal extraction conditions. Water extracts of Ilpumbyeo rice bran showed the highest ACE inhibitory activities of 7730%. ACE inhibitor from Ilpumbyeo rice bran was maximally extracted when its powder was treated with 10 times of distilled water for 12h at $30^{\circ}C$.

• KSBB Journal
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• v.6 no.1
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• pp.55-61
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• 1991

The objective of this in vitro study is to screen a possible inhibitor, originated from some chinese herb medicines, of 3-hydroxy-3-methylglutaryl Coenzyme A (HMG-CoA) reductase that is the major regulatory enzyme of hepatic cholesterol biosynthesis. Fourteen kinds of herbal plant were extracted with water and evaporated for prescreening. The methanol extracts of the effective 3 kinds (9 species) were fractionated with chloroform, ethylacetate, butanol and water, and vacuum evaporated. The degree of inhibition of the extracts to HMG-CoA reductase activity was calculated by the spectrophotometric method using microsomal protein of Saccharomyces cerevisiae ATCC 42949 as an enzyme source. Among these samples, marked inhibitory effects were observed in the extracts of ethylacetate and chloroform fractions of the Rosa rugosa roots, and those of butanol, ehtylacetate and water fractions of pine leaves. Also, the inhibitory effects of the extracts obtained from buckwheat shell and the roots of Rosaceae were found.

• Preventive Nutrition and Food Science
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• v.9 no.1
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• pp.95-97
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• 2004

An angiotensin converting enzyme (ACE) inhibitory substance was isolated and purified from Lycium chinense Miller. A crude water extract of Lycium chinense Miller was prepared by adding it to water shaking at $25^{\circ}C$ for 1 hr, followed by centrifugation at 8000 ${\times}$ g for 30 min. The crude extract was then filtered using YM-3 and YM-1 membranes. An ACE inhibitor was isolated using consecutive chromatographic methods including: ion exchange chromatography, gel permeation chromatography, and FPLC. The inhibitor was identified to have a molecular mass of 862 daltons by mass spectrometry.

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2002.10a
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• pp.90-91
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• 2002

The angiotensin converting enzyme (ACE) generates the powerful vasoconstrictor angiotensin II by removing the C-terminal dipeptide from the precursor decapeptide angiotensin I (1). The enzyme also inactivates the vasodilator bradykinin (2). There have been many studies on ACE inhibitory substances as functional in food, and ACE inhibitory peptides were isolated (3-5). (omitted)