• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 1998.05a
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• pp.164-164
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• 1998

• 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)

• Proceedings of the Ginseng society Conference
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• 1990.06a
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• pp.15-19
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• 1990

We have been isolating various physiologically active substances from non-saponin fraction of Korean Red Ginseng These are adenosine, gyro-glutamic acid, dencichine and acidic polysaccharide. Adenosine and gyro-glutamic acid are loom to inhibit epinephrine-induced lipolysis in fat cells and stimulate the insulin-mediated lipogenesis. In addition to these actions, adenosine was found to inhibit both norepinephrine- and histamine-induced aorta constriction, and pyre·glutamic acid inhibits angiotensin-converting enzyme. Dencichine stimulated histamine-induced aorta constriction. Finally, acidic polysaccharide was found to inhibit both lipolytic and anorexigenic actions of Toxohormone-L. Based on these experimental results, I presented a brief review on these compounds isolated from non- saponin fraction of Korea Red Ginseng. Keywords Panax ginseng, Korean red ginseng, adenosine, pyroglutamic acid, dencichine, acidic polysac- charide, lipolysis, lipogenesis, angiotensin-converting enzyme, toxohormone-L.

• Asian-Australasian Journal of Animal Sciences
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• v.21 no.5
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• pp.732-737
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• 2008

This study developed a natural ingredient as a functional food possessing properties of attenuation of hypertension and cardiovascular hypertrophy. In a previous study hydrolysates obtained from chicken leg bone protein using Alcalase strongly inhibited angiotensin I converting enzyme (ACE) in vitro. In particular, hydrolysate (A4H) from four hours of incubation exhibited the highest ACE inhibitory activity (IC50 = 0.545 mg/ml). A4H was selected as a potent ACE inhibitor and orally administrated to spontaneously hypertensive rats (SHR) for eight weeks to investigate attenuating effects on age-related development of hypertension and cardiovascular hypertrophy. Results showed that treatment with A4H of SHRs attenuated the development of hypertension as effectively as the clinical antihypertensive drug captopril. Moreover, a significantly lower heart to body weight ratio and thinness of coronary arterial wall was observed in SHRs that had been treated with A4H or captopril. The results suggest that A4H can be utilized in developing an ACE inhibitor as a potential ingredient of functional foods to alleviate hypertension and cardiovascular hypertrophy.

• Mycobiology
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• v.38 no.3
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• pp.206-209
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• 2010

To produce bioactive compound enriched yeast using medicinal Gugiga (Lycium chinensis Mill), several edible Saccharomyces species were cultured in Gugija extracts added yeast extract, peptone and dextrose medium (GE - YEPD medium) at $30^{\circ}C$ for 24 hr, and their growth were determined. Growth of Saccharomyces cerevisiae K-7 and Sacchromyces cerevisiae ACTC 7904 were better than those of the other yeasts. Two yeasts were selected and then determined their some physiological functionalities after cultivated the yeasts in the GE - YEPD medium and compared those grown on YEPD medium. Antihypertensive angiotensin I-converting enzyme (ACE) inhibitory activity of S. cerevisiae K-7 grown on GE - YEPD medium was about 20% higher than that grown on YEPD medium. Superoxide dismutase-like activity of S. cerevisiae ACTC 7904 was also about 12% more high. However, the other physiological functionalities were almost same or lower. Optimal addition concentration of Gugija extract was 10%, and maximally growth and ACE inhibitory activity of S. cerevisiae K-7 were shown when the strain was cultured in 10% Gugija extracts containing YEPD medium at $30^{\circ}C$ for 12 hr.

• Preventive Nutrition and Food Science
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• v.20 no.1
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• pp.67-72
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• 2015

Squid is one of the most important commercial fishes in the world and is mainly utilized or consumed as sliced raw fish or as processed products. The biofunctional activities of enzymatic squid meat hydrolysate were determined to develop value-added products. Enzymatic squid hydrolysate manufactured by Alcalase effectively quenched 1,1-diphenyl-2-picrylhydrazyl radical, hydroxyl radical, and hydrogen peroxide radical with $IC_{50}$ values of 311, 3,410, and $111.5{\mu}g/mL$, respectively. Angiotensin I-converting enzyme inhibitory activity of squid hydrolysate was strong with an $IC_{50}$ value of $145.1{\mu}g/mL$, while tyrosinase inhibitory activity with an $IC_{50}$ value of 4.72 mg/mL was moderately low. Overall, squid meat hydrolysate can be used in food or cosmetic industries as a bioactive ingredient and possibly be used in the manufacture of seasoning, bread, noodle, or cosmetics.

• Food Science and Biotechnology
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• v.14 no.6
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• pp.772-777
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• 2005

The goal of this study was to screen and characterize the physiological functions of Korean traditional wines (TW) and liquors (TL). Forty-two TW and TL were collected and evaluated for quality and cardiovascular activities. Ethanol content ranged from $9.0%{\sim}41%$, and pH ranged from $3.0{\sim}7.8$, and they also contained 0.01% to 0.67% of total acid. Samples contained a maximum of 2.0% of crude protein and $0.1%{\sim}14.0%$ of reducing sugar. Commercial CM-wine showed the highest antihypertensive angiotensin I-converting enzyme (ACE) inhibitory activity, 85.9%. The greatest fibrinolytic activity and platelet aggregation inhibitory activity were also found in commercial CM-wine (31.8U) and commercial SS2-wine (38.6 %), respectively. Commercial SHBI-liquor showed the highest HMG-CoA reductase inhibitory activity, 78%. The ACE inhibitor from commercial CM-wine was a peptide compound and also showed an antihypertensive effect in spontaneous hypertensive rats at a dosage of 1.5 mg/kg.

• Journal of Microbiology and Biotechnology
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• v.25 no.8
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• pp.1315-1320
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• 2015

To enhance the γ-aminobutyric acid (GABA) content, the optimized fermentation of soybean with added sea tangle extract was evaluated at 30℃ and pH 5.0. The medium was first inoculated with Aspergillus oryzae strain FMB S46471 and fermented for 3 days, followed by the subsequent inoculation with Lactobacillus brevis GABA 100. After fermentation for 7 days, the fermented soybean showed approximately 1.9 g/kg GABA and exhibited higher ACE inhibitory activity than the traditional soybean product. Furthermore, several peptides in the fraction containing the highest ACE inhibitory activity were identified. The novel fermented soybean enriched with GABA and ACE inhibitory components has great pharmaceutical and functional food values.

• Journal of the Korean Society of Food Science and Nutrition
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• v.25 no.5
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• pp.871-877
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• 1996

Hot-water extract and enzymatic hydrolysate prepared from fresh water fish such as carp, snakehead, eel and israeli cart were tested for inhibitory activity against Angiotensin I converting enzyme(ACE). ACE inhibitory activity of enzymatic hydrolysate was higher than that of hot-water extract, and was the highest in enzymatic hydrolysate of carp among the tested samples. ACE inhibitory activity of 70% ethanol soluble fraction was higher than that of precipitated fraction, the highest in enzymatic hydrolysate of carp. Molecular weight of active fraction was about 1,400 in hot-water extract and slightly above in enzymatic hydrolysate. Amino acid of active fraction of hot-water extract was abundant in glycine, alanine, leucine and proline, whereas amino acids of aspartic acid, glutamic acid, glycine, alanine, valine, leucine and proline were abundant in enzymatic hydrolysate. $IC_{50}$/(amounts of inhibitors need for 50% inhibition) of hot-water extract was the range of 50.3~56.9$\mu\textrm{g}$, those of enzymatic hydrolysate 42.6~57.7$\mu\textrm{g}$.

• 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.