• Korean Journal of Fisheries and Aquatic Sciences
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• v.25 no.3
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• pp.229-235
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• 1992

Fish protein hydrolysates(FPH) prepared from defatted mackerel meal by proteases such as complex enzymes, bromelain, alcalase, $\alpha-chymotrypsin,$ trypsin, papain and pepsin were tested for inhibitory activity against angiotensin-I converting enzyme(ACE). Among proteases tested, the hydrolysates obtained from the treatment of complex enzymes or bromelain showed relatively higher activity. ACE inhibitory activity of the hydrolysates increased until hydrolysis of 8 hrs, and was stable by heat treatment for 20min at $100^{\circ}C.$ From the profiles of fractionation of the hydrolysates with Bio-gel P-2, the most active fraction had about MW 1,450 and it's amino acid was abundant in Asp, Glu, Lys, Leu, Val and Ala. $IC_{50}\;(amounts\;of\;inhibitors\;needed\;for\;50\%\;inhibition)$ of the active fraction of the hydrolysates obtained from the treatment of complex enzyme and bromelain was 90 and $130 {\mu}g,$ respectively.

• Journal of Animal Science and Technology
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• v.47 no.1
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• pp.83-90
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• 2005

ACE-inhibitory peptides derived from goat's whey hydrolyzed by various proteolytic enzymes were separated and purified for antihypertension materials. The highest ACE-inhibitory activity of goat's whey hydrolysates was 85.5 % by pepsin for 72 hrs. Also the highest ACE-inhibitory activity of goat's whey hydrolysates was F-4 by pepsin for 72 hrs by Sephadex G-25 gel chromatograms. F-4e and F-4ed from F-4 by RP-HPLC to first and second purification were the highest in ACE-inhibitory activity, respectively. The most abundant amino acid was leucine(I 8.54 %) in F-4ed of ACE-inhibitory peptides after second purification. Amino acid sequence of F-4ed of ACE-inhibitory peptides showed Leu-Lys-Asp-Tyr-Gly-GlyVal- Ser-Leu and Leu-Gly-Asp-Gly-Ala-Gly- Asp-Val-Ala-Phe. $IC_{50}$ calibrated in peptic hydrolysates(72 hrs), F-4, F-4e and F-4ed from goat's whey hydrolysates by pepsin for 72 hrs were 33.93, 28.75, 11.74 and 1.09 mg/ml, respectively. From the results of this experiment, goat's whey hydrolysate by pepsin was shown to have ACE-inhibitory activity.

• Journal of the Korean Society of Food Science and Nutrition
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• v.30 no.4
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• pp.721-725
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• 2001

Physiological activity in different parts of Dolsan leaf mustard (DLM) was investigated. To determine the physiological activity, DLM was crushed filtered centrifuged and then the supernatant was used as a sample. of 1%, 3% and 6%. By adding of improved root juice(20th day) with the concentration of 6% the cytotoxicity against HepG2 was the highest about 78.2%. And antioxidative effects in different parts of DLM was measured by using the DPPH method. Antioxidative effects was higher in all leaves than other parts. In particular antioxidative effects was the highest in leaves of traditional DLM at the 20th day of growth about 80.4%. In leaves of improved DLM at the 60th growth angiotensin-I converting enzyme inhibitory effect was the highest about 94.0%. Consequently there was not significant difference of physiological activity between improved and traditional DLM. However the cytotoxicity against HepG2 was the highest in roots of DLM. And the antioxidative and the ACE inhibitory effect in leaves of DLM were higher than those of other parts.

• Korean journal of food and cookery science
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• v.30 no.5
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• pp.613-619
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• 2014

For the development of a hangover soup containing blue mussel, 11 kinds of hot water extracts were prepared - A (mistletoe); B (shepherd's purse); C (arrowroot); D (bean sprout); E (oriental raisin); F (blue mussel); G (blue mussel and mistletoe); H (blue mussel and shepherd's purse); I (blue mussel and arrowroot); J (blue mussel and bean sprout); and K (blue mussel and oriental raisin). Extract C showed the highest effect for increasing the activities of alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase (ALDH); however, the addition of blue mussel did not provide a synergy effect on extract C. Other than the arrowroot-containing extracts (C and I), extract H showed relatively higher ADH ($237.4{\pm}1.7%$) and ALDH ($136.5{\pm}2.1%$) activities. Moreover, extract H showed the highest DPPH radical scavenging activity ($93.9{\pm}0.1%$) and angiotensin I converting enzyme (ACE) inhibitory activity ($42.7{\pm}1.6%$). The combination of blue mussel with shepherd's purse had a synergic effect on its ADH and ACE inhibitory activities.

• Asian-Australasian Journal of Animal Sciences
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• v.18 no.5
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• pp.741-746
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• 2005

To investigate the basic information and the possibility of ACE-inhibitory peptides for antihypertension materials, goat's caisin (CN) was hydrolyzed by various proteolytic enzymes and ACE-inhibitory peptides were separated and purified. ACE-inhibition ratios of enzymatic hydrolysates of goat's CN and various characteristics of ACE-inhibitory peptides were determined. ACE-inhibition ratios of goat's CN hydrolysates were shown the highest with 87.84% by pepsin for 48 h. By Sephadex G-25 gel chromatograms, Fraction 3 from goat's CN hydrolysates by pepsin for 48 h was confirmed the highest ACE-inhibition activity. Fraction 3 g and Fraction 3 gh from peptic hydrolysates by RP-HPLC to first and second purification were the highest in ACE-inhibition activity, respectively. The most abundant amino acid was leucine (18.83%) in Fraction 3 gh of ACE-inhibitory peptides after second purification. Amino acid sequence analysis of Fraction 3 gh of ACE-inhibitory peptides was shown that the Ala-Tyr-Phe-Tyr, Pro-Tyr-Tyr and Tyr-Leu. IC$_{50}$ calibrated in peptic hydrolysates at 48 h, Fraction 3, Fraction 3 g and Fraction 3 gh from goat's CN hydrolysates by pepsin for 48 h were 29.89, 3.07, 1.85 and 0.87 g/ml, respectively. Based on the results of this experiment, goat's CN hydrolysates by pepsin were shown to have ACE-inhibitory activity.

• Journal of the Korean Society of Food Science and Nutrition
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• v.37 no.5
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• pp.535-541
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• 2008

Pine mushroom (Tricholoma matsutake Sing.) is an expensive and highly prized delicacy in Korean and Japanese cuisines with its unique flavor and functional properties. The biological activities of pine mushroom juice (soluble solid contents $4.3^{\circ}$Brix) were evaluated using different tests; DPPH radical scavenging assay for its antioxidant activity, fibrin plate method for fibrinolysis and angiotensin I converting enzyme (ACE) inhibitory activity for anti-hypertensive effect. Free radical scavenging activity of the pine mushroom juice was $48.3{\pm}2.2%$ at the concentration of 1.0 mg/mL. The fibrinolytic activity of pine mushroom was about 2 times greater than that of plasmin used as positive control and the activity increased dose-dependently. The pine mushroom juice inhibited ACE activities dose-dependently and $IC_{50}$ value of ACE activity was $1.03^{\circ}$Brix. These results suggest that pine mushroom is a healthy delicacy.

• Journal of Life Science
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• v.21 no.6
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• pp.811-818
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• 2011

Physiological activities of hot water (MHW) and 80% ethanol (MEH) extracts from Maesaengi (Capsosiphon fulvescens) were investigated in this study. For the evaluation of antioxidant activities for MHW and MEH, 2,2-diphenyl-1-pic-rylhydrazyl (DPPH) radical scavenging activity and superoxide dismutase (SOD)-like activity were measured. DPPH radical scavenging activity and SOD-like activity of MHW, and MEH were increased weekly in a dose-dependent manner, and were about 10.8, 13.8, 62.4, and 27.1% at 10 mg/ml, respectively. The angiotensin converting enzyme (ACE) inhibitory activities of MHW and MEH were about 5.9% and 49.7% at 1 mg/ml, respectively. The ${\alpha}$-glucosidase inhibitory effect of MHW and MEH were about 1.4% and 67.3% at 1 mg/ml, respectively. To determine the influence of MHW and MEH on alcohol metabolizing activity, the generating activities of reduced-nicotinamide adenine dinucleotide (NADH) by alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase (ALDH) were measured. Facilitating rates of ADH activity by MHW and MEH were increased weekly in a dose-dependent manner and ALDH activities were not detected. Elastase inhibitory activities of MHW and MEH were 75.9% and 51.2% at 10 mg/ml, respectively.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.27 no.1
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• pp.1-6
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• 1994

Hydrolyzates which inhibit the angiotensin-I converting enzyme(ACE) were prepared from defatted anchovy meal by pepsin. These were tested for inhibitory activity against ACE, which is one of the hypertension inducing factors. The ACE inhibitory activity of the hydrolyzates increased until 20hrs of hydrolysis had elapsed but slightly decreased after that time. And presence of $50\%$ ethanol soluble peptide-nitrogen increased slowly up to 12hrs of hydrolysis, and then mainly increased until 20hrs of hydrolysis was completed. From the profiles of gel permeation chromatography on a Bio-gel P-2 of $50\%$ ethanol soluble fraction obtained from hydrolyzate for 20hrs, the higher active fractions were 2'($IC_{50}=45\;{\mu}g\;protein/ml$) and 4'($IC_{50}=76\;{\mu}g\;protein/ml$). Amino acid analysis showed major quantities of glutamic acid, leucine, lysine for 2'and aspartic acid, threonine for 4' respectively.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.26 no.5
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• pp.416-423
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• 1993

Fish sauces prepared from sardine, Sardinops melanosticta were tested for inhibitory activity against angiotensin-I converting enzyme(ACE). Three kinds of fish sauces were prepared from scrap(S), meat(M) and round(R) of sardine, respectively. ACE inhibitory activity of sardine sauce S and R decreased with the elapse of fermentation period, whereas that of sardine sauce M increased to 30 days and thereafter decreased. ACE inhibitory activity of sardine sauce M fermented with koji was higher than that without koji. And occurrence of $5\%$ TCA soluble peptide-nitrogen was similar to tendancy of the ACE inhibitory activity. The ACE inhibitory activity increased with an increment of amounts added and was stable at heat treatment in boiling water bath for 5hrs. $IC_{50}\%$ (Amounts of inhibitors need for $50\%$ inhibition) of the sardine sauce S, M and R fermented with(without) koji during 90 days was $125{\mu}g(140{\mu}g),\;200{\mu}g(100{\mu}g)$ and $125{\mu}g(135{\mu}g)$, respectively. From the profiles of fractionation of the sardine sauce R fermented without koji for 90 days, the molecular weight of most active fraction was about 1,400 and the amino acids of Glu, Ala, Leu and Lys were found in abundance.

• Korean Journal of Medicinal Crop Science
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• v.26 no.5
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• pp.370-381
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• 2018

Background: To enhance the taste and physiological characteristics of Lycii fructus (Gugija) extracts, we investigated the changes in the physiological characteristics of Gugija extracts caused by adding white ginseng (WG) and red ginseng (RG) Methods and Results: Gugija extracts, including 10G10, 10GW-G8 : 2, -G6 : 4, -G4 : 6, -G2 : 8, and -G0 (mixtures made by replacing 0, 20, 40, 60, 80, and 100% of Gugija with WG), as well as 10G10, 10GR-G8 : 2, -G6 : 4, -G4 : 6, -G2 : 8, and -G0 (mixture made by replacing 0, 20, 40, 60, 80, and 100% of Gugija with RG) were extracted with water at 10 times the respective mixture's volume. The antioxidant activities of Gugija extracts were investigated by assessing their 1,1-diphenyl-2-picrydrazyl (DPPH) and 2,2'-azinobis(3ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activity, ferric reducing antioxidant potential (FRAP) activity, nitrite scavenging activity, and angiotensin converting enzyme (ACE) inhibitory activity. As the amount of WG added increased, the DPPH, and, ABTS radical scavenging activity, and FRAP activity of the Gugija extract decreased. The half maximal inhibitory concentration ($IC_{50}$) value of 10G10, 10GW-G6 : 4, 10GR-G6 : 4, and 10GR-G0 for DPPH radical scavenging activity were $25.50{\pm}1.04$, $52.06{\pm}1.46$, $16.87{\pm}1.24$, and $9.50{\pm}0.16{\mu}{\ell}/m{\ell}$, respectively. On the other hand, the physiological activity of Gugija extract increased with the addition of increasing amounts of RG. However, ACE inhibitory activity was the highest ($50.25{\pm}2.58%$) in the Gugija 10-fold extract without any added RG. Conclusions: From the above results, we suggest that adding RG to Gugija extracts increase their antioxidant, FRAP, and nitrite scavenging activities.