• Journal of Life Science
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• v.22 no.2
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• pp.220-225
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• 2012

The peptides of enzymatic hydrolysates from oyster were determined by inhibitory activity against angiotensin-converting enzyme. The ACE inhibitory activity of enzymatic oyster hydrolysates increases with hydrolysis time. Among enzymatic oyster hydrolysates, oyster hydrolysates incubated with Protamex showed the best ACE inhibitory activity after 10 h. Hydrolysates were filtered through a HiSep ultrafiltration membrane (M.W. cut-off 30 kDa, 10 kDa) to obtain the peptide fractions with ACE inhibition activity. These fractions were applied to an HPLC column (watchers 120 ODS-AP $250{\times}4.6$ ($5{\mu}m$)). Six active fractions were collected and the range of ACE inhibition was from 29.56 to 85.85%. Peptide was purified from fraction B, showing the highest ACE inhibitory activity, and its sequence was Leu-Gln-Pro. These results suggest that PEH may be beneficial for developing antihypertensive food and drug.

• Korean Journal of Medicinal Crop Science
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• v.15 no.2
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• pp.120-127
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• 2007

The objective of this research was to evaluate the ability of water and ethanol extracts from mulberry fruit (Morus alba L.) to influence the inhibitory activity of angiotensin converting enzyme (ACE) and xanthine oxidase(XOase). The total phenol contents and sixteen phenolic compounds were investigated in water and ethanol extracts. In order to understand the factors responsible for the potent antioxidant and antihypertensive ability of mulberry, it has been evaluated for anti-oxidative activity using Fenton's reagent/ethyl linoleate system and for free radical scavenging activity using the 1,1-diphenyl-2-picryl hydrazyl free radical generating system. The total phenol contents and total of phenolic compounds in ethanol extract showed higher levels than water extract in mulberry fruit six phenolic compounds (chlorogenic acid, narigin, syringic acid, quercetin, naringenin, kampferol) has a higher individual phenolic compound content in the 60% ethanol extraction than 80% ethanol extract. The inhibitory activity on angiotensin converting enzyme (ACE) were highest in 80% ethanol extract (9.0%). Also, activity of xanthine oxidase(XOase) inhibition appeared highest in 80% ethanol extracts and correlated well with the total phenolic content, which was modulated by the concentration of individual phenolic compounds. This result revealed, that strong biological activity was caused by specific phenol compound contents. Utilization of water and ethanol extracts from mulberry fruit are expected to be good candidate for development into source of free radical scavengers and anti-hypertentive activity

• Korean Journal of Food Science and Technology
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• v.35 no.4
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• pp.684-689
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• 2003

In previous paper, we isolated the bacteria, Bacillus subtilis JM-3, with proteolytic and fibrinolytic activity for candidate microorganisms that have rapid fermenting and physiological functions from anchovy sauce. This study was carried out to search physiological functions of Bacillus subtilis JM-3, such as antimicrobial, antioxidative, antimutagenic, angiotensin-converting enzyme inhibition, and anticarcinogenic activity in vitro. The cell free culture of Bacillus subtilis JM-3 showed strong antibacterial activity against Listeria monocytogenes, antioxidative activity with 87% of inhibition rate against linoleic acid, 50% of antimutagenic activity against N-nitrosodimethylamine and N-nitrosomorpholine, and 88.9% of growth inhibition rate against SNU-1 cell line (stomach cancer cell of human). However, Bacillus subtilis JM-3 did not show angiotensin-converting enzyme inhibition activity.

• Journal of Ginseng Research
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• v.20 no.3
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• pp.248-255
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• 1996

This study was devised to observe in vitro, the inhibitory effects of acidic polysaccharide fractions from Korean red ginseng (KRG) and white ginseng (KWG) on the lipolytic action of loxohormone-L and on angiotensin converting enzyme (ACE, peptidyldipeptidase hydrolase, EC 3.4.15.1) . The crude acidic polysaccharides (CAP) extracted from main and lateral roots of KRG and KWG were separately purified through several procedures. The total inhibitory activities on the lipolytic action of toxohormone-L of CAP from main roots of KRG and KWG was higher than those of CAP from lateral roots of KRG and KWG, respectively, and that of CAP from main root of KRG was 3.1 times higher than that of CAP from main root of KWG. The specific activity of CAP from main root of KRG was measured as 5.40 units/mg, when one unit was defined as the amount giving 50% inhibition on toxohormone-L induced lipolysls. A subfraction named PG4 3 obtained by replanted chromatography on DEAE-TOYOPEARL 650M gave the specific activity of 24.4 units/mg. On the other hand, it was found that the total inhibitory activity on ACE of CAP from lateral root of KRG was the highest among the 4 kinds of CAP, but the specific activity of CAP from lateral root of KWG was the highest.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.35 no.5
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• pp.529-533
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• 2002

The peptides inhibiting angiotensin converting enzyme (ACE) were isolated from the hydrolysate of manila clam (Ruditapes philippinamm) proteins prepared with thermolysin. The thermolysin hydrolysate was pretreated with membrane filter (MW cut-off 10,000) to obtain the peptide fraction with ACE inhibition. The crude peptides were applied to a Sephadex LH-20 column and eluted with $30\%$ methanol. The three active fractions (A, B and C) were collected and concentrated, and then applied to a SP-Toyopearl 650S column equilibrated with distilled water and was eluted with a linear gradient of NaCl concentration (0 to 1 M). The four active fractions (A-1, A-2, B-1 and C-1) were collected and concentrated, and then applied to a SuperQ-Toyopearl 650S column equilibrated with distilled water and was eluted with a linear gradient of NaCl concentration (0 to 1 M). The maximum inhibitory activity was observed in the fraction B-1Q showed the IC_{50} values of 0.748 $\mu$g. The abundant amino acids obtained from active fraction B-1Q were leucine, isoleucine, alanine and threonine.

• The Korean Journal of Food And Nutrition
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• v.36 no.6
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• pp.572-580
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• 2023

Hypertension is characterized by excessive renin-angiotensin system activity, leading to blood vessel constriction. Several synthetic compounds have been developed to inhibit renin and angiotensin-converting enzyme (ACE). These drugs often have adverse side effects, driving the exploration of plant protein-derived peptides as alternative or supplementary treatments. This study assessed the phenolic compound and amino acid content and the antioxidant and antihypertensive activity of 5 South Korean staple crops. Sorghum had the highest phenolic compound content and exhibited the highest antioxidant activity. Millet grains, particularly finger millet (38.86%), showed higher antihypertensive activity than red beans (14.42%) and sorghum (17.16%). Finger millet was found to contain a large proportion of branched-chain, aromatic, and sulfur-containing amino acids, which are associated with ACE inhibition. In particular, cysteine content was positively correlated with ACE inhibition in the crops tested (r=0.696, p<0.01). This study confirmed that the amino acid composition was more correlated with the antihypertensive activity of grains than the phenolic compound content. Finger millet mainly contained amino acids, which have higher ACE inhibitory activity, resulting in the strongest antihypertensive activity. These findings underscore the antihypertensive potential of select crops as plant-based food ingredients, offering insight into their biological functions.

• Food Science of Animal Resources
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• v.22 no.1
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• pp.87-93
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• 2002

Angiotensiri-I converting enzyme(ACE) catalyst the removal of the C-terminal dipeptide from the angiotensin-I to give the angiotensin-II, a potent peptide that causes constriction of regulation of blood pressure. Recently, ACE inhibitor peptides have been isolated from enzymatic digests of food protein. The aim of this study was to identify bovine casein hydrolysates with ACE inhibitory properties in different enzymatic hydrolysis conditions. The casein were hydrolyzed neutrase, alcalase, protamax, flavourzyme, premed 192, sumizyme MP, sumizyme LP and pescalase alone and with an enzyme combination. Premed 192 produced ACE inhibitory peptides most efficiently. In order to ACE inhibitory peptide produced enzymatic hydrolysis condition were premed 192 added to casein ratio of 1:100(w/w), and incubated at 47$\^{C}$ for 12hrs. Casein hydrolysate gave 50% inhibition(IC$\_$50/ value) of ACE activity at concentration with 248ug/ml(general method) and 265ug/ml(pretreatment method) respectively.

• Journal of the Korean Society of Food Science and Nutrition
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• v.43 no.1
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• pp.110-117
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• 2014

In this study, the biological activity of water and ethanol extracts from Chrysanthemum incidicum Linne by ultrafine grinding for functional food source are examined. The content of phenolic compounds from Chrysanthemum incidicum Linne were the highest when extracted for 6 hr with 70% ethanol. The extraction yield of water and ethanol extracts were $7.12{\pm}1.61$ mg/g and $7.51{\pm}2.14$ mg/g, respectively. With ultrafine grinding, water and ethanol extracts were $8.63{\pm}1.15$ mg/g and $9.33{\pm}1.35$ mg/g, respectively. In determining anti-oxidative activity of Chrysanthemum incidicum Linne extracts, DPPH of normal grinding extracts was 83.52% and ultrafine grinding was 92.37%. In ABTS radical cation decolorization, normal grinding, fine grinding, and ultrafine grinding extracts were 90% or higher. In antioxidant protection factor (PF), water and ethanol extracts of ultrafine grinding showed relatively high anti-oxidative activities of each 1.82 PF and 2.16 PF, respectively. The TBARS value of ultrafine grinding extracts were lower than normal grinding and fine grinding extracts. The inhibition activity on xanthin oxidase of Chrysanthemum incidicum Linne extracts was 67.53% in ultrafine grinded water extracts and 83.45% in ultrafine grinded ethanol extracts. Inhibition on xanthin oxidase of ethanol extracts showed a higher inhibition effect than water extracts, and ultrafine grinding was higher than normal grinding. In angiotensin converting enzyme inhibition activity, ultrafine grinding water extract was 24% or higher, and ethanol extract was 34% or higher. The elastase inhibition activity of ultrafine grinding extract was 25.56%, which was higher than 20.34% of fine grinding extracts. Water extracts did not show hyaluronidase inhibition activity but ethanol extracts showed 35% of hyaluronidase inhibition activity. The determining expression inhibition of iNOS and COX-2 protein in macrophage by Chrysanthemum incidicum Linne extracts with a Western blot analysis, iNOS and COX-2 protein expression inhibition by Chrysanthemum incidicum Linne ethanol extracts were 40% and 15%, respectively at 100 ${\mu}g/mL$ concentration. The inhibitory patterns of iNOS and COX-2 protein expression was concentration dependent. The result suggests that Chrysanthemum incidicum Linne extracts by ultrafine grinding may be more useful than normal grinding as potential sources due to anti-oxidation, angiotensin converting enzyme and xanthine oxidase inhibition, anti-inflammation effect.

• Archives of Pharmacal Research
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• v.21 no.2
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• pp.168-173
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• 1998

The epoxyalkanoyl derivatives were designed and synthesized as ACE inhibitors. Coupling of unsaturated carboxylic acids with amino acids and following epoxidation with dimethyldioxirane gave the epoxyalkanoyls with high yield. The inhibitory activity of synthesized compounds on angiotensin converting enzyme was $IC_{50}$ values of 0.06~5.5 ${\mu}M$.

• Preventive Nutrition and Food Science
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• v.6 no.4
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• pp.244-246
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• 2001

Angiotensin converting enzyme (ACE) inhibitor acts on the inhibition of ACE and causes a decrease in blood pressure. There have been several reports on screening of ACE inhibitors from natural food products and protein hydrolysates of various food sources. Ripe Cucurbita moschata Duch has been used as an oriental medicine in Korea. To isolate ACE inhibitors, crude water extracts of the edible portion of ripe Cucurbita moschata Duch were obtained after heating in water at 95$^{\circ}C$ for 2 h. Crude extracts were then filtered using PM-10 and YM-1 membranes. The membrane-filtered solution was loaded onto Sephadex G-15 column equlibrated with a phosphate buffer. Among the four major fractions of gel permeation chromatography, the second fraction had the highest inhibitory activity of 65%. Further purification of the fraction using reversed-phase HPLC with a $C_{18}$ column produced ACE inhibitors, which were identified as a mixture having molecular mass of 222 and 273 by Tandem mass spectrometry.