• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2002.10a
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• pp.191-192
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• 2002

Angiotensin I converting enzyme [EC 3.4.15.11 (ACE) is important in the maintenance of blood pressure. The enzyme removes histidyl-leucine from angiotensin I to form the blood-vessel-constricting octapeptide, angiotensin II, and degrades vasodilative bradykinin in blood vessels and stimulates e release of aldosterone in the adrenal cortex. (omitted)

• Preventive Nutrition and Food Science
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• v.3 no.4
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• pp.379-381
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• 1998

An angiotensin converting enzyme (ACE) inhibitor was isolated and partially purified from bovine blood plasma. Bovine blood plasma was obtained after removing blood cells by centrifugation, followed by the addition of anticoagulant to whole bovine blood. To precipitate plasma proteins, bovine blood plasma was treated with 4% trichloroacetic acid (TCA) as a final concentration .An ACE inhibitor was isolated from TCA supernatnat, using ultrafiltration, gel permeation chormatography, and reverse-phase high pressure liquid chromatogrpahy. The ACE inhibitor purified from TCA supernatant had IC50 values of 9.4$\mu$M.

• 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.

• Journal of Physiology & Pathology in Korean Medicine
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• v.18 no.5
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• pp.1505-1511
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• 2004

Inhibition of angiotensin converting enzyme (ACE) activity is one of the common antihypertensive methods functioned by drugs such as captopril, lisinopril and enalapril to serve as inhibitors of ACE. This study was designed to compare the effects of enalapril, an angiotensin-converting enzyme inhibitor and GLM002, an oriental medicine, on tail systolic pressure, aorta and plasma properties in spontaneously hypertensive rats (SHR) after 4 weeks of treatment. During the treatment, blood pressure was depressed to normal in GLM002 and enalapril groups. The treatments of enalapril and GLM002 were discontinued in 4 weeks. One week after the treatment stop, systolic blood pressure was smoothly increased in both groups; the increment of blood pressure was slightly greater in GLM002-SHR, but the increment of plasma ACE activity was proportionately similar in each group. In the aspects of the triglyceride, HDL and total cholesterol level, those levels were slightly different among each group. We also conducted clinical dosage of GLM002 to the patients who have mild and severe hypertension for approximately 7 weeks. Clinical treatments also showed remarkable efficiencies on blood pressure (systolic blood pressure, diastolic blood pressure), complete blood count (CBC) routine, differ count (NEUTRO, LYM, MONO, EOS and BASO) and R-chemistry. We conclude that GLM002, like already proven enalapril, plays a role as an angiotensin-converting enzyme inhibitor, and can be suggested as a drug candidate for curing hypertension.

• Korean Journal of Food Science and Technology
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• v.31 no.3
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• pp.848-854
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• 1999

Inhibitory compounds of angiotensin converting enzyme (ACE) were separated from Doenjang (traditional Korean fermented soybean paste). Water extracts from Doenjang which showed ACE inhibitory activity were separated with gel permeation chromatography (GPC), in which two fractions with high ACE inhibitory activities were obtained. The first fraction from GPC was further isolated by semi-preparative reverse phase preparative-HPLC (high performance liquid chromatography) and 2-dimensional electrophoresis/thin layer chromatography (TLC). The purified spot had molecular weight of 759 daltons and ninhydrin-positive non-peptide. The second fraction from GPC was also further isolated by semi-preparative reverse phase HPLC and $NH_2-column$ HPLC. One fraction with high ACE inhibitory activity was purified and characterized. Molecular weight of this fraction by LC-MS was 272.34 daltons. The active fraction was identified as Arg-Pro with ACE $IC_{50}$ of $92\;{\mu}M$.

• Asian-Australasian Journal of Animal Sciences
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• v.28 no.6
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• pp.855-861
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• 2015

Lactobacillus plantarum is used for fermentation of fish products, meat and milk. However, the utilization of these bacteria in egg processing has not been done. This study was designed to evaluate the potential of fermented egg albumen as a functional food that is rich in angiotensin I-converting enzyme inhibitors activity (ACE-inhibitor activity) and is antihypertensive. A completely randomized design was used in this study with six durations of fermentation (6, 12, 18, 24, 30, and 36 h) as treatments. Six hundred eggs obtained from the same chicken farm were used in the experiment as sources of egg albumen. Bacteria L. plantarum FNCC 0027 used in the fermentation was isolated from cow's milk. The parameters measured were the total bacteria, dissolved protein, pH, total acid and the activity of ACE-inhibitors. The results showed that there were significant effects of fermentation time on the parameters tested. Total bacteria increased significantly during fermentation for 6, 12, 18, and 24 h and then decreased with the increasing time of fermentation to 30 and 36 h. Soluble protein increased significantly during fermentation to 18 h and then subsequently decreased during of fermentation to 24, 30, and 36 h. The pH value decreased markedly during fermentation. The activities of ACE-inhibitor in fermented egg albumen increased during fermentation to 18 h and then decreased with the increasing of the duration of fermentation to 24, 30, and 36 h. The egg albumen which was fermented for 18 h resulted in a functional food that was rich in ACE-inhibitor activity.

• Journal of the Korean Society of Food Science and Nutrition
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• v.29 no.4
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• pp.719-725
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• 2000

This study focused on the purification and characterization of ACE inhibitor from Porphyra yezoensis. The dried Porphyra yezoensis was ground and hydrolyzed with 2.5 N HCl, followed by neutralization and centrifugation. Then, the subsequential purification of ACE inhibitor was carried out by Amberlite XAD 8, DEAE-Toyopearl 650C, Sephadex LH-20 column chromatography and reverse phase HPLC with C18 column. The purified ACE inhibitor was peptide which consisted of glycine (24.5%), arginine (56.8%) and proline (18.8%). Also, it showed the competitive inhibition pattern to ACE. The apparent molecular mass of purified peptide was 580 dalton, and an IC50 value of ACE inhibitor was 10.6 $\mu\textrm{g}$.

• Korean Journal of Microbiology
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• v.46 no.1
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• pp.9-14
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• 2010

In this study, lactic acid bacteria with high angiotensin converting enzyme inhibitor activity were isolated from Korean fermented food, such as kimchi and salted seafood. The strain HLJ59, isolated from salted shrimp showed the highest angiotensin converting enzyme inhibitor activity in DeMan Rogosa Sharpe broth. Optimum growth temperature of Lactobacillus brevis HLJ59 was at $34^{\circ}C$. Acid treatment at pH 3.0 for 1.5 h decreased cell viability from $9.9{\times}10^8$ CFU/ml to $3.11{\times}10^4$ CFU/ml. The bile extract concentration of 0.3%, 0.5%, and 1.0% in MRS broth did not inhibit the growth of HLJ59. Isolated strain HLJ59 showed more sensibility to amikacin, gentamycin, neomycin, streptomycin, kanamycin, cefmetazole, cephalothin, ampicillin, ticarcillin, sulbactam+ampicillin, amoxicillin+clavulanic acid (AMC), tetracycline, and sulfamethoxazole+trime thoprim (SXT) as compare to other 7 different antibiotics. However, it showed more resistance to cefoxatin, ceftnaxone, penicillin, ciprofloxacin, nalidixic acid, lincomycin, and chloramphenicol.

• Korean Journal of Microbiology
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• v.40 no.4
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• pp.355-358
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• 2004

Chunkookjang, Korean traditional fermented soybean food emerges as a functional food to improve intestinal function and blood circulation. During Chungkookjang fermentation, microorganisms, enzymes, and diverse bioactive compounds increase sharply. Chungkookjang contains diverse oligo-peptides. Formation of peptides was confirmed by SDS-PAGE. Solube fermented soybean in our sample contained Tyr, Gln-Lys, Trp, Gln, and Lys-Pro as major components. Lys-Pro (0.083 mg/100 g sample) was purified by HPLC analysis. Angiotensin I­converting enzyme (ACE) causes hypertension by converting angiotensin I to angiotension II. ACE inhibitory activity of Lys-Pro was determined to be $IC_{50}=32.1\;{\mu}M.$ Whether or not eating Chungkookjang can lower blood pressure was also determined. Sistolic blood pressure dropped by 15 mmHg, and diastolic blood pressure by 8 mmHg 2 hr after a single administration of 20 g of fermented soybean. Chungkookjang might be helpful in improving blood circulation since it has ACE inhibitor and antihypertenisve effect.

• The Korean Journal of Mycology
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• v.39 no.3
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• pp.194-197
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• 2011

Forty eight strains of yeast were cultured in potato dextorse(PD) broth at $30^{\circ}C$ for 24 hr and centrifuged with 12,000 rpm for 20 min. After concentrated the cultures, antihypertensive angiotensin I-converting enzyme(ACE) inhibitory activities of its concentrates were investigated. Among them, the concentrates from Saccharomyces cerevisiae Y183-3 showed the highest ACE inhibitory activity of 71.8%. The ACE inhibitor from Saccharomyces cerevisiae Y183-3 was maximally produced when Saccharomyces cerevisiae Y183-3 cultured in PD broth at $30^{\circ}C$ for 36 hr.