• 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.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.44 no.2
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• pp.118-125
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• 2011

In this study, an angiotensin I-converting enzyme (ACE) inhibitor from squid skin was purified and characterized. Squid (Todarodes pacificus) skin protein isolates were hydrolyzed using six commercial proteases: alcalase, ${\alpha}$-chymotrypsin, neutrase, papain, pepsin, and trypsin. The peptic hydrolysate had the highest ACE inhibitory activity. The ACE inhibitory peptide was purified using Sephadex G-25 column chromatography and reverse phase high-performance liquid chromatography (HPLC) with a $C_{18}$ column. The purified ACE inhibitory peptide was identified and sequenced, and found to consist of seven amino acid residues: Ser-Ala-Gly-Ser-Leu-Val-Pro (657Da). The $IC_{50}$ value of the purified ACE inhibitory peptide was 766.2 ${\mu}M$, and Lineweaver-Burk plots suggested that the purified peptide acts as a noncompetitive ACE inhibitor. These results suggest that the ACE inhibitory peptide purified from the peptic hydrolysate of squid skin may be of benefit in developing antihypertensive drugs and functional foods.

• Mycobiology
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• v.39 no.1
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• pp.67-69
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• 2011

A cell-free extract of Saccharomyces cerevisiae containing the angiotensin I-converting enzyme (ACE) inhibitory peptide was treated in a successive simulated gastric-intestinal bioreactor (step 1: amylase digestion, step 2: gastric fluid digestion, step 3: intestinal fluid digestion) to illustrate the absorption pattern of antihypertensive ACE inhibitory peptide, and the ACE inhibitory activities of each step were determined. Total ACE inhibitory activities of step 1, step 2, and step 3 were 55.96%, 80.09%, and 76.77%, respectively. The peptide sequence of each steps was analyzed by MS/MS spectrophotometry. Eleven kinds of representative peptide sequences were conserved in each step, and representative new peptides including RLPTESVPEPK were identified in step 3.

• Mycobiology
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• v.33 no.3
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• pp.142-146
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• 2005

To produce a novel antihypertensive angiotensin I-converting enzyme (ACE) inhibitor from yeast, a yeast isolate, designated G-14 showing the highest ACE inhibitory activity was obtained and identified as Malassezia pachydermatis based on morphological, biochemical and cultural characteristics. The maximal extracellular ACE inhibitor production was obtained from M. pachydermatis G-14 when the strain was cultured in YEPD medium containing 0.5% yeast extract, 3.0% peptone and 2.0% glucose at $30^{\circ}C$ for 24 h and the final ACE inhibitory activity was 48.9% under the above condition.

• The Journal of Natural Sciences
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• v.16 no.1
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• pp.1-13
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• 2005

The angiotensin I-converting enzyme (ACE) inhibitor has anti-hypertensive effects and has long been used as prevention or remedy of hypertension. This study were carried out to produce and purify a new ACE inhibitor from recombinant E. coli and further elucidate its structure-function relationship. Recombinant pGEX-4T-3 containing ACE inhibitory peptide gene of Saccharomyces cerevisiae was transformed into E. coli BL21(DE3). Glutathione-S transferase (GST) fusion protein from E. Coli BL21(DE3) harboring the recombination pGEX-4T-3 was obtained and the ACE inhibitory peptide was purified with Sephadex G-25 column chromatography. The purified ACE inhibitory peptide was a novel decapeptide with sequence Tyr-Asp-Gly-Gly-Val-Phe -Arg-Val-Tyr-Thr which shows very low similarity to the other ACE inhibitory peptide sequence. The purified ACE inhibitor competitively inhibited ACE.

• BMB Reports
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• v.35 no.3
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• pp.251-254
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• 2002

The genetic factors that contribute to the development of coronary artery disease (CAD) are poorly understood. It is likely that multiple genes that act independently or synergistically contribute to the development of CAD and the outcome. Recently, an insertion/deletion (I/D) polymorphism of the human angiotensin I-converting enzyme (ACE) gene, a major component of the renin-angiotensin system (RAS), was identified. The association of the ACE gene D allele with essential hypertension and CAD has been reported in the African-American, Chinese, and Japanese populations. However, other studies have failed to detect such an association. It has been suggested that these inconsistencies may be due to the difference in backgrounds of the population characteristics. In the present study, we investigated the I/D polymorphism of the ACE gene in 103 subjects of both sexes, consisting of 59 normal controls and 44 patients with hypertension. The allele and genotype frequency were significantly different between the hypertensive and control groups (p < 0.01). Among the three ACE I/D variants, the DD genotype was associated with the highest value of the mean systolic blood pressure [SBP] and mean diastolic blood pressure [DBP] (p = < 0.05) in men, but not in women. In the overall population, the mean SBP and DBP was highest in DD subjects, intermediate in I/D subjects, and the least in II subjects.

• 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.

• The Korean Journal of Physiology and Pharmacology
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• v.2 no.5
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• pp.645-650
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• 1998

To assess the relationship between angiotensin-converting enzyme (ACE) gene polymorphism and myocardial infarction in Koreans, we recruited 112 healthy, unrelated subjects (mean age 53.4 years) and 104 myocardial infarction survivors (mean age 54.2 years) of both sexes. An insertion/deletion (I/D) polymorphism of the ACE gene was typed by polymerase chain reaction. The I allelic frequency of ACE gene in Korean subjects was irrelavant to myocardial infarction (patients, 65 control subjects 66%), as was true with the D allele. When compared with other populations, the frequency of D allele in Koreans (0.34) was lower than that in Caucasians, and was close to that of other Oriental populations. The data suggest that the ACE gene polymorphism is not an independent genetic risk factor for myocardial infarction in Koreans.

• Journal of Animal Science and Technology
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• v.49 no.1
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• pp.129-136
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• 2007

This study was performed to determine the protein profiles using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Angiotensin-I-converting enzyme(ACE) inhibitory activity (IC50) as affected by the various meat cuts, digestion times with pepsin. Hydrolysates having the protein concentration of 10 ug/mL had approximately 36∼39% ACE inhibitory activities, regardless of meat cut and digestion time. Protein concentration and ACE inhibitory activity of the diluted hydrolysate increased after 1-hr digestion. In original hydrolysates, ACE inhibitory activities of loin had higher than those of round (P<0.05). In addition, non-heated hydrolysates had higher ACE inhibitory activities than heated counterparts. When myosin B was digested by pepsin more than 1 hr, improved ACE inhibitory activities were observed as compared to the non-digested control.

• Biomedical Science Letters
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• v.18 no.4
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• pp.406-412
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• 2012

The polymorphism (insertion, I or deletion, D) of angiotensin converting enzyme (ACE) gene is designated as the presence of a 287 bp Alu repeat. The D/D homozygote carrier is associated with high ACE activity, and this high activity has been implicated with hypertension, coronary artery disease, or diabetic nephropathy. We studied the clinical candidate marker in ACE gene polymorphism using chemical and hematological analysis. The subjects are divided into normotensive and hypertensive groups and ACE genotype in the group was confirmed by PCR method. Chemical analysis was preceded with Hitachi7060, and hematological analysis was performed using Mythic 22. In 116 targeted people, 17 (38.64%) of 44 I/I genotype group are hypertension, 15 (34.09%) in 44 with D/I, but, D/D type in the 28 cases is 15 patients (53.57%) in hypertension. In hypertension group, biochemical analysis (triglyceride, and alkaline phosphatase) and hematological analysis (white blood cell, platelet) are showed high value in D/D genotype of ACE gene. The relationship between hypertension and ACE genotype is the same results as previously reported and we thought that the high laboratory value of white blood cell, platelet, triglycerides, and alkaline phosphatase are also indicator of hypertension in D/D type of ACE.