• 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 $92\;{\mu}M$.

• 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 Food Science and Technology
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• v.35 no.4
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• pp.733-737
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• 2003

To develop a high-valuable Korean traditional rice wine having antihypertension, effects of some cereal kojis and legumes on alcohol fermentation and angiotensin I-converting enzyme (ACE) inhibitory activity of Korean traditional rice wine were investigated. Korean traditional rice wine brewed by addition of 10% Indian-millet koji into the mash showed the greatest ACE inhibitory activity of 43.0% and good ethanol productivity. The ACE inhibitory activity increased up to 69.2% by addition of 50% of mungbean powder and 1% of dandelion petal into the mash.

• Journal of the Korean Society of Food Science and Nutrition
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• v.26 no.5
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• pp.775-783
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• 1997

Morphologically different 18 strains were isolated and examined for their abilities to inhibit ACE. Those strains were cultured in the medium containing 10% of soybean extract at 37$^{\circ}C$ for 48hr or fermented with boiled soybean at 3$0^{\circ}C$ for 60 days. The concentration of inhibitors to inhibit 50% of ACE activity, $IC_{50}$ was measured on the culture broth of each strain and also on the hot-water extract from 20, 40 and 60 day fermented Doenjang by each strain. As a result, SCB-3 which is isolated from Meju showed the highest ACE inhibitoryactivity on the cultured broth and 40 day matured Doenjang. Then, $IC_{50}$ of SCB-3 was 0.02 mg/ml and 0.26mg/ml respectively. SCB-3 was identified as a Bacillus subtilis based upon its morphological, biochemical and physiological properties. Changes in general components and ACE inhibitory activity of Doenjang fermented by SCB-3 were examined during 90 days. Total acidity of Doenjang was increased from 1.39% to 1.66% and pH was decreased from 6.02 to 5.79 after 90 days fermentation. Total sugar contents were decreased from 16.4% to 15.1% and reducing sugar contents was also decreased from 2.45% to 1.62%. Total nitrogen contents were nearly not changed, but amino nitrogen contents were drastically increased from 196mg% to 541mg%. The numbers of total microorganism were increased to 1.1$\times$$10^{8}$ cells/g after 45 days. Protease activity was increased to 622.1U/g after 75 days. The highest ACE inhibitory activity was shown in 60 day fermented Doenjang and $IC_{50}$ of the hot-water extract was 0.31mg/ml.

• Food Science of Animal Resources
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• v.28 no.5
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• pp.587-595
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• 2008

In order to develop a new starter for fermented milk, 1037 bacterial strains were isolated from raw milk. The strain that showed excellent acid producing and angiotensin converting enzyme (ACE) inhibitory activity (88.6%) was selected and identified as a Lactobacillus zeae based on the result of API carbohydrate fermentation pattern and 16S rDNA sequence. Lactobacillus zeae RMK354 was investigated further to study its physiological characteristics. It showed strong ACE inhibitory activity compared with commercial LAB starters tested. The optimum growth temperature of L. zeae RMK354 was $40^{\circ}C$ and it took 10 hr to reach pH 4.3 under this condition. L. zeae RMK354 showed more sensitive to penicillin-G, bacitracin, novobiocin, in a comparison of 14 different antibiotics, and showed most resistance to polymyxin B and vancomycin. It showed higher esterase and leucine arylamidase activities compared with 16 other enzymes. It was comparatively tolerant to bile juice and able to survive at pH 2 for 3 hr. It showed inhibitory activity against Salmonella Typhimurium with the rate of 60%. Based on these and previous results, L. zeae RMK354 could be an excellent starter culture for fermented milk with high level of ACE inhibitory activity.

• 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.

• The Korean Journal of Food And Nutrition
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• v.16 no.4
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• pp.347-352
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• 2003

Physiological functionalities of various extracts from Danmemil and legumes were determined and its optimal extraction conditions were also investigated. Angiotensin I-converting enzyme (ACE) inhibitory activity and tyrosinase inhibitory activity of Danmemil were higher in water extracts (53%, 58%) than those of ethanol extracts. However, its electron-donating ability was the highest in ethanol extracts (72%). ACE inhibitory activity and electron-donating ability of Black bean No. 1 and Taekwangkong(one of bean) were higher in water extracts than those of ethanol extracts, whereas SOD-like activity was the highest in ethanol extracts. ACE inhibitor and tyrosinase inhibitor of Danmemil were maximally extracted when it were treated with 20 times of distilled water at 35$^{\circ}C$ for 24 h and 36 h, respectively. Its electron donating compound was maximally extracted by treatment of 50$^{\circ}C$ for 18 h. ACE inhibitor of Black bean No. 1 was extracted maximally when it was treated with distilled water (1 :20) at 20$^{\circ}C$ for 24 h, whereas the other functional compounds were maximally extracted at 20$^{\circ}C$ for 18 h.

• BMB Reports
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• v.35 no.2
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• pp.239-243
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• 2002

Angiotensin I that converts the enzyme (ACE) inhibitory peptide, Gly-Pro-Leu, previously purified and identified from the Alaskan pollack skin gelatin hydrolysate, were synthesized. In addition, the peptides Gly-Leu-Pro, Leu-Gly-Pro, Leu-Pro-Gly, Pro-Gly-Leu, Pro-Leu-Gly, Gly-Pro, and Pro-Leu, which consisted of glycine, proline, and leucine, were synthesized by the solid-phase method. The $IC_{50}$ values of each tripeptide - namely Leu-Gly-Pro, Gly-Leu-Pro, Gly-Pro-Leu, Pro-Leu-Gly, Leu-Pro-Gly, and Pro-Gly-Leu - were 0.72, 1.62, 2.65, 4.74, 5.73, and $13.93{\mu}M$, respectively. The ACE inhibitory activity of these tripeptides was higher than that of dipeptides, such as Gly-Pro and Pro-Leu with $IC_{50}$ values of 252.6 and $337.3\;{\mu}M$, respectively. Among the tripeptides, Leu-Gly-Pro and Gly-Leu-Pro had higher inhibitory activity than Gly-Pro-Leu that was isolated from the Alaskan pollack skin gelatin hydrolysate. Among the different types of tripeptides that were examined, the highest ACE inhibitory activity was observed for Leu-Gly-Pro. It had the leucine residue at the N-terminal and proline residue at the C-terminal.

• 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.

• Preventive Nutrition and Food Science
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• v.6 no.2
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• pp.117-121
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• 2001

Changes in antioxidative activity and Angiotensin converting enzyme(ACE) inhibitory activity in juice prepared from Dolsan leaf mustard kimchi (DLMK) ar various fermentation temperatures were investigated. Antioxidative activity of juice from optimally ripened DLMK at 20 and 3$0^{\circ}C$ showed 80 and 83%, respectively. Juice from 10-day fermented DLMK at 3$0^{\circ}C$ showed 62% inhibitory activity against the ACE. In the juice fermented DLMK at 2$0^{\circ}C$~3$0^{\circ}C$, physiological activity was higher than that of the 4~1$0^{\circ}C$. In particular, optimally ripened DLMK at 3$0^{\circ}C$ showed the highest physiological activity. The physiological activity in DLMK juice at the fermentation period increased significantly with an increase in the growth of microbes. Consequently, a maximum physiological activity was shown at the maximum cell number. These results suggest that the microorganisms in DLMK juice would play an important role in the physiological activity.