• Asian-Australasian Journal of Animal Sciences
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• 제16권9호
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• pp.1369-1373
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• 2003

ACE (Angiotensin-I converting enzyme) inhibitory peptides derived from foods are thought to suppress high blood pressure by inhibiting ACE. We tried to make efficient production of the ACE inhibitory hydrolysate from egg albumen. A hydrolysate digested by neutrase presented the highest ACE inhibitory activity ($IC_50\;value=256.35{\mu}g/ml$) and the proper proteolysis was occurred by 1.0% enzyme addition and 4 h incubation at $47^{\circ}C$. Antihypertensive effect of neutrase hydrolysate was investigated in spontaneously hypertensive rats (SHR, n=5). Systolic blood pressure (SBP) was decrease by 6.88% (-14.14 mmHg, p<0.05) at 3 h after oral administration of 300 mg/kg body weight, and by 13.33% (-27.72 mmHg, p<0.05) by emulsified hydrolysate. These results showed that it is very effective to utilize egg albumen as a protein source for the production of ACE inhibitory peptides. However, further studies are required to investigate the methods to increase recovery yield and the isolation of active peptide is necessary for determining its sequence responsible for ACE inhibitory activity.

• 생명과학회지
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• 제8권3호
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• pp.312-317
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• 1998

This study was designed to investigate the angiotensin convertin enzyme (ACE) inhibitory activity of skipjack/yellowpin tuna cooking broth. The cooking broth was pretreated with membrane filter (MW cut-off 5,000) to obtain the peptide fraction with ACE inhibition. the crude peptides fractionated with Amberlite IR-120 ($H^{+}$ form and followed by Bio-gel P-2, were separated into nine fractions (T-1 to T-9). The maximum inhibitory activity was observed in the fraction T-4 ($IC_{50}$ value, 0.619mg/ml). The abundant amino acids obtained from active fraction T-4 were phenylaanine, leucine and glutamic acid.

• 한국수산과학회지
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• 제44권2호
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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.

• Food Science and Biotechnology
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• 제16권4호
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• pp.565-571
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• 2007

This study was carried out to investigate an optimum condition for the high angiotensin-l converting enzyme (ACE) inhibitory activity and the yield on enzyme concentration, casein concentration, and hydrolysis time. The optimum condition was performed by response surface methodology for acquirement of casein hydrolysate of milk which shows high ACE inhibitory activity, Among 8 tested enzymes, Protamex showed the highest activation degree with 77.03 unit/g from casein. Their hydrolysis degrees of flovourzyme 500MG, protamex, mixture from 1% casein were 85.5, 88.5, and 93.5%, respectively. The ranges of enzyme concentration (0.25-1.25%), casein concentration (2.5-12.5%), and hydrolysis time (20-100 min) as 3 independent variables through preliminary experiments of the yield of casein hydrolysate and ACE inhibitory activity, and it shows optimum response surface at a saddle point. It shows enzyme concentration (0.64%), casein concentration (8.38%), and hydrolysis time (55.81 min) in the yield aspect and showed the highest activity at enzyme concentration (0.86%), casein concentration (5.97%), and hydrolysis time (63.86 min) in ACE inhibitory aspect. The $R^2$ value of a fitted optimum formula on the hydrolysis yield was 0.9751 as the significant level of 1%. The $R^2$ value of a fitted optimum formula on ACE inhibitory activity is 0.8398, and the significance is recognized in the range of 5%.

• Asian-Australasian Journal of Animal Sciences
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• 제16권3호
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• pp.417-424
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• 2003

Inhibitory activities against angiotensin I-converting enzyme (ACE) of enzymatic hydrolysates of porcine skeletal muscle proteins were investigated. Myosin B, myosin, actin, tropomyosin, troponin and water-soluble proteins extracted from pork loin were digested by eight kinds of proteases, including pepsin, $\alpha$-chymotrypsin, and trypsin. After digestion, hydrolysates produced from all proteins showed ACE inhibitory activities, and the peptic hydrolysate showed the strongest activity. In the case of myosin B, the molar concentration of peptic hydrolysate required to inhibit 50% of the activity increased gradually as digestion proceeded. The hydrolysates produced by sequential digestion with pepsin and $\alpha$-chymotrypsin, pepsin and trypsin or pepsin and pancreatin showed weaker activities than those by pepsin alone, suggesting that ACE inhibitory peptides from peptic digestion might lose their active sequences after digestion by the second protease. However, the hydrolysates produced by sequential digestion showed stronger activities than those by $\alpha$-chymotrypsin, trypsin or pancreatin alone. These results suggested that the hydrolysates of porcine meat were able to show ACE inhibitory activity, even if they were digested in vivo, and that pork might be a useful source of physiologically functional factors.

• Applied Biological Chemistry
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• 제49권2호
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• pp.114-124
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• 2006

생리활성을 갖는 새로운 기능성 물질을 개발할 목적으로 108종의 뽕잎을 이용하여 물과 80% 에탄올 추출물을 제조하고 이들의 Angiotensin converting enzyme(ACE) 활성억제효과 및 XOase(xanthine oxidase) 활성억제효과를 탐색하여 본 결과, 페놀함량이 물 추출물에서는 각자용산, 대정선 등 10종이, 80% 에탄올 추출물에서는 와룡, 하수상 등 23종이 15 mg/g 이상의 총 페놀함량을 나타내었으며, Angiotensin converting enzyme (ACE) 활성억제효과는 야마나까다까스께, 미지로 등 10종이 물 추출물 및 80% 에탄올 추출물에서 동시에 100%의 활성억제효과를 나타내었으며, 그 외 청일뽕 등 34종은 물 추출물에서, 원주고조 등 34종은 80% 에탄올 추출물에서 90% 이상의 활성억제효과를 나타내었다. 또한 XOase(xanthine oxidase) 활성억제효과는 물 추출물에서 청십조생, 수원상3호 등 5종이, 80% 에탄올 추출물에서 적목이 50% 이상의 활성억제효과를 나타내었으며, 그 외 수원뽕 등 27종은 물 추출물에서, 홍올뽕 등 21종은 80% 에탄올 추출물에서 약간씩의 효과를 나타내었다. 이상의 결과, g당 페놀함량이 적은 뽕잎이지만 높은 생리활성기능을 나타내는 여러 종의 뽕잎 물과 80% 에탄올 추출물들은 항고혈압 및 항관절염의 효과가 있는 기능성 식품소재로 활용할 수 있을 것으로 판단되었다.

• Mycobiology
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• 제39권2호
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• pp.137-139
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• 2011

A Vitis hybrid-Vitis coignetiae red wine was vinified by fermentation of a mixture of a Vitis hybrid.Vitis coignetiae must with Saccharomyces cerevisiae KCTC 7904 at $25^{\circ}C$ for 10 days. The Vitis hybrid-Vitis coignetiae red wine showed high antihypertensive angiotensin I-converting enzyme (ACE) inhibitory activity (67.8%) and antioxidant activity (76.7%). The antihypertensive ACE inhibitor in the Vitis hybrid-Vitis coignetiae red wine was partially purified by solid phase extraction chromatography, and its ACE inhibitory activity yielded an $IC_{50}$ of 1.8 mg/mL. Six kinds of oligopeptides, including five new kinds, were contained in the partially purified ACE inhibitor fraction from the red wine after 10 days of fermentation. Antioxidant activity decreased significantly from 76.7% to 40.5% when the post-fermentation period was prolonged to 30 days.

• Mycobiology
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• 제33권3호
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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.

• 한국식품과학회지
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• 제31권3호
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• pp.848-854
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• 1999

전통된장으로부터 안지오텐신전환효소(angiotensin converting enzyme; ACE)를 저해하는 물질을 추출하여 그 구조를 밝혀냈다. ACE 저해물질을 열수추출한 다음 gel permeation chromatography (GPC)를 통하여 ACE 저해작용이 큰 두 개의 큰 획분을 받았다. 앞획분은 90%와 70%의 ACE 저해효과를 나타내었으나 단일물질로 분리되지 않아 계속하여 역상 HPLC를 통하여 순수 분리를 하였다. 그러나 앞획분은 순수분리되지 않아 결국 2차원 전기영동/TLC를 통하여 분리한 결과 분자량이 759.63인 아미노기를 갖고 있는 비펩타이드 물질임이 밝혀졌다. 뒷획분은 다른 조건의 HPLC(reverse column과 $NH_2$, column)를 이용하여 순수분리에 성공하였다. 이중 ACE 저해효과가 큰 물질은 분자량 271.33인 dipeptide인 arginine-proline임을 밝혀냈다. 이물질의 ACE $IC_{50}$은 $92\;{\mu}M$이었다. 본 연구 결과는 대부분 ACE 저해물질이 3개 내지 7개 등의 긴 펩타이드임을 감안할 때, 짧은 dipeptide로 ACE 저해펩타이드가 한국의 전통된장에서 생산할 수 있음을 보여주고 있다.

• Asian-Australasian Journal of Animal Sciences
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• 제32권3호
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• pp.430-436
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• 2019

Objective: This study identified angiotensin I-converting enzyme (ACE) inhibitory peptides in beef M. longissimus injected with thermolysin (80 ppm) and stored for 3 days at $5^{\circ}C$. Methods: Crude peptides (molecular weight <3 kDa) were obtained from the thermolysin hydrolysate and separated into seven fractions. Fraction V showing the highest ACE inhibitory activity was further fractionated, yielding subfractions V-15, V-m1, and V-m2, and selected for superior ACE inhibitory activity. Finally, twelve peptides were identified from the three peak fractions and the ACE inhibitory activity ($IC_{50}$) of each peptide was evaluated. Results: The Leu-Ser-Trp, Phe-Gly-Tyr, and Tyr-Arg-Gln peptides exhibited the strongest ACE inhibitory activity ($IC_{50}$ values of 0.89, 2.69, and 3.09 mM, respectively) and had higher concentrations (6.63, 10.60, and 29.91 pg/g; p<0.05) relative to the other peptides tested. Conclusion: These results suggest that the thermolysin injection process is beneficial to the generation of bioactive peptides with strong ACE inhibitory activity.