• 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.

• Journal of Microbiology and Biotechnology
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• 제16권5호
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• pp.757-763
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• 2006

Angiotensin I-converting enzyme (ACE) inhibitors have generally been very useful to remedy or prevent hypertension. This study describes the extraction and characterization of an ACE inhibitor from the fruiting body of Pholiota adiposa ASI 24012, which can be used as an antihypertensive drug. The maximal ACE inhibitory activity $(IC_{50};0.25mg)$ was obtained when the fruiting body of Pholiota adiposa ASI 24012 was extracted with distilled water at $30^{\circ}C$ for 12 h. After the purification of ACE inhibitor with ultrafiltration, Sephadex G-25 column chromatography, and reverse-phase HPLC, an active fraction with an $IC_{50}$ of 0.044 mg was obtained. The purified ACE inhibitory peptide was a novel pentapeptide, showing very little similarity to other ACE inhibitory peptide sequences. The molecular mass of the purified ACE inhibitor was estimated to be 414 daltons with a sequence of Gly-Glu-Gly-Gly-Pro, and showed a clear antihypertensive effect on spontaneously hypertensive rats (SHR) at a dosage of 1 mg/kg.

• Journal of Microbiology and Biotechnology
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• 제14권6호
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• pp.1318-1323
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• 2004

This study describes the purification and characterization of a novel antihypertensive angiotensin 1­converting enzyme (ACE) inhibitory peptide from Saccharomyces cerevisiae. Maximal production of the ACE inhibitor from Saccharomyces cerevisiae was obtained from 24 h of cultivation at $30^{\circ}C$ and its ACE inhibitory activity was increased by about 1.5 times after treatment of the cell-free extract with pepsin. After the purification of ACE inhibitory peptides with ultrafiltration, Sephadex G-25 column chromatography, and reverse-phase HPLC, an active fraction with an $IC_{50}$ of 0.07 mg and $3.5\%$ yield was obtained. The purified peptide was a novel decapeptide, showing very low similarity to other ACE inhibitory peptide sequences, and its amino acid sequence was Tyr-Asp-Gly-Gly-Val-Phe-Arg-Val-Tyr-Thr. The purified inhibitor competitively inhibited ACE and also showed a clear antihypertensive effect in spontaneously hypertensive rats (SHR) at a dosage of 1 mg/kg body weight.

• 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.

• 자연과학논문집
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• 제16권1호
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• pp.1-13
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• 2005

안지오텐신(ACE) 저해제는 항고혈 효과를 갖고 있으므로 오랫동안 고혈압의 예방이나 치료에 이용되어 왔다. 본 연구는 재조합 대장균으로부터 새로운 ACE 저해제를 생산하고 정제하며 나아가 이들이 구조-기능 관P를 규명하기 위해 수행되었다. Saccharomyces cerevisiae의 ACE 저해 펩타이드 유전자를 함유하고 있는 재조합 pGEX-4T-3을 대장균 BL21(DE3)로 형질전환 시켰다. 재조합 pGEX-4T-3을 갖고 있는 대장균 BL21(DE3)로부터 생산된 Glutathione-s 전이효소(GST) 융합 단백질을 얻어서 그중 ACE저해 펩타이드를 Sephadex G-25 컬럼 크로마토그래피로 정제하였다. 정제된 ACE 저해 펩타이드는 타이로신-아스파틱엑시드-그리신-글리신-발린-페닐알라린-아르기닌-발린-타이로신-트레오닌의 서열을 가진 새로운 decapeptide이었고 ACE에 대하여 경쟁적으로 저해하였다.

• 한국균학회지
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• 제39권3호
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• pp.194-197
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• 2011

항고혈압 효능이 우수하며 부작용이 없는 새로운 고혈압 예방 소재를 개발하고자 한국 식품연구원에서 분리, 동정한 48종의 효모들의 PD broth 배양 농축물들을 대상으로 angiotensin 전환효소(ACE) 저해활성을 조사하여 활성이 우수한 효모들을 선정한 다음 ACE 저해물질의 생산 최적 조건을 검토하였다. ACE 저해활성은 Saccharomyces cerevisiae Y183-3 균주의 PD broth 배양 농축물이 71.8%의 가장 높은 ACE 저해활성을 보여 최종 우수 균주로 선발하였다. 그리고 이 Y183-3 효모를 $30^{\circ}C$에서 36시간 PD broth에 배양했을 때 ACE 저해물질이 가장 많이 생산되었다.

• 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.

• Journal of Microbiology and Biotechnology
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• 제22권3호
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• pp.339-342
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• 2012

This study describes the characterization of a new angiotensin I-converting enzyme (ACE) inhibitory peptide from a Korean traditional rice wine. After purification of the ACE inhibitor peptides with ultrafiltration, Sephadex G-25 column chromatography, and successively $C_{18}$ and SCX solid-phase extraction, reverse-phase HPLC, and size exculsion chromatography, two types of the purified ACE inhibitors with $IC_{50}$ values of 0.34 mg/ml and 1.23 mg/ml were finally obtained. The two purified ACE inhibitors (F-1 and F-2) were found to have two kinds of novel oligopeptides, showing very little similarity to other ACE inhibitory peptide sequences. The amino acid sequences of the two purified oligopeptides were found to be Gln-Phe-Tyr-Ala-Val (F-1) and Ala-Gly-Pro-Val-Leu-Leu (F-2), and their molecular masses were estimated to be 468.7 Da (F-1) and 357.7 Da (F-2), respectively. They all showed a clear antihypertensive effect on spontaneously hypertensive rats at a dosage of 500 mg/kg.

• 한국축산식품학회지
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• 제43권1호
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• pp.184-194
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• 2023

Recently, interest in food-derived bioactive peptides as promising ingredients for the prevention and improvement of hypertension is increasing. The purpose of this study was to determine the structure and antihypertensive effect of an antioxidant peptide purified from velvet antler in a previous study and evaluate its potential as a various bioactive peptide. Molecular weight (MW) and amino acid sequences of the purified peptide were determined by quadrupole time-of-flight electrospray ionization mass spectroscopy. The angiotensin I-converting enzyme (ACE) inhibition activity of the purified peptide was assessed by enzyme reaction methods and in silico molecular docking analysis to determine the interaction between the purified peptide and ACE. Also, antihypertensive effect of the purified peptide in spontaneously hypertensive rats (SHRs) was investigated. The purified antioxidant peptide was identified to be a pentapeptide Asp-Asn-Arg-Tyr-Tyr with a MW of 730.31 Da. This pentapeptide showed potent inhibition activity against ACE (IC₅₀ value, 3.72 μM). Molecular docking studies revealed a good and stable binding affinity between purified peptide and ACE and indicated that the purified peptide could interact with HOH2570, ARG522, ARG124, GLU143, HIS387, TRP357, and GLU403 residues of ACE. Furthermore, oral administration of the pentapeptide significantly reduced blood pressure in SHRs. The pentapeptide derived from enzymatic hydrolysate of velvet antler is an excellent ACE inhibitor. It might be effectively applied as an animal-based functional food ingredient.

• 약학회지
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• 제37권1호
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• pp.41-48
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• 1993

The effect of captopril on the lung angiotensin converting enzyme (ACE) was investigated after 3 weeks oral administration (120~160 mg/kg/day) through drinking water in SpragueDawley rats. On the $^{125}$I-351A, an ACE inhibitor, binding assay in the isolated perpused lungs, the number of ACE molecules at the intrapulmonary endothelial cell surface was significantly decreased (p<0.001), and recovered to the normal level 7 days after discontinuation of captopril treatment. Intrapulmonary conversion ratio of Al to All was also significantly decreased (p<0.05) in the isolated perpused lungs. Bolus intravenous injection of angiotensin I did not showed pressor response in the both of systemic and pulmonary blood pressure of the anesthetized rats. ACE activity of the lung homogenates was also significantly reduced. These data consistently indicate the decrease of functionally active ACE molecule at the pulmonary artery after chronic captopril treatment. However, serum ACE activity was increased three fold in captopril treated rats compared to the normal rats. So, these results suggest that the functionally active ACE molecule at the pulmonary artery was still inhibited, which is directly associated with the antihypertensive effects, even if the total angiotensn converting enzyme induction was resulted after chronic captopril treatment.