• Journal of Microbiology and Biotechnology
• /
• v.14 no.6
• /
• pp.1318-1323
• /
• 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.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.26 no.4
• /
• pp.321-329
• /
• 1993

The present study was conducted to elucidate the body modulating function of fermented seafood products. Angiotensin converting enzyme (ACE) acts in blood pressure regulation, converting angiotensin I to the potent vasoconstrictor angiotensin II and inactivating the vasodilator bradykinin to raise blood pressure. Salted and fermented anchovy which is one of the traditional fermented seafood in Korea was tested for inhibitory activity against ACE. ACE inhibitory activity of salted anchovy during the period of fermentation was increased with the elapse of fermentation days until fermentation of 60 days, but thereafter decreased inversely. When the fermented product was extracted with $50\%$ ethanol, the ACE inhibitory activity was the highest. And the ACE inhibitory activity was proportion to the content of $50\%$ ethanol soluble peptide-nitrogen of the fermented product. From the profiles of gel permeation chromatography on a Bio-Gel P-2 of $50\%$ ethanol soluble fraction obtained from salted and fermented anchovy fermented for 60 days at an ambient temperature, the higher activity fractions were C'($IC_{50}=97{\mu}g\;protein/ml$) and D'($IC_{50}=65{\mu}g\;protein/ml$). Amino acid analysis showed that the large quantify of threonine, glutamic acid, lysine for C' and serine, proline for D', respectively.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.29 no.3
• /
• pp.395-400
• /
• 2000

양파 조미액으로부터 ACE 저해활성 물질을 분리하기 위해 hexane, ethylether, ethylacetate, butanol과 물로 분획시, 4.8g의 당 함량과 31.9 mg의 phenol성 물질을 함유한 butanol 분획이 82.1%의 ACE 저해활성을 나타내었고, 70.3%의 ACE 저해활성을 보인 양퍄 조미액보다 높은 저해활성을 보였다. Butanol 분획을 Amberite XAD-2column으로 분리한 결과, ACE 저해활성을 보이는 미흡착 분획(F1)를 얻었다. 활성분획 F1을 Sephadex LH-20column으로 분획한 결과, 4개(F1-1,F1-2,F1-3,F1-4)의 분획을 얻었으며, 이중 F1-3 분획의 ACE 저해활성은 93%로 가장 높은 저해활성을 보였다. Sephadex LH-20 column chromatography에 의해 얻어진 활성분획F1-3을 Supercosil LC-18 column을 이용하여 분리한 결과, 6분대에서 ACE 저해활성을 가지는 단일 peak(F1-3a)를 얻었다. 각 정제 과정에서 얻은 분획들은 전형적인 flavonoid의 band I과 bandII의 피크를 보였다. 또한 ACE에 대한 저해기작은 flavonoid 물질이 보이는 전형적인 비경쟁적 저해양상을 보였다.

• BMB Reports
• /
• v.37 no.5
• /
• pp.552-555
• /
• 2004

Several studies have demonstrated the importance of angiotensin-converting enzyme (ACE) insertion (I)/deletion (D) polymorphisms in the pathogenesis of hypertension. This study sought to determine the association between the ACE I/D polymorphism and essential hypertension in young Pakistanis. The frequency of the ACE I/D polymorphism was established by a comparative cross-sectional survey of Pakistani patients suffering from essential hypertension and ethnically matched normotensive controls. Samples were collected from tertiary care hospitals in northern Pakistan. Hypertensive individuals were defined as those with a systolic blood pressure > 140 mmHg and/or diastolic blood pressure > 90 mmHg on three separate occasions, or those currently receiving one, or more, anti-hypertensive agents. DNA samples obtained from hypertensive (n=211) and normotensive (n=108) individuals were typed by PCR. The frequency of the ACE I/I genotype was significantly higher in hypertensive patients, aged 20-40 years, than in normotensive controls of the same age group ($\chi^2$ = 4.0, P = 0.041). Whereas no overall significant differences were observed between the I/I, I/D and D/D ACE genotypes (One way ANOVA, F=0.672; P=0.413). The association between the ACE I/I genotype and essential hypertension in individuals aged $\leq$ 40 years suggests that ACE has a role in early onset essential hypertension in Pakistan.

• Proceedings of the Korean Society of Fisheries Technology Conference
• /
• 2001.10a
• /
• pp.171-172
• /
• 2001

체내에 널리 분포되어 있는 angiotensin 전환효소(angiotensin converting enzyme, ACE ; peptidyldipeptide hydrolase, EC 3.4.15.1)는 angiotensinogen이 renin의 특이적 분해를 받아서 생성된 불활성형인 angiotensin I의 말단 dipeptide(His-Leu)를 절단하여 octapeptide인 활성형의 angiotensin II로 전환시키며, 이렇게 생성된 angiotensin II는 직접적으로 혈압상승 작용을 하거나 adrenal로부터 sediumretaining steroid hormone인 aldosterone의 유리를 촉진시켜 체내 나트륨을 저류시킨다. (중략)

• BMB Reports
• /
• v.35 no.2
• /
• pp.239-243
• /
• 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
• /
• v.12 no.1
• /
• pp.59-64
• /
• 2002

An angiotensin I-converting enzyme (EC 3.4.15.1) (ACE), which can convert inactive angiotensin I into angiotensin II, a vasoconstrictor, is one of the key enzymes in controlling hypertension. It is suggested that the inhibition of ACE prevents hypertension, and many inhibitory peptides have already been reported. In the current study, oligonucleotides encoding ACE inhibitory peptides (IY, VKY) were chemically synthesized and designed to be multimerised due to isoschizomer sites (BamHI, BglII). The cloned gene named AP3 was multimerised up to 6 times in pBluescript and expressed in BL2l containing pGEX-KG. The fusion protein (GST-AP3) was easily purified with a high recovery by an affinity resin, yielding 38 mg of synthetic AP3 from a 1-1 culture. The digestion of AP3 by chymotrypsin exhibited an $IC_50$ value of $18.53{\mu}M$. In conclusion, the present experiment indicated that AP3 could be used as a dietary antihypertensive drug, since the potent ACE inhibitory activity of AP3 could be activated by chymotrypsin in human intestine.

• Microbiology and Biotechnology Letters
• /
• v.36 no.4
• /
• pp.291-298
• /
• 2008

The cardiovascular angiotensin I-converting enzyme inhibitory activity, fibrinolytic activity and bbb-secretase inhibitory activity of four kinds of red wine were investigated during fermentation and post-fermentation. After 10 days of fermentation, the antihypertensive angiotensin I-converting enzyme (ACE) inhibitory activities of all the red wines ranged from 38.6% to 58.8%. However, the ACE inhibitory activities increased with the prolongation of the post-fermentation period; moreover, in the Vitis hybrid red wine, the ACE inhibitory activity reached its highest value, 76.9%, after 120 days of post-fermentation. During the fermentation and post-fermentation of all the red wines, fibrinolytic activity was weak or not detected. After 10 days of fermentation, Vitis labrusca B red wine exhibited the greatest antidementia $\beta$-secretase inhibitory activity of 54.8%, though $\beta$-secretase inhibitory activity decreased significantly to less than 10% during 120 days of post-fermentation. In conclusion, we obtained a highly valuable Vitis hybrid red wine that was fermented for 10 days at $25^{\circ}C$ with Vitis hybrid and S. cerevisiae K-7 and then post-fermentation for 120 days at $4^{\circ}C$.

• Fisheries and Aquatic Sciences
• /
• v.16 no.4
• /
• pp.237-242
• /
• 2013

We investigated the antioxidant and angiotensin I converting enzyme (ACE) inhibitory activities of red snow crab Chionoecetes japonicas shell (RSCS) hydrolysate by enzymatic hydrolysis and its molecular weight cut-off fractions. The RSCS hydrolysate was fractionated through two ultrafiltration membranes of 3 and 10 kDa cut-offs. Three fractions (<3 kDa, 3-10 kDa, and >10 kDa) were evaluated for total amino acid composition, antioxidant activities using 2'-azino-bis[3-ethylbenzthiazoline-6-sulfonic acid] ($ABTS^+$) radical scavenging and superoxide dismutase (SOD)-like activities and reducing power assays, and ACE inhibitory activity using Hou's method. Although all fractions showed activity, the <3 kDa fraction of RSCS hydrolysate exhibited the greatest $ABTS^+$ radical scavenging, SOD-like and ACE inhibitory activities. However, these fractions exhibited low reducing power. These results suggest that the low-molecular-weight enzymatic hydrolysate of RSCS could be used as a functional ingredient to control oxidative stress and ACE activity.

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