• Title/Summary/Keyword: ACE저해

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Separation and Purification of Angiotensin I-converting Enzyme Inhibitory peptide from Mackerel (고등어 유래 항고혈압 peptide의 분리 정제)

  • DO Jeong-Ryong
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.33 no.2
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    • pp.153-157
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    • 2000
  • Hydrolysate which inhibit the Angiotensin I-converting enzyme (ACE) was prepared from mackerel muscle by pretense. The ACE inhibitory activity of mackerel muscle hvdrolysate (MMH) was $967 {\mu}g of IC_(50)$. ACE inhibitory peptides were isolated by ultrafiltration, gel permeation column chromatography (GPC), reversed phase column chromatography(RPC), reversed phasehigh performance liquid chromatography (RP-HPLC), and gel permeation high performance liquid chromatography (GP-HPLC) from the MMH. The amino acid sequence of the ACE inhibitory peptides was Tyr-Val-Ala. The $IC_(50)$ of this peptide for ACE from rabbit lung was $1.4 {\mu}M$.

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Antioxidant and ACE Inhibitory Activities of Styela clava according to Harvesting Time (채취시기에 따른 미더덕의 부위별 항산화 활성 및 ACE 저해 활성)

  • Lee, Dong-Won;You, Dong-Hyun;Yang, Eun-Kyung;Jang, In-Cheol;Bae, Myung-Suk;Jeon, Yuo-Jin;Kim, Suk-Ju;Lee, Seung-Cheol
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.39 no.3
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    • pp.331-336
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    • 2010
  • The antioxidant and angiotensin converting enzyme (ACE) inhibitory harvesting times were evaluated. During February and July of 2008, Styela clava were harvested once per month, and divided into flesh and tunic parts. Each collected part was extracted with water and 70% ethanol. DPPH radical scavenging activity (RSA) for flesh part was higher than that of tunic part, and water extract of flesh harvested at April showed the highest value (53.02% at 10 mg/mL). The highest ABTS RSA was found at water extract of flesh part harvested at March. Water extracts of flesh parts harvested from March to May showed relatively higher ACE inhibitory activity, and freezing did not affect ACE inhibitory activity. The results indicated that antioxidant and ACE inhibitory activity of S. clava were variable depending on harvesting time and parts.

Characteristics of Angiotensin-I Converting Enzyme Inhibitors Derived from Fermented Fish Product -1. Characteristics of Angiotensin-I Converting Enzyme Inhibitors Derived from Salted and Fermented Anchovy- (수산발효식품 중의 Angiotensin-I 전환효소 저해제의 특성 -1. 멸치젓갈 중의 Angiotensin-I 전환효소 저해제의 특성-)

  • KIM Seon-Bong;LEE Tae-Gee;PARK Yeung-Beom;YEUM Dong-Min;KIM Oi-Kyung;BYUN Han-Seok;PARK Young-Ho
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.26 no.4
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    • pp.321-329
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    • 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.

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Angiotensin I Converting Enzyme Inhibitory Activity of Hot-Water Extract and Enzymatic Hydrolysate of Fresh Water Fish (담수어 열수추출물 및 효소가수분해물의 Angiotensin I 전환효소 저해작용)

  • 김태진;윤호동;이두석;장영순;서상복;염동민
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.25 no.5
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    • pp.871-877
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    • 1996
  • Hot-water extract and enzymatic hydrolysate prepared from fresh water fish such as carp, snakehead, eel and israeli cart were tested for inhibitory activity against Angiotensin I converting enzyme(ACE). ACE inhibitory activity of enzymatic hydrolysate was higher than that of hot-water extract, and was the highest in enzymatic hydrolysate of carp among the tested samples. ACE inhibitory activity of 70% ethanol soluble fraction was higher than that of precipitated fraction, the highest in enzymatic hydrolysate of carp. Molecular weight of active fraction was about 1,400 in hot-water extract and slightly above in enzymatic hydrolysate. Amino acid of active fraction of hot-water extract was abundant in glycine, alanine, leucine and proline, whereas amino acids of aspartic acid, glutamic acid, glycine, alanine, valine, leucine and proline were abundant in enzymatic hydrolysate. $IC_{50}$/(amounts of inhibitors need for 50% inhibition) of hot-water extract was the range of 50.3~56.9$\mu\textrm{g}$, those of enzymatic hydrolysate 42.6~57.7$\mu\textrm{g}$.

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장내 가수분해조건에 의한 Casein 가수분해물의 Angiotensin Converting Enzyme 저해 효과

  • Hwang, Yu-Jin;Yang, Hui-Jin;Do, Jeong-Ryong;Lee, Su-Won
    • Proceedings of the Korean Society for Food Science of Animal Resources Conference
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    • 2005.10a
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    • pp.290-293
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    • 2005
  • 장내 단백질 가수분해효소에 의한 casein 분해산물들의 ACE 저해 활성을 비교하기 위하여 인공위액, 인공장액 및 인공위액과 장액 연속처리를 각각 반응조건으로 일정시간 casein을 가수분해한 후 각 효소 가수분해물이 혈압상승 peptide 생성효소인 Angiotensin converting enzyme(ACE)에 대한 저해활성을 측정하였다. 각 소화액에 따른 가수분해물은 모두 ACE 저해활성을 나타내었으며, 2시간 효소처리를 하였을 때, 인공위액, 인공장액, 인공위액과 장액 가수분해물은 각각 69%, 80% 및 88%로 최대 ACE 저해활성을 보였다. 그리고 casein의 가수분해 정도를 확인하기 위한 SDS-PAGE에서는 인공위액으로 처리한 군보다 인공장액으로 처리한 군이 더 작은 분자량으로 분해되는 것을 확인할 수 있었고, 인공위액과 장액을 함께 처리한 군에서는 1시간 안에 대부분의 분해가 이루지는 것을 관찰할 수 있었다.

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Angiotensin-I Converting Enzyme Inhibitory Activity of Algae (해조류의 Angiotensin-I 전환효소 저해작용)

  • LEE Heon-Ok;KIM Dong-Soo;DO Jeong-Ryong;KO Young-Su
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.32 no.4
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    • pp.427-431
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    • 1999
  • This study was conducted to investigate the inhibitory activity of water extracts and its enzymatic hydrolysates from algae against angiotensin-I converting enzyme (ACE). The 7 kinds of algae were extracted with water at $50^{\circ}C,\;70^{\circ}C$ and $98^{\circ}C$. ACE inhibitory activities of water extracts were the highest at $70^{\circ}C$, and those of ceylon moss, layer, green layer, sea mustard, seaweed fusiforme sea tangle and sea staghorn were $10.9\%,\;9.3\%,\;8.9\%,\;8.2\%,\;7.5\%,\;7.1\%$ and $7.0\%$, respectively. Layer, green laver sea mustard and ceylon moss of high ACE inhibitory activities among the 7 kinds of water extracts were hydrolyzed by maxazyme and papain during 24hrs. ACE inhibitory activity of enzymatic hydrolysates was higher than that of water extracts, and was the highest in enzymatic hydrolysates of laver among the tested samples. In laver hydrolysates by proteases, the highest ACE inhibitory activity and peptide-nitrogen contents were observed at 8 hours hydrolysis and the hydrolysates by maxazyme showed relatively higher activity than those by papain(31.3 and $27.9\%$, respectively). But peptide-nitrogen contents were greater in papain hydrolysates than in maxazyme.

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Angiotensin-Converting Enzyme Inhibitory Activity of Enzymatic Hydrolysates of Crassostrea gigas (Oyster) (굴 효소 가수분해물의 angiotensin converting enzyme 저해작용)

  • Do, Hyung-Joo;Park, Hye-Jin;Kim, Ok-Ju;Kim, Andre;Choi, Yeung-Joon;Choung, Se-Young;Ha, Jong-Myung
    • 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.

Angiotensin I-Converting Enzyme Inhibitory Activity of the ${\kappa}-Casein$ Fragments Hydrolysated by Chymosin, Pepsin, and Trypsin (${\kappa}-Casein$의 Chymosin, Pepsin 및 Trypsin 가수분해물에 대한 안지오텐신 변환효소 저해효과의 탐색)

  • Oh, Se-Jong;Kim, Sae-Hun;Kim, Sang-Kyo;Baek, Young-Jin;Cho, Kyung-Hyun
    • Korean Journal of Food Science and Technology
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    • v.29 no.6
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    • pp.1316-1318
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    • 1997
  • The isolated ${\kappa}-Casein$ on gel permeation chromatography was hydrolyzed by chymosin, trypsin, and pepsin. The 3% TCA soluble portion of the hydrolysates were dialyzed on the angiotensin-I converting enzyme (ACE) inhibition rate (%,) and inhibitory activity $(IC_{50})$ were determined. The trypsin hydrolysate exhibited the highest ACE inhibition rate while the chymosin hydrolysation showed the lowest activity. The hydrolysate was dialyzed using dialysis membrane with various molecular cut-offs, and $IC_{50}$ was determined. As the pore size of the dialysis tubing increased, the ACE inhibitory activity decreased.

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Effects of Salted-Fermented Fish Products and Their Alternatives on Angiotensin Converting Enzyme Inhibitory Activity of Kimchi During Fermentation (젓갈 및 젓갈 대용 부재료가 김치의 숙성 중 Angiotensin 전환효소 저해작용에 미치는 영향)

  • Park, Douck-Choun;Park, Jae-Hong;Gu, Yeun-Suk;Han, Jin-Hee;Byun, Dae-Seok;Kim, Eun-Mi;Kim, Young-Myung;Kim, Seon-Bong
    • Korean Journal of Food Science and Technology
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    • v.32 no.4
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    • pp.920-927
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    • 2000
  • Angiotensin converting enzyme(ACE) inhibitory activity of Kimchi added with salted-fermented fish products(SFFP), such as salted-fermented anchovy(SFA), salted-fermented anchovy sauce(SFAS), low salt-fermented anchovy sauce(LSFAS), salted-fermented small shrimp(SFS), low salt-fermented sandlance sauce(LSFSS) and their alternatives, such as oyster hydrolysate(OH), Alaska pollack hydrolysate(APH) and sea-staghorn extract(SSE) were studied during fermentation at $20^{\circ}C,\;10^{\circ}C\;and\;4^{\circ}C$. ACE inhibitory activities of Kimchi samples added with SFFP were increased until some fermentation period and then kept similarly constant levels at every fermentation temperature. Similar tendencies were occurred in amino nitrogen (AN) content. ACE inhibitory activities of Kimchi samples added with SFFP alternatives rapidly increased in 1st or 2nd day fermentation and then very slowly increased but AN contents showed roughly constant levels $(400{\sim}600\;mg/100\;g)$ in every fermentation temperature. Kimchi added with LSFAS had higher ACE inhibitory activity (>80%) with elevated level of AN (>600 mg/100 g) among the tested Kimchi samples. Kimchi samples added with SFFP alternatives also showed comparable activity to Kimchi added with SFFP This study shows that Kimchi added with SFFP and their alternatives is a good source as a functional food.

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ACE Inhibitory and Antihypertensive Effect of Chitosan Oligosaccharides in SHR (Chitosan 올리고당의 안지오텐신 전환효소 활성 억제 및 SHR에서의 고혈압 억제 특성)

  • Hong, Sang-Pill;Kim, Myung-Hee;Oh, Se-Wook;Han, Chan-Kyu;Kim, Yong-Hyun
    • Korean Journal of Food Science and Technology
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    • v.30 no.6
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    • pp.1476-1479
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    • 1998
  • Effect of chitosan oligosaccharides on the ACE (angiotensin I converting enzyme) inhibition and antihypertension in SHR (Spontaneously hypertensive rat) was examined. The ACE inhibition activity was observed in all the chitosan oligosaccharides used in this study, and chitosan trimer exhibited the highest inhibitory activity $(IC_{50}=0.9{\mu}M)$ compared with other chitosan oligosaccharides $(IC_{50}\;:\;2.4{\sim}100\;{\mu}M)$. The results suggested that chitosan trimer was a good inhibitor of ACE in molecular level. When the single oral dose (2.14 mg/kg, similar to dose level of Captopril, known as strong ACE inhibitor) of chitosan trimer was given to 8 or 21 week aged SHR, the blood pressure reduction of both SHRs in 4hrs were $27{\pm}4.8\;mmHg\;and\;36{\pm}4.3\;mmHg$, respectively. Therefore, it was suggested that chitosan trimer could be applicable as natural ACE inhibitor related to antihypertension.

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