• Applied Biological Chemistry
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• 제41권4호
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• pp.270-272
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• 1998

Angiotensin converting enzyme (ACE) inhibitor was isolated from beef bone extract hydrolysate. After hydrolysis of beef bone extract with a commercial protease, ACE inhibitory peptide was purified by using ultrafiltration, gel permeation chromatography, and reverse-phase high pressure liquid chromatography. The purified ACE inhibitor was a pentapeptide, Gly-Pro-X-Gly-Pro.

• KSBB Journal
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• 제28권2호
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• pp.131-136
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• 2013

The hydrolysates prepared with various enzyme digestion of Capsosiphon fulvescens were used to measure the inhibitory effects against angiotensin I converting enzyme (ACE). The commercially available enzymes such as Celluclast, Viscozyme, Lysing enzyme, Flavourzyme, Alcalase and Pectinex were used to digest C. fulvescens and produce hydrolysates. The maximum ACE inhibitory activity was observed using Alcalase hydrolysis (72.9%). The optimal conditions of Alcalase extraction were pH 8.0 and extraction time for 12 hr. The hydrolysates were fractionated using preparative-LC and anion-exchange chromatography on DEAE-cellulose and the fraction B and B-2 were isolated. The ACE inhibitory activity of fraction B-2 by anion-exchange chromatography was 82.6%. The molecular weight of fraction B-2 estimated using size exclusion chromatography was about 1 kDa. The monosaccharide composition of the fraction B-2 was determined to be mannose (1.1%), glucuronic acid (1.3%), galactose (1.3%) and glucose (96.3%).

• Mycobiology
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• 제39권1호
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• pp.67-69
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• 2011

A cell-free extract of Saccharomyces cerevisiae containing the angiotensin I-converting enzyme (ACE) inhibitory peptide was treated in a successive simulated gastric-intestinal bioreactor (step 1: amylase digestion, step 2: gastric fluid digestion, step 3: intestinal fluid digestion) to illustrate the absorption pattern of antihypertensive ACE inhibitory peptide, and the ACE inhibitory activities of each step were determined. Total ACE inhibitory activities of step 1, step 2, and step 3 were 55.96%, 80.09%, and 76.77%, respectively. The peptide sequence of each steps was analyzed by MS/MS spectrophotometry. Eleven kinds of representative peptide sequences were conserved in each step, and representative new peptides including RLPTESVPEPK were identified in step 3.

• Fisheries and Aquatic Sciences
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• 제15권3호
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• pp.183-190
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• 2012

The purpose of this study was the purification and characterization of an angiotensin I converting enzyme (ACE) inhibitory peptide purified from enzymatic hydrolysates of rainbow trout Oncorhynchus mykiss muscle. After removal of lipid, the approximate composition analysis of the rainbow trout revealed 24.4%, 1.7%, and 68.3% for protein, lipid, and moisture, respectively. Among six hydrolysates, the peptic hydrolysate exhibited the highest ACE inhibitory activity. We attempted to purify ACE inhibitory peptides from peptic hydrolysate using high performance liquid chromatography on an ODS column. The $IC_{50}$ value of purified ACE inhibitory peptide was $63.9{\mu}M$. The amino acid sequence of the peptide was identified as Lys-Val-Asn-Gly-Pro-Ala-Met-Ser-Pro-Asn-Ala-Asn, with a molecular weight of 1,220 Da, and the Lineweaver-Burk plots suggested that they act as a competitive inhibitor against ACE. Our study suggested that novel ACE inhibitory peptides purified from rainbow trout muscle protein may be beneficial as anti-hypertension compounds in functional foods.

• Fisheries and Aquatic Sciences
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• 제5권1호
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• pp.21-27
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• 2002

Angiotensin I converting enzyme inhibitory activities of shelled krill (Euphausia superba) hydrolysates by autolysis and by hydrolysis with commercial proteases were analyzed. Among the proteases, Alcalase was the most effective protease for the hydrolysis of krill considering the degree of hydrolysis $(87.5\%)$ and the ACE inhibitory activity $(60\%)$. Four hour hydrolysis suggested as the most suitable and economic. In order to establish the optimum hydrolysis condition of krill, degree of hydrolysis and ACE inhibitory activity as affected by Alcalase concentration and water amount added were statistically analyzed by response surface methodology (RSM). The optimum hydrolysis condition was $2.0\%$ Alcalase hydrolysis in 2 volumes (v/w) of water at $55\% for 4 hr. The hydrolysate prepared from the optimum hydrolysis condition was fractionated by molecular weight. The lower molecular weight fraction showed the higher ACE inhibitory activity. $IC_{50}$ of the fraction under 500 Da was 0.57mg protein/mL.

• KSBB Journal
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• 제14권5호
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• pp.600-605
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• 1999

본 연구는 도축 폐기물인 가축혈액을 이용하여 항고혈압 기능성 식품소재로서의 angiotensin I converting enzyme 저해 펩타이드 분획을 생산하기 위한 조건과 가능성을 조사하기 위하여 수행되었다. 산업적으로 이용 가능한 단백분해효소 중 Alcalase가 혈장 원액 및 그로부터 분리된 albumin에 대하여 가장 높은 활성의 가수분해물을 생성하였다. 특히 albumin의 Alcalase 가수분해물과 이를 gel chromatography를 통새 분획하여 얻은 고활성 분획의 $IC_50$값은 각각 0.5 및 0.02 mg/mL로서 지금까지 보고된 식품단백질 유래 펩타이드 혼합물들과 비교할 때 활성이 매우 높은 것에 속함을 알 수 있었다. 또한 이 고활성 펩타이드 분획은 혈장 원액으로부터 단순한 한외여과만을 거쳐도 얻을 수 있음을 확인함으로써 산업적 실용화 가능성이 높은 공정임을 알게 되었다.

• Natural Product Sciences
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• 제17권4호
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• pp.363-366
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• 2011

Guibi-tang is a traditional medicine used for the treatment of colds. We investigated the levels of several compounds in Guibi-tang before and after fermentation with Lactobacillus and tested their ability to inhibit angiotensin-converting enzyme. Six known compounds (decursin, decursinol angelate, nodakenin, liquiritin, formononetin, and 6-gingerol) and 2 unidentified compounds were detected in Guibi-tang (GB) and fermented Guibi-tang (FGB) by an established HPLC-DAD method. The levels of the 6 known compounds were decreased after fermentation. FGB showed more potent inhibition of angiotensin-converting enzyme activity than GB. In conclusion, fermentation with Lactobacillus affects the content of several compounds in GB and improves its angiotensin-converting enzyme inhibitory activity.

• 동의생리병리학회지
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• 제19권1호
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• pp.119-123
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• 2005

In the courses of in vitro screening for the angiotensin converting enzyme (ACE) inhibitory activity of the various extracts from medicinal plants, n-BuOH soluble extract of the seeds of Xanthium strumarium was found to exhibit distinctive angiotensin converting enzyme (ACE) inhibitory activity. Bioassay-guided fractionation and purification of the n-BuOH soluble extract of the seeds of Xanthium strumarium afforded a new $xanthiazone-11-{\beta}-glucopyranoside$. The ACE activity was significantly inhibited by the addition of a new $xanthiazone-11-{\beta}-glucopyranosidein$ a dose-dependent manner of which $IC_{50}$ value was $21.8\;{\mu}g/ml$.

• 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.

• 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.