• 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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• 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.

• 대한화장품학회:학술대회논문집
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• 대한화장품학회 2003년도 IFSCC Conference Proceeding Book II
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• pp.479-479
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• 2003

We investigated the tyrosinase inhibitory effect using whitening materials such as arbutin, ethyl ascorbyl ether, glabridin, kojic acid, magnesium ascorbyl phosphate and ascorbic acid. Tyrosinase inhibition rate were determined varying the enzyme concentration, reaction time, reaction temperature and pH. The optimal conditions to measure the inhibitory efficacy were as follows. : enzyme concentration 1,500 or 2,000IU/mL, reaction time 15min(for the enzyme concentration 1,500 IU/mL) and l0min(for the enzyme concentration 2,000IU/mL), reation temperature 42$^{\circ}C$, pH 6.5. Under these conditions $IC_{50}$/ of arbutin, ethyl ascorbyl ether, glabridin, kojic acid, magnesium ascorbyl phosphate and ascorbic acid were calculated. In the case of magnesium ascorbyl phosphate, the inhibitory effect of tyrosinase was very low and the $IC_{50}$/ of magnesium ascorbyl phosphate could not be calculated. Other five materials showed good inhibitory effect of tyrosinase and can be used for the whitening materials.

• 한국식품영양과학회지
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• 제22권2호
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• pp.226-233
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• 1993

효소에 의한 가수분해로 식품단백질로부터 생리활성 peptide의 생성을 밝히기 위한 연구의 일환으로 효소에 의한 단백질 가수분해물의 ACE 저해작용을 검토한 결과는 다음과 같다. 1. 가수분해에 따른 ACE 저해능은 가수분해 8시간까지는 급격히 증가하다가 그 후로는 완만하게 증가하였으며, 특히 복합효소, bromelain 및 pepsin등에 의해 우수하게 나타났다. 그러나 trypsin 및 $\alpha$-chymotrypsin에 의한 egg albumin 및 casein 가수분해시에는 가수분해 8시간 이후에는 오히려 감소하는 경향을 나타내었다. 2. 단백질 가수분해물의 ACE 저해능은 첨가량의 증가와 함께 우수한 것으로 나타났으며, 가열에 대하여 비교적 안정한 것으로 나타났다. 3. 단백질 가수분해물의 아미노산 조성은 거의 유사한 것으로 나타났으며, 특히 glutamic acid의 함량이 월등히 많은 것으로 나타났다. 그러나 egg albumin 가수분해물의 경우는 glutamic acid의 함량이 적은 반면 alanine 및 cysteine의 함량이 다소 많은 것으로 나타났다 4. Gel 여과에 의한 단백질 가수분해물의 획분별 ACE 저해작용은 서로 비슷한 획 분에서 나타났으며 이 때의 분자량은 1,400부근으로 나타났다. 5. Gel 여과에 의한 ACE 저해작용 획분의 아미노산 조성은 서로 다른 것으로 나타났다.

• ALGAE
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• 제21권3호
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• pp.343-348
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• 2006

This study was conducted to screen in vitro angiotensin - I converting enzyme (ACE) inhibitory activities of methanol (MeOH) and aqueous extracts at 20°C and 70°C, respectively, prepared from twenty-six red algae obtained from the coast of Jeju Island in Korea. Among aqueous extracts at 20°C (20AE) from red algae Lomentaria catenata showed the strongest ACE inhibitory activity and Lithophyllum okamurae recorded the second highest activity. From MeOH extract at 20°C (20ME) Ahnfeltiopsis flabelliformis possessed the strongest ACE inhibitory activity. Remarkable activities from MeOH extracts at 70°C (70ME) were observed in Grateloupia filicina, Sinkoraena lancifolia and Grateloupia lanceolata. However, no significant activity was found in aqueous extracts at 70°C (70AE). The IC50 values, which are concentrations required to inhibit 50% activity of ACE, for ACE inhibitory activities of 20AE from Lithophyllum okamurae and L. catenata were 13.78 and 12.21 μg mL–1, respectively. The IC50 values of 20ME from A. flabelliformis and Laurencia okamurae were 13.84 and 106.15 μg mL–1. Those of the 70ME from Bonnemaisonia hamifera, Grateloupia filicina, Sinkoraena lancifolia, G. lanceolata, Gracilaria vermiculophylla and L. okamurae ranged from 25.82 to 124.69 μg mL–1.

• Preventive Nutrition and Food Science
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• 제10권3호
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• pp.239-243
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• 2005

Angiotensin I-converting enzyme (ACE) inhibitory activities of elk antler hydrolysates prepared with three kinds of proteases, pepsin, trypsin and $\alpha-chymotrypsin$, were investigated. The ACE inhibitory activity of the pepsinolytic hydrolysate was the highest with an $IC_{50}$ value of $9.3\mu g/mL.$ In addition, three kinds of pepsinolytic hydrolysates with relatively high molecular weights (over 10,000 Da), medium molecular weights (5,000 to 10,000 Da), and low molecular weights (below 5,000 Da) were fractionated using an ultrafiltration membrane system. The below 5,000 Da hydrolysate exhibited the highest ACE inhibitory activity. These results indicate that the pepsinolytic hydrolysates of elk velvet antler could be a good source of peptides with ACE inhibitory activity.

• Food Science and Biotechnology
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• 제16권4호
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• pp.572-575
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• 2007

The angiontensin converting enzyme (ACE) inhibitory peptides were separated from beef sarcoplasmic protein extract and their amino acid sequences were identified as GFHI, DFHINQ, FHG, and GLSDGEWQ. The 4 peptides were synthesized in a laboratory and the ACE inhibitory activities of pep tides was measured after 2 months of storage at $4^{\circ}C$ under different pH conditions (6.0, 6.5, 7.0, 7.5, and 8.0) and the exposure of different temperatures (70, 80, 90, and $100^{\circ}C$) for 20 min to evaluate industrial use. No significant difference was detected by pH and temperature abuse for 20 min during storage. When the synthetic peptides were digested by pepsin, trypsin, and chymotrypsin, the ACE inhibitory activity was not changed. These results indicated that the 4 synthetic peptides with ACE inhibitory activity were pH-stable, heat-stable, and resistant to proteinases in gastro-intestinal tracts. Therefore, those 4 peptides can be used as a source for functional food product with various applications.

• BMB Reports
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• 제35권2호
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• pp.239-243
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• 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.

• 한국식품과학회지
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• 제46권1호
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• pp.44-50
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• 2014

고압처리가 발아벼 추출물의 성인병관련 예방효과에 미치는 영향을 살펴보기 위하여 발아기간 및 고압처리 시간에 따른 효소저해활성을 살펴보았다. 발아기간은 6일로 하였고, 30 MPa의 압력 하에서 24시간 및 48시간 동안 처리하였다. ${\alpha}$-Glucosidase 저해활성은 발아초기에 대조구에 비해 고압처리 시 높은 범위의 저해활성을 나타내었으며, ${\alpha}$-amylase 저해활성은 발아기간 및 고압처리시간이 증가함에 따라 유의적으로 증가하였다. ACE 및 lipase 저해활성은 ${\alpha}$-glucosidase 저해활성과 유사하였으며, 고압처리가 대조구보다 높은 저해활성을 나타내었으며, 48시간 고압처리한 2일차 발아벼에서 가장 높은 저해활성을 나타내었다. Xanthine oxidase 저해활성은 발아초기에는 대조구보다 고압처리시 높았지만 발아가 진행됨에 따라 감소하였다. 이상의 결과로 부터 발아와 고압처리를 병행한 벼는 무발아 및 발아벼에 비하여 활용가치가 높을 것으로 판단되며, 성인병 예방을 위한 기능성식품소재로써 이용이 가능할 것으로 판단된다.

• 한국약용작물학회:학술대회논문집
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• 한국약용작물학회 2010년도 심포지엄 및 추계학술발표회
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• pp.430-430
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• 2010

In this study ethanol extracts of aerial part of Geranium thunbergii Sieb. et Zucc. was investigated for their ability to inhibit a-glucosidase, and thus was fractionated using two organic solvents, including dichloromethane, ethyl acetate. The ethyl acetate-soluble fraction, which manifested potent enzyme inhibitory properties, was then followed by tracking down the active compound by combining HPLC micro-fractionation to an enzyme assay in 96-well plate. The ${\alpha}$-glucosidase inhibitory activity profile showed that two peaks exhibited potent inhibitory activity, and then the structural analyses of the two peaks were carried out by HPLC-UV-MS. The main ${\alpha}$-glucosidase inhibitory compounds in the ethyl acetate-soluble fractions of ethanol extracts of Geranium thunbergii Sieb. et Zucc. were tentatively identified as geraniin and kaempferol-7-rhamnoside.