• 제목/요약/키워드: enzyme inhibitory activity

검색결과 1,009건 처리시간 0.026초

향신료의 약물대사효소 CYP3A4 저해효과 (Inhibitory Effect of a Drug Metabolizing Enzyme CYP3A4 on Spices)

  • 차배천
    • 생약학회지
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    • 제34권1호통권132호
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    • pp.86-90
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    • 2003
  • For the determination of inhibiting cytochrome P450(CYP)3A4 activity, an improvement HPLC method was established by using a new internal standard and solvent system. Moreover, CYP3A4 amount for a optimum reaction of enzyme was determined by a comparative study with a variety concentration of enzyme. Using a established method, inhibitory effect of CYP3A4 that is drug metabolizing enzyme Investigated on EtOAc extracts of 5-class spices. As a result of experiment, EtOAc extract of white pepper (Piper nigrum L.) showed strong inhibitory activity. On a continuous experiment, the fraction 2, 4 and 5 of while pepper extract showed remarkable inhibitory activity. Pipeline, a main constituent of pepper was not included in these fraction. It is suggested that major compounds for the inhibitory activity of white pepper may be other ingredient that is not piperine.

Optimization of Enzymatic Hydrolysis Conditions for Production of Angiotensin-I Converting Enzyme Inhibitory Peptide from Casein

  • Do, Jeong-Ryong;Kim, Ki-Ju;Kim, Hyun-Ku;Kim, Young-Myoung;Park, Yeung-Beom;Lee, Yang-Bong;Kim, Seon-Bong
    • Food Science and Biotechnology
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    • 제16권4호
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    • pp.565-571
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    • 2007
  • This study was carried out to investigate an optimum condition for the high angiotensin-l converting enzyme (ACE) inhibitory activity and the yield on enzyme concentration, casein concentration, and hydrolysis time. The optimum condition was performed by response surface methodology for acquirement of casein hydrolysate of milk which shows high ACE inhibitory activity, Among 8 tested enzymes, Protamex showed the highest activation degree with 77.03 unit/g from casein. Their hydrolysis degrees of flovourzyme 500MG, protamex, mixture from 1% casein were 85.5, 88.5, and 93.5%, respectively. The ranges of enzyme concentration (0.25-1.25%), casein concentration (2.5-12.5%), and hydrolysis time (20-100 min) as 3 independent variables through preliminary experiments of the yield of casein hydrolysate and ACE inhibitory activity, and it shows optimum response surface at a saddle point. It shows enzyme concentration (0.64%), casein concentration (8.38%), and hydrolysis time (55.81 min) in the yield aspect and showed the highest activity at enzyme concentration (0.86%), casein concentration (5.97%), and hydrolysis time (63.86 min) in ACE inhibitory aspect. The $R^2$ value of a fitted optimum formula on the hydrolysis yield was 0.9751 as the significant level of 1%. The $R^2$ value of a fitted optimum formula on ACE inhibitory activity is 0.8398, and the significance is recognized in the range of 5%.

매생이 유래 올리고당의 추출 분리 및 Angiotensin I Converting Enzyme 저해능 분석 (Analysis of Angiotensin I Converting Enzyme Inhibitory Activity of Oligosacchride Extracted from Capsosiphon fulvescens)

  • 김현우;이중헌
    • 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%).

Antioxidant and ACE Inhibitory Activities of Soybean Hydrolysates: Effect of Enzyme and Degree of Hydrolysis

  • Lee, Ji-Soo;Yoo, Mi-Ae;Koo, Seung-Hyun;Baek, Hyung-Hee;Lee, Hyeon-Gyu
    • Food Science and Biotechnology
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    • 제17권4호
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    • pp.873-877
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    • 2008
  • Native soy protein isolate (SPI) was hydrolyzed with 4 different proteolytic enzymes, including bromelain, papain, Neutrase, and Flavourzyme. SPI hydrolysates with the degree of hydrolysis (DH) in range of 6 to 15% were prepared by each enzyme. The angiotensin 1 converting enzyme (ACE) inhibitory and the antioxidant activities of the SPI hydrolysates, such as superoxide dismutase-like activity and inhibition of the linoleic acid autoxidation, were evaluated. Overall, as the DH increased, all evaluated bioactivities of the SPI hydrolysates significantly increased. The significantly highest ACE inhibitory and antioxidant activities were found in hydrolysates made with papain and bromelain, respectively. SPI hydrolysates by Flavourzyme showed the significantly lowest activity in all tested bioactivities. The results suggested that ACE inhibitory and antioxidant activities of SPI hydrolysates were determined by the DH and by the enzyme used.

Angiotensin I Converting Enzyme Inhibitory Activity of Krill (Euphausia superba) Hydrolysate

  • Kim Dong-Soo;Park Douck-Choun;Do Jeong-Ryong
    • 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.

Screening of Extracts from Red Algae in Jeju for Potentials MarineAngiotensin - I Converting Enzyme (ACE) Inhibitory Activity

  • 차선희;이기완;전유진
    • 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.

적포도주들의 발효와 후 발효 중 심혈관 관련 Angiotensin I 전환효소 저해활성과 혈전용해활성 및 $\beta$-secretase 저해 활성의 변화 (Changes of Angiotensin I-Converting Enzyme Inhibitory Activity, Fibrinolytic Activity and $\beta$-Secretase Inhibitory Activity of Red Wines During Fermentation and Post-Fermentation)

  • 노재덕;이은나;서동수;천종필;최신양;이종수
    • 한국미생물·생명공학회지
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    • 제36권4호
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    • pp.291-298
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    • 2008
  • 본 연구는 4종류의 한국산 포도를 이용하여 포도주를 제조한 후 이들의 발효와 후 발효중의 심혈관 관련 angiotensis I 전환효소 저해 확정과 혈전 용해 활성 및 항치매성 $\beta$-secretase 저해활성을 조사하였다. 발효 10일 후 모든 시료 포도주들의 항고혈압성 엔지오텐신 전환효소(ACE)저해활성은 $38.6%{\sim}58.8%$ 이었다. 그러나 후발효가 진행됨에 따라 ACE저해활성은 증가하여 세리단(Vitis hybrid) 포도주가 후발효 120일 후 최고인 76.9%에 도달하였다. 혈전용해활성은 모든 시료 포도주들에서 미약하거나 없었다. 발효 10일 후, 켐벨어리(Vitis labrusca B) 포도주가 54.8%의 가장 높은 항치매성 $\beta$-secretase저해 활성을 보였으나 후발효 120일 후에는 10% 미만으로 현저하게 감소되었다. 결론적으로 본 연구에서는 세리단 포도를 S. cerevisiae K-7 효모로 $25^{\circ}C$에서 10일간 발효 시킨 후 $4^{\circ}C$에서 120일간 후발효 시켜서 고부가가치의 생리 기능성을 가진 세리단 적포도주를 제조하였다.

Antihypertensive Angiotensin I-Converting Enzyme Inhibitory Activity and Antioxidant Activity of Vitis hybrid-Vitis coignetiae Red Wine Made with Saccharomyces cerevisiae

  • Jang, Jeong-Hoon;Lee, Jong-Soo
    • 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.

식품단백질 효소가수분해물의 Angiotensin-I 전환효소 저해작용 (Angiotensin-I Converting Enzyme Inhibitory Activity of Enzymatic Hydrolysates of Food Proteins)

  • 염동민;노승배;이태기;김선봉;박영호
    • 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.

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발아와 고압처리에 따른 벼(Oryza sativar L.) 추출물의 효소저해활성 (The Enzyme Inhibitory Activity of Ethanol Extracts Derived from Germinated Rough Rice (Oryza sativar L.) Treated by High Pressure)

  • 김민영;이상훈;장귀영;박혜진;;김신제;이연리;이준수;정헌상
    • 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.