• 제목/요약/키워드: enzyme inhibitory

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참치 자숙액의 Angiotensin 전환효소 저해작용 (Angiotensin Converting Enzyme Inhibitory Activity of Skipjack/Yellow Tuna Cooking Broth)

  • 여생규;이태기;안철우;김인수;구연숙;박영호;김선봉
    • 생명과학회지
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    • 제8권3호
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    • pp.312-317
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    • 1998
  • This study was designed to investigate the angiotensin convertin enzyme (ACE) inhibitory activity of skipjack/yellowpin tuna cooking broth. The cooking broth was pretreated with membrane filter (MW cut-off 5,000) to obtain the peptide fraction with ACE inhibition. the crude peptides fractionated with Amberlite IR-120 ($H^{+}$ form and followed by Bio-gel P-2, were separated into nine fractions (T-1 to T-9). The maximum inhibitory activity was observed in the fraction T-4 ($IC_{50}$ value, 0.619mg/ml). The abundant amino acids obtained from active fraction T-4 were phenylaanine, leucine and glutamic acid.

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Inhibition of Aminopeptidase N by 2-Hydroxy-3-amino-4-(p-nitrophenyl)butyryl Peptide Derivatives

  • Chung, Myung-Chul;Lee, Choong-Hwan;Lee, Ho-Jae;Chun, Hyo-Kon;Kho, Yung-Hee
    • Applied Biological Chemistry
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    • 제41권8호
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    • pp.608-610
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    • 1998
  • To investigate the inhibitory activity of 2-hydroxy-3-amino-4-phenylbutyrate-harboring aminopeptidase N inhibitors, p-nitro-AHPA-peptide derivatives (1 and 2) and an AHPA-peptide derivative (3) were synthesized by chain elongation from C-terminal end using DCC/HOBt as a coupling reagent. The peptides $1{\sim}3$ exerted strong inhibitory activities against aminopeptidase N with $IC_{50}$ values of 1.8, 7.3 and $24.0\;{\mu}g/ml$, respectively, and cytotoxicity on cancer cell lines in vitro.

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Isolation and identification of angiotensin I-converting enzyme inhibitory peptides derived from thermolysin-injected beef M. longissimus

  • Choe, Juhui;Seol, Kuk-Hwan;Kim, Hyun-Jin;Hwang, Jin-Taek;Lee, Mooha;Jo, Cheorun
    • Asian-Australasian Journal of Animal Sciences
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    • 제32권3호
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    • pp.430-436
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    • 2019
  • Objective: This study identified angiotensin I-converting enzyme (ACE) inhibitory peptides in beef M. longissimus injected with thermolysin (80 ppm) and stored for 3 days at $5^{\circ}C$. Methods: Crude peptides (molecular weight <3 kDa) were obtained from the thermolysin hydrolysate and separated into seven fractions. Fraction V showing the highest ACE inhibitory activity was further fractionated, yielding subfractions V-15, V-m1, and V-m2, and selected for superior ACE inhibitory activity. Finally, twelve peptides were identified from the three peak fractions and the ACE inhibitory activity ($IC_{50}$) of each peptide was evaluated. Results: The Leu-Ser-Trp, Phe-Gly-Tyr, and Tyr-Arg-Gln peptides exhibited the strongest ACE inhibitory activity ($IC_{50}$ values of 0.89, 2.69, and 3.09 mM, respectively) and had higher concentrations (6.63, 10.60, and 29.91 pg/g; p<0.05) relative to the other peptides tested. Conclusion: These results suggest that the thermolysin injection process is beneficial to the generation of bioactive peptides with strong ACE inhibitory activity.

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.

열수 및 효소적 가수분해로 제조된 틸라피아 비늘 젤라틴 가수분해물의 ACE 저해 활성 (Angiotensin I Converting Enzyme Inhibitory Effects of Gelatin Hydrolysates Prepared from Tilapia mossambica Scales by Hot Water and Enzymatic Extraction)

  • 안용석;이원우;이승홍;안긴내;고창익;오창경;오명철;김동우;전유진;김수현
    • 한국수산과학회지
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    • 제42권5호
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    • pp.426-433
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    • 2009
  • Fish scales have potential in functional food preparation due to their antioxidant and antihypertensive properties. We investigated the angiotensin I converting enzyme (ACE) inhibitory activity of Tilapia mossambica scale extracts. Hydrolysates of tilapia scales were prepared by enzymatic extraction using five proteases (${\alpha}$-chymotrypsin, Alcalase, Kojizyme, Protamex and trypsin) after scales were treated with hot water for 3 hr. Scale enzymatic hydrolysates prepared using both hot water and enzyme treatments exhibited elevated hydrolysis (about 25%-55%) compared to only enzyme treatment (about 15%-45%). Enzymatic hydrolysates (1 mg/mL) prepared by both hot water and enzyme treatments also showed significantly increased ACE inhibitory activities from about 20%-75%. The pattern of ACE inhibitory activities was similar to the degree of hydrolysis. Alcalase and ${\alpha}$-chymotrypsin hydrolysates displayed the highest ACE inhibitory activities ($IC_{50}$ = 0.83 mg/mL and 0.68 mg/mL, respectively). In addition, the ACE inhibitory effects of $IC_{50}$-chymotrypsin hydrolysates increased with decreasing molecular weight (5 kDa>, 10 kDa> and 30 kDa>), with the 5 kDa> fraction displaying the highest ACE inhibitory activity (about 89.9% and $IC_{50}$ = 0.1 mg/mL). We suggest that the peptide compounds of enzymatic hydrolysates prepared from tilapia scale enhances ACE inhibitory activity and might be useful as an antihypertensive material.

발아기간에 따른 벼(Oryza sativa L.)의 부위별 효소저해활성 (Enzyme Inhibition Activities of Ethanol Extracts from Germinating Rough Rice (Oryza sativar L.))

  • 김민영;이상훈;장귀영;박혜진;;김신제;이연리;이준수;정헌상
    • 한국식품영양과학회지
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    • 제42권6호
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    • pp.917-923
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    • 2013
  • 본 연구에서는 발아기간 및 부위별 벼 추출물에 대한 다양한 효소활성 저해효과를 조사하였다. 발아기간은 6일까지로 하였고, 발아된 벼는 왕겨+싹 부위와 현미로 나누어 80% ethanol로 환류 추출하였다. ${\alpha}$-Glucosidase 저해활성은 왕겨+싹 추출물에서 발아 전 26.32%에서 발아 5일차 39.38%로 증가하였으며, ${\alpha}$-amylase 저해활성은 왕겨+싹 추출물에서 발아 전 59.98%에서 발아 5일차 75.32%로 증가하였고, DPP-4 저해활성 또한 왕겨+싹 추출물에서 발아 전 38.80%에서 발아 5일차 47.77%로 증가하여 발아에 의해 효소활성 저해가 증가하였다. ACE 저해활성은 왕겨+싹 추출물에서 가장 높았으며 발아에 의해 증가하였다. Xanthine oxidase 저해활성은 발아가 진행됨에 따라 감소하였다. Lipase 저해활성은 발아 4일차 왕겨+싹 추출물이 36.78%로 무발아 31.72%에 비하여 증가하였다. 본 연구결과 벼를 발아시킬 경우 왕겨+싹에서 성인병 관료 효소를 억제하는 성분이 증가함을 알 수 있었으며, 추후에 어떠한 성분에 의한 것인지에 대한 연구가 수행되어야 할 것으로 판단된다.

Polysaccharide Degrading Enzyme을 이용한 참모자반 효소분해 추출물의 생리활성 연구 (Biological Analysis of Enzymatic Extracts from Sargassum fulvellum Using Polysaccharide Degrading Enzyme)

  • 조은경;강수희;최영주
    • KSBB Journal
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    • 제28권6호
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    • pp.349-355
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    • 2013
  • SC092 strain, producing a polysaccharide degrading enzyme, was isolated from the seawater. This strain was identified as Microbulbifer sp. using the comparative sequence analysis against known 16S rRNA sequence. A polysaccharide degrading enzyme from this strain was used to acquire the enzymatic extracts of Sargassum fulvellum. DPPH radical scavenging and SOD activity of the enzyme extracts of S. fulvellum were about 61.9% and 82.9% at 2 mg/mL, respectively. Nitrite scavenging activities was 52.5% at 2 mg/mL on pH 1.2. In addition, ${\alpha}$-glucosidase inhibitory activity was also increased in a dose-dependent manner and was about 52.7% at 2 mg/mL. To determine the influence of enzyme extracts of S. fulvellum on alcohol metabolism, the generating activity of reduced-nicotinamide adenine dinucleotide (NADH) by alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) were measured. ADH and ALDH activities were 118.0% and 177% at 2 mg/mL, respectively. ${\alpha}$-glucosidase inhibitory activity of enzyme extracts of S. fulvellum was remarkably increased in a dose-dependent manner and was about 52.7% at 2 mg/mL. These results indicate alcoholizing and ${\alpha}$-glucosidase inhibitory activities can be enhanced by the enzymatic extracts of S. fulvellum.

Enzymatic Characteristics of steroid $\Delta^1$-dehydrogenase from Arthrobacter simplex

  • Lee, Mi-Kyung;Bae, Moo
    • Journal of Microbiology and Biotechnology
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    • 제4권2호
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    • pp.119-125
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    • 1994
  • Steroid $\Delta^1$-dehydrogenase purified from hydrocortisone-induced cells of Arthrobacter simplex converted various 3-ketosteroids into their corresponding $\Delta^1$-dehydrogenated products. The transformation efficiencies depend upon the chemical structure of the steroids, especially length of the side chain at 17 position and hydroxyl groups at 11 and 17 positions. The Km values for androstenedione, the most favorable substrate examined, and hydrocortisone were 74 ${\mu}M$ and 294 ${\mu}M$, respectively. The optimum temperature and pH of the enzyme reaction were 35$^{\circ}C$ and pH 9, respectively, and the enzyme was relatively stable at the range from 20 to 35$^{\circ}C$ and from pH 5 to 10 after one hour of incubation. The enzyme activity was markedly inhibited in the presence of $Cu^{2+},\;Fe^{3+},\;Hg^{2+},\;Mo^{6+}$ ions, and somewhat inhibited by $Zn^{2+}$ and $Fe^{2+}$. $\alpha,\alpha'$-Dipyridyl that inhibits 9$\alpha$-hydroxylase and accumulates 1,4-androstadiene-3,17-dione from sterols revealed no inhibitory effect on this enzyme. EGTA showed inhibitory effect. $\beta$-Estradiol competitively inhibited the enzyme activity. Chemical modifications of the enzyme were attempted with several reagents. p-Hydroxymer-curibenzoate showed inhibition of the enzyme activity and protection of the substrate. This suggests that cysteine residue may be involved in the active site of the enzyme.

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오징어 간 액젓으로부터 분리된 Angiotensin Converting Enzyme 저해 Peptide의 특성 (Characteristics of Angiotensin Converting Enzyme Inhibitory Peptides from Salt-fermented Squid Liver Sauce)

  • 박영범
    • 한국식품영양과학회지
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    • 제39권11호
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    • pp.1654-1659
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    • 2010
  • 오징어 가공 부산물인 오징어 간의 효율적 이용을 위하여 오징어 간을 이용하여 액젓을 제조하고 이들 액젓의 ACE 저해효과를 살펴보았다. 액젓의 ACE 저해활성은 12개월까지는 점차적으로 증가하였으나 그 이후에는 저해활성이 둔화되어 거의 일정한 저해활성을 유지하였다. 숙성 액젓 중 15개월째 액젓($IC_{50}=29.66\;{\mu}g$)을 한외여과막으로 통과시켜 회수한 분자량 10,000 Da 이하의 저분자물질을 Bio-gel P-2 gel chromatography를 행하여 ACE 저해효과를 가지는 3개획분을 분취하였다. 이들 획분 중에서 ACE 저해효과가 가장 높은 B 획분을 SuperQ-Toyopearl 650S column을 이용한 음이온 교환크로마토그래피에 의해 B-1의 활성획분을 분리하였다. 획분 B-1의 아미노산 조성은 lysine, glycine 및 proline의 함량이 가장 많아 전체의 약 85%를 차지하였으며 $IC_{50}$$5.46\;{\mu}g$으로 나타났다.

Antioxidant and angiotensin I-converting enzyme inhibitory activities of northern shrimp (Pandalus borealis) by-products hydrolysate by enzymatic hydrolysis

  • Kim, Sang-Bo;Yoon, Na Young;Shim, Kil-Bo;Lim, Chi-Won
    • Fisheries and Aquatic Sciences
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    • 제19권7호
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    • pp.29.1-29.6
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    • 2016
  • In the present study, we investigated to the antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activities of the northern shrimp (Pandalus borealis) by-products (PBB) hydrolysates prepared by enzymatic hydrolysis. The antioxidant and ACE inhibitory activities of five enzymatic hydrolysates (alcalase, protamex, flavourzyme, papain, and trypsin) of PBB were evaluated by the 2, 2'-azino-bis [3-ethylbenzothiazoline-6-sulfonic acid] ($ABTS^+$) radical scavenging and superoxide dismutase (SOD)-like activities, reducing power and Li's method for ACE inhibitory activity. Of these PBB hydrolysates, the protamex hydrolysate exhibited the most potent ACE inhibitory activity with $IC_{50}$ value of $0.08{\pm}0.00mg/mL$. The PBB protamex hydrolysate was fractionated by two ultrafiltration membranes with 3 and 10 kDa (below 3 kDa, between 3 and 10 kDa, and above 10 kDa). These three fractions were evaluated for the total amino acids composition, antioxidant, and ACE inhibitory activities. Among these fractions, the < 3 kDa and 3-10 kDa fractions showed more potent $ABTS^+$ radical scavenging activity than that of > 10 kDa fraction, while the > 10 kDa fraction exhibited the significant reducing power than others. In addition, 3-10 kDa and > 10 kDa fractions showed the significant ACE inhibitory activity. These results suggested that the high molecular weight enzymatic hydrolysate derived from PBB could be used for control oxidative stress and prevent hypertension.