• 제목/요약/키워드: angiotensin converting enzyme (ACE) inhibitory activity

검색결과 279건 처리시간 0.028초

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.

기호음료 성분의 Angiotensin-I 전환효소 저해작용 (Angiotensin-I Converting Enzyme Inhibitory Activity by the Component of Traditional Tea Materials)

  • 도정룡;김선봉;박영호;김동수
    • 한국식품과학회지
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    • 제25권5호
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    • pp.456-460
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    • 1993
  • 전통 기호음료 성분에 의하여 나타나는 기능특성을 조사하기 위한 연구의 일환으로 결명자,들깨, 대추, 모과, 오미자, 오갈피 및 생강 추출물을 ion-exchange chromatography, 유기용매에 의한 분획, silica gel column chromatography, thin layer chromatography에 의하여 여러 가지 획분으로 분획하여 Angiotensin I 전환효소(ACE) 저해작용을 조사한 결과는 다음과 같다. 기호음료 원료에서 추출한 수용성 획분의 ACE 저해작용은 생강>오갈피>오미자>들깨>결명자>모과>대추의 순으로 나타났다. 일반 가정에서 널리 이용되고 있는 결명자에서 분리한 compound C 는 ACE 저해제로 알려져 있는 bradykinin에 비하여 ACE 저해작용이 비교적 낮았다.

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Fractionation and Angiotensin I-converting Enzyme (ACE) Inhibitory Activity of Gelatin Hydrolysates from by-products of Alaska Pollock Surimi

  • Park, Chan-Ho;Kim, Hyung-Jun;Kang, Kyung-Tae;Park, Jae-W.;Kim, Jin-Soo
    • Fisheries and Aquatic Sciences
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    • 제12권2호
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    • pp.79-85
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    • 2009
  • Gelatin hydrolysates with a high inhibitory activity against angiotensin I-converting enzyme (ACE) were fractionated from Alaska pollock surimi refiner discharge. The ACE-inhibitory activity, expressed as $IC_{50}$ (mg/mL), was highest (0.49 mg/mL) in gelatin hydrolysates formed by sequential 2-hr treatments of Pronase and Flavourzyme. After fractionation through four different membrane filters with molecular weight cut-offs of 3, 5, 10, and 30 kDa, the highest ACE-inhibitory activity (0.21 mg/mL) was observed with the 3-kDa filtrate.

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.

간장으로부터 Angiotensin Converting Enzyme 활성 저해물질 생성 균주의 분리 동정 (Isolation and Characterization of the Strain Producing Angiotensin Converting Enzyme Inhibitor from Soy Sauce)

  • 차명화;박정륭
    • 한국식품영양과학회지
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    • 제30권4호
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    • pp.594-599
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    • 2001
  • 혈압상승을 주도하는 효소인 angiotensin converting enzyme(ACE)의 활성을 저해하는 펩타이드를 생산하는 protease 분비 균을 간장으로부터 분리하여 동정하였다. 여러대두 발효식품으로부터 단백질 분해능이 있는 균주를 분리하고, 분리된 균주들 중에서 ACE 저해활성이 가장 높은 균주인 SS103 균주를 선정하였다. 선정된 SS103 균주는 운동성이 있는 gram 양성 간균으로 내생포자를 형성하는 호기성균이었으며, pH 5~9 사이에서 생육하고 생육온도는 2$0^{\circ}C$~$50^{\circ}C$로 내열성이 약한 중온균의 특성을 보였으며, glucose, sucrose, mannitol 및 sorbitol 등의 당 이용 특성을 보였다. 그리고 세포의 지방산 조성은 $C_{15:0}$ anteiso, $C_{17:0}$ cis 형 및 $C_{17:0}$ iso 형이 주된 지방산으로 각각 33.9%, 18.8% 및 16.5%의 분포를 나타내었다. 이상과 같은 분석 겨과를 토대로 SS103 균주는 Bacillus subtilis로 동정되었다. Bacillus subtilis SS103 균주의 최적 배양 조건은 $37^{\circ}C$, 초기배양액 pH 8.0에서 배양시간 48시간으로 나타났으며, 이때 통기량이 높은 경우 효소활성도 높은 특성을 보였다.을 보였다.

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Characterization of Antihypertensive Angiotensin I-Converting Enzyme Inhibitor from Saccharomyces cerevisiae

  • KIM, JAE-HO;LEE, DAE-HYOUNG;JEONG, SEOUNG-CHAN;CHUNG, KUN-SUB;LEE, JONG-SOO
    • Journal of Microbiology and Biotechnology
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    • 제14권6호
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    • pp.1318-1323
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    • 2004
  • This study describes the purification and characterization of a novel antihypertensive angiotensin 1­converting enzyme (ACE) inhibitory peptide from Saccharomyces cerevisiae. Maximal production of the ACE inhibitor from Saccharomyces cerevisiae was obtained from 24 h of cultivation at $30^{\circ}C$ and its ACE inhibitory activity was increased by about 1.5 times after treatment of the cell-free extract with pepsin. After the purification of ACE inhibitory peptides with ultrafiltration, Sephadex G-25 column chromatography, and reverse-phase HPLC, an active fraction with an $IC_{50}$ of 0.07 mg and $3.5\%$ yield was obtained. The purified peptide was a novel decapeptide, showing very low similarity to other ACE inhibitory peptide sequences, and its amino acid sequence was Tyr-Asp-Gly-Gly-Val-Phe-Arg-Val-Tyr-Thr. The purified inhibitor competitively inhibited ACE and also showed a clear antihypertensive effect in spontaneously hypertensive rats (SHR) at a dosage of 1 mg/kg body weight.

효소가수분해 조건에 따른 우유 케이신의 Angiotensin-I 전환효소 저해효과 (Angiotensin- I Converting Enzyme Inhibitory Properties of Bovine Casein Hydrolysates in Different Enzymatic hydrolysis Conditions)

  • 김현수;인영민;정석근;함준상;강국희;이수원
    • 한국축산식품학회지
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    • 제22권1호
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    • pp.87-93
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    • 2002
  • 최근 고혈압을 예방하기 위한ACE 저해 펩타이드에 대한 연구는 주로 여러 가지 식품 단백질의 효소 가수분해물로부터 얻어진 펩타이드를 중심으로 이루어지고 있다. 본 연구에서는 케이신을 여러 가지 상업용 단백질분해 효소를 사용하여 ACE저해 효과가 높은 가수분해물 제조시 가수분해 조건이 ACE저해효과에 미치는 영향을 알아보자 하였으며 적정 가수분해 조건을 설정하고자 하였다. ACE 저해효과를 가지는 케이신 가수분해 물을 제조하기 위한 효소 종류, 첨가량 및 가수분해시간은 효소는 Aspergillus oryzae 유래의 promod 192를 사용하고, 효소의 첨가량은 케이신에 대하여 1%, 반응시간은 47$^{\circ}C$에서 12시간으로 하는 것이 적당하였다. 이 때 케이신 가수분해물의 $IC_{50}$/값은 248.71ug/m1(통상법), 265.84ug/ml(전처리법)로서 ACE 저해효과가 높았다.

Purification and Characterization of Angiotensin I-Converting Enzyme Inhibitors from Sinapis alba L.

  • Yuk, Jin-Su;Lim, Young-Hee;Cho, Hong-Yon
    • Preventive Nutrition and Food Science
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    • 제5권2호
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    • pp.75-80
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    • 2000
  • To separate ACE inhibitors from edible plants, spices, and herbs, 285 extracts of 95 sources were screened for ACE inhibitory activity. The extract of Sinapis alba L. had the most potent ACE inhibitory activity. Mustard seeds were crushed homogeneously and extracted with hexane and water successively. Lyophilized water extract was fractionated with $H_2O$:butanol(1:1). The ACE inhibitor was purified from butanol fraction by methanol precipi-tation, gel filtration, HPLC, and FPLC with Superdex peptide HQ 10/30 column. The active fraction has been purified to homogeneity, which was proven by gel filtration using FPLC system. The yield was 0.02%. The com-pound has a molecular weight of about 640. The compound competitively inhibited ACE activity and the $IC_{50}$ value was 79$\mu\textrm{g}$/ml. The purified compound showed uterus contraction activity in isolated rat uterus.

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Antioxidant and Angiotensin I Converting Enzyme Inhibitory Activities of Red Snow Crab Chionoecetes japonicas Shell Hydrolysate by Enzymatic Hydrolysis

  • Yoon, Na Young;Shim, Kil-Bo;Lim, Chi-Won;Kim, Sang-Bo
    • Fisheries and Aquatic Sciences
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    • 제16권4호
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    • pp.237-242
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    • 2013
  • We investigated the antioxidant and angiotensin I converting enzyme (ACE) inhibitory activities of red snow crab Chionoecetes japonicas shell (RSCS) hydrolysate by enzymatic hydrolysis and its molecular weight cut-off fractions. The RSCS hydrolysate was fractionated through two ultrafiltration membranes of 3 and 10 kDa cut-offs. Three fractions (<3 kDa, 3-10 kDa, and >10 kDa) were evaluated for total amino acid composition, antioxidant activities using 2'-azino-bis[3-ethylbenzthiazoline-6-sulfonic acid] ($ABTS^+$) radical scavenging and superoxide dismutase (SOD)-like activities and reducing power assays, and ACE inhibitory activity using Hou's method. Although all fractions showed activity, the <3 kDa fraction of RSCS hydrolysate exhibited the greatest $ABTS^+$ radical scavenging, SOD-like and ACE inhibitory activities. However, these fractions exhibited low reducing power. These results suggest that the low-molecular-weight enzymatic hydrolysate of RSCS could be used as a functional ingredient to control oxidative stress and ACE activity.

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.