• Title/Summary/Keyword: ACE inhibitory

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Physiological Characteristics and ACE Inhibitory Activity of Lactobacillus zeae RMK354 Isolated from Raw Milk (원유에서 분리한 Lactobacillus zeae RMK354의 생리적 특성 및 ACE 억제능)

  • Lim, Sang-Dong;Kim, Kee-Sung;Do, Jeong-Ryong
    • Food Science of Animal Resources
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    • v.28 no.5
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    • pp.587-595
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    • 2008
  • In order to develop a new starter for fermented milk, 1037 bacterial strains were isolated from raw milk. The strain that showed excellent acid producing and angiotensin converting enzyme (ACE) inhibitory activity (88.6%) was selected and identified as a Lactobacillus zeae based on the result of API carbohydrate fermentation pattern and 16S rDNA sequence. Lactobacillus zeae RMK354 was investigated further to study its physiological characteristics. It showed strong ACE inhibitory activity compared with commercial LAB starters tested. The optimum growth temperature of L. zeae RMK354 was $40^{\circ}C$ and it took 10 hr to reach pH 4.3 under this condition. L. zeae RMK354 showed more sensitive to penicillin-G, bacitracin, novobiocin, in a comparison of 14 different antibiotics, and showed most resistance to polymyxin B and vancomycin. It showed higher esterase and leucine arylamidase activities compared with 16 other enzymes. It was comparatively tolerant to bile juice and able to survive at pH 2 for 3 hr. It showed inhibitory activity against Salmonella Typhimurium with the rate of 60%. Based on these and previous results, L. zeae RMK354 could be an excellent starter culture for fermented milk with high level of ACE inhibitory activity.

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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    • v.16 no.4
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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.

γ-Aminobutyric Acid (GABA) Production and Angiotensin-I Converting Enzyme (ACE) Inhibitory Activity of Fermented Soybean Containing Sea Tangle by the Co-Culture of Lactobacillus brevis with Aspergillus oryzae

  • Jang, Eun Kyeong;Kim, Nam Yeun;Ahn, Hyung Jin;Ji, Geun Eog
    • Journal of Microbiology and Biotechnology
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    • v.25 no.8
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    • pp.1315-1320
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    • 2015
  • To enhance the γ-aminobutyric acid (GABA) content, the optimized fermentation of soybean with added sea tangle extract was evaluated at 30℃ and pH 5.0. The medium was first inoculated with Aspergillus oryzae strain FMB S46471 and fermented for 3 days, followed by the subsequent inoculation with Lactobacillus brevis GABA 100. After fermentation for 7 days, the fermented soybean showed approximately 1.9 g/kg GABA and exhibited higher ACE inhibitory activity than the traditional soybean product. Furthermore, several peptides in the fraction containing the highest ACE inhibitory activity were identified. The novel fermented soybean enriched with GABA and ACE inhibitory components has great pharmaceutical and functional food values.

Screening for Angiotensin 1-Converting Enzyme Inhibitory Activity of Ecklonia cava

  • Athukorala Yasantha;Jeon, You-Jin
    • Preventive Nutrition and Food Science
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    • v.10 no.2
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    • pp.134-139
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    • 2005
  • Seven brown algal species (Ecklonia cava, Ishige okamurae, Sargassum fulvellum, Sargassum horneri, Sargassum coreanum, Sargassum thunbergii and Scytosiphon lomentaria) were hydrolyzed using five proteases (Protamex, Kojizyme, Neutrase, Flavourzyme and Alcalase) and screened for angiotensin 1-converting enzyme (ACE) inhibitory activities. Most algal species examined showed good ACE inhibitory activities after the enzymatic hydrolysis. However, E. cava was the most potent ACE inhibitor of the seven species. Flavourzyme digest of E. cava exhibited an $IC_{50}$ of around $0.3\;{\mu}g/mL$ for ACE; captopril has an $IC_{50}$ of $\~0.05\;{\mu}g/mL$. The Flavourzyme digest was separated to three fractions by an ultrafiltration membrane (5, 10, 30 kDa MWCO) system according to the molecular weights. The active components were mainly concentrated in >30 kD fraction which are composed of the highest protein content $(27\%)$ and phenolic content (261 mg/100 mL) compared to the other two smaller molecular weight fractions. Therefore, the active compounds appear to be relatively high molecular weight complex molecules associated with protein (glycoprotein) and polyphenols. Therefore, E. cave is a potential source of antihypertensive compound.

Antihypertensive peptides from whey proteins fermented by lactic acid bacteria

  • Daliri, Eric Banan-Mwine;Lee, Byong H.;Park, Byun-Jae;Kim, Se-Hun;Oh, Deog-Hwan
    • Food Science and Biotechnology
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    • v.27 no.6
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    • pp.1781-1789
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    • 2018
  • In this study, whey proteins were fermented with 34 lactic acid bacteria for 48 h at $37^{\circ}C$ and their ability to inhibit angiotensin 1-converting enzyme (ACE) activity were compared. All the lactic acid bacteria displayed varying proteolytic abilities in whey. Their fermentates also displayed varying abilities to inhibit ACE in vitro. Seven fermentates showed strong ACE inhibitory abilities between $84.70{\pm}0.67$ and $52.40{\pm}2.1%$ with $IC_{50}$ values between $19.78{\pm}1.73$ and $2.13{\pm}0.7mg/ml$. Pediococcus acidilactici SDL1414 showed the strongest ACE inhibitory activity of $84.7{\pm}0.67%$ ($IC_{50}=19.78{\pm}1.73{\mu}g/ml$). Mass spectrometry revealed that more than half (57.7%) of the low molecular weight peptides (< 7 kDa) in the P. acidilactici SDL1414 fermented samples were ACE inhibitory peptides. Our results show that P. acidilactici SDL1414 could be used as a starter culture in the dairy industry to develop antihypertensive functional foods for hypertension management.

ACE inhibitory activity of Peptide from krill(Euphausia superba) Hydrolysate

  • Kim, Dong-Soo;Kim, Young-Myoung;Park, Douck-Choun;Do, Jeong-Ryong
    • Proceedings of the Korean Society of Fisheries Technology Conference
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    • 2001.10a
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    • pp.183-184
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    • 2001
  • Angiotensin I converting enzyme (ACE) in renin-angiotensin system is a cause of essential hypertension, which covers most hypertension, one of the major adult diseases. Thus, the inhibition of ACE would be indispensable for the prevention and cure of hypertension. Therefore, a lot of studies on the ACE inhibitor have been conducted. Peptides from the protein hydrolysate have been reported as an remarkable inhibitor. Especially, various ACE inhibitory peptides were isolated and identified from marine products for their utilization as value added products. (omitted)

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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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    • v.5 no.2
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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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Improving the Functional Properties of Oyster Hydrolysates by Two-step Enzymatic Hydrolysis (2단 가수분해에 의한 굴 가수분해물의 기능성 개선)

  • Chung In-Kwon;Kim Jin-Soo;Heu Min-Soo
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.39 no.3
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    • pp.269-277
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    • 2006
  • This study prepared functional oyster hydrolysates using two-step enzymatic hydrolysis and investigated their functional properties. To prepare two-step enzymatic hydrolysates (TSEH), oysters were hydrolyzed using 1% Protamex (PR) at $40^{\circ}C$ and pH 6.0 for 1 hr before sequential treatment with one of the following enzymes for 1 hr: Alcalase (AL), Flavourzyme (FL), Neutrase (NE), pepsin (PE), and trypsin (TR). The PRAL, PRNE and PRTR hydrolysates had significantly greater angiotensin I converting enzyme (ACE) inhibitory activity than did PR and the other TSEHs. Only the antioxidant activity of the PRNE hydrolysate was significantly different (p<0.05), while none of the TSEHs had antimicrobial activity. The oyster hydrolysate prepared by sequential treatment with Protamex and Neutrase (PRNE) had the best ACE inhibitory activity and antioxidant activity, with $IC_{50}$ values of 0.40 and 0.94 mg/mL, respectively. The PRNE hydrolysate was processed through an ultrafiltration (UF) series with molecular weight cut-off (MWCO) membranes of 3, 5, 10, and 30 kDa, and the ACE inhibitory, antioxidant, and antimicrobial activities of the permeates were determined. The permeate through the 3-kDa MWCO membrane had greater ACE inhibitory activity and antioxidant activity than did the other PRNE permeates, with $IC_{50}$ values of 0.11 and 0.40 mg/mL, respectively.

Angiotensin I Converting Enzyme Inhibitory Effect of Doenjang Fermented by B. subtilis SCB-3 Isolated from JeJu, Korean Traditional Food (메주 유래의 B. subtilis SCB-3으로 제조된 된장의 Angiotensin I Converting Enzyme 저해효과)

  • 황종현
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.26 no.5
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    • pp.775-783
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    • 1997
  • Morphologically different 18 strains were isolated and examined for their abilities to inhibit ACE. Those strains were cultured in the medium containing 10% of soybean extract at 37$^{\circ}C$ for 48hr or fermented with boiled soybean at 3$0^{\circ}C$ for 60 days. The concentration of inhibitors to inhibit 50% of ACE activity, $IC_{50}$ was measured on the culture broth of each strain and also on the hot-water extract from 20, 40 and 60 day fermented Doenjang by each strain. As a result, SCB-3 which is isolated from Meju showed the highest ACE inhibitoryactivity on the cultured broth and 40 day matured Doenjang. Then, $IC_{50}$ of SCB-3 was 0.02 mg/ml and 0.26mg/ml respectively. SCB-3 was identified as a Bacillus subtilis based upon its morphological, biochemical and physiological properties. Changes in general components and ACE inhibitory activity of Doenjang fermented by SCB-3 were examined during 90 days. Total acidity of Doenjang was increased from 1.39% to 1.66% and pH was decreased from 6.02 to 5.79 after 90 days fermentation. Total sugar contents were decreased from 16.4% to 15.1% and reducing sugar contents was also decreased from 2.45% to 1.62%. Total nitrogen contents were nearly not changed, but amino nitrogen contents were drastically increased from 196mg% to 541mg%. The numbers of total microorganism were increased to 1.1$\times$$10^{8}$ cells/g after 45 days. Protease activity was increased to 622.1U/g after 75 days. The highest ACE inhibitory activity was shown in 60 day fermented Doenjang and $IC_{50}$ of the hot-water extract was 0.31mg/ml.

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

  • 차명화;박정륭
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.30 no.4
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    • pp.594-599
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    • 2001
  • This study was attempted to isolate and identify the strain revealing high angiotensin converting enzyme (ACE) inhibitory activity from various soy fermented foods, i.e. meju, soybean paste and soy sauce. Forty-two strains with morphologically different characteristics were selected and the ACE inhibitory and proteolytic activities were examined. Of the strains tested, SS103 which was isolated from soy sauce showed the highest ACE inhibitory and proteolytic activities and was finally selected for further studies. The SS103 strain showed motility, rod form and ellipsoidal spores. The shape of colonies on the agar media was irregular, mucoidal and surface dull. The strain could grow under aerobic conditions of pH 5~9 and 10~$50^{\circ}C$. Main cellular fatty acid was $C_{15:0}$ anteiso, $C_{17:0}$ cis and $C_{17:0}$ iso, which was 33.9%, 18.8% and 16.5%, respectively. Based upon these morphological, biochemical and cultural properties, SS103 was identified as a Bacillus subtilis. Optimum cultural condition of Bacillus subtilis SS103 was pH 8.0, $37^{\circ}C$ and 48 hr.48 hr.

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