• Title/Summary/Keyword: Angiotensin I converting enzyme (ACE)

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Screening of Lactic Acid Bacteria as Starter Culture for Making Fermented Sausage (발효 소시지 제조를 위한 기능성 유산균의 선발)

  • Han, Soo-Min;Kim, Young-Joo;Lee, Hong-Chul;Chin, Koo-Bok;Oh, Se-Jong
    • Food Science of Animal Resources
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    • v.26 no.4
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    • pp.511-516
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    • 2006
  • The objectives of this study was to compare the probiotic characteristics of lactic acid bacteria (LAB) for their ability to assimilate cholesterol, production of bacteriocin, inhibition of angiotensin I-converting enzyme (ACE), and viability under artificial gastrointestinal fluids. Among tested lactic acid bacteria, L167 strain exhibited the highest ACE inhibitory activity (58.75%). The production of ACE inhibitory peptide derived from fermented milk by L167 strain started at the beginning of stationary phase with maximum activity occurring late of the stationary phase. The highest ACE inhibitory activity was observed at 20 h in 10% skim milk medium. L155 strain exhibited cholesterol assimilation activity compared with probiotic strains such as Lactobacillus acidophilus ATCC 43121. With addition of bacteriocin culture, viable cells of Staphylococcus aureus in fermented sausage were slightly decreased during storage. Among selected strains of LAB, 3 strains weve identified as L. plantarum (L155, L165, L167), and two strains were identified as Pediococcus damnosus (L12) and L. paracasei ssp. paracasei (P113) by use of API carbohydrate fermentation pattern and physiological tests.

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 Characteristics of Angiotensin-I Converting Enzyme Inhibitory Activity of Peptic Hydrolyzates of Anchovy Muscle Protein (멸치육 단백질 효소가수분해물로부터 Angiotensin-I 전환효소 저해제의 분리 및 그 특성)

  • KIM Seon-Bong;LEE Tae-Gee;PARK Yeung-Beom;YEUM Dong-Min;KIM Oi-Kyung;DO Jeong-Ryong;PARK Young-Ho
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.27 no.1
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    • pp.1-6
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    • 1994
  • Hydrolyzates which inhibit the angiotensin-I converting enzyme(ACE) were prepared from defatted anchovy meal by pepsin. These were tested for inhibitory activity against ACE, which is one of the hypertension inducing factors. The ACE inhibitory activity of the hydrolyzates increased until 20hrs of hydrolysis had elapsed but slightly decreased after that time. And presence of $50\%$ ethanol soluble peptide-nitrogen increased slowly up to 12hrs of hydrolysis, and then mainly increased until 20hrs of hydrolysis was completed. From the profiles of gel permeation chromatography on a Bio-gel P-2 of $50\%$ ethanol soluble fraction obtained from hydrolyzate for 20hrs, the higher active fractions were 2'($IC_{50}=45\;{\mu}g\;protein/ml$) and 4'($IC_{50}=76\;{\mu}g\;protein/ml$). Amino acid analysis showed major quantities of glutamic acid, leucine, lysine for 2'and aspartic acid, threonine for 4' respectively.

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Angiotensin-I Converting Enzyme Inhibitory Activity of Enzymatic Hydrolysates of Mackerel Muscle Protein (효소에 의한 고등어 근육단백질 가수분해물의 Angiotensin-I 전환효소 저해작용)

  • YEUM Dong-Min;LEE Tae-Gee;BYUN Han-Seok;KIM Seon-Bong;PARK Yeung-Ho
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.25 no.3
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    • pp.229-235
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    • 1992
  • Fish protein hydrolysates(FPH) prepared from defatted mackerel meal by proteases such as complex enzymes, bromelain, alcalase, $\alpha-chymotrypsin,$ trypsin, papain and pepsin were tested for inhibitory activity against angiotensin-I converting enzyme(ACE). Among proteases tested, the hydrolysates obtained from the treatment of complex enzymes or bromelain showed relatively higher activity. ACE inhibitory activity of the hydrolysates increased until hydrolysis of 8 hrs, and was stable by heat treatment for 20min at $100^{\circ}C.$ From the profiles of fractionation of the hydrolysates with Bio-gel P-2, the most active fraction had about MW 1,450 and it's amino acid was abundant in Asp, Glu, Lys, Leu, Val and Ala. $IC_{50}\;(amounts\;of\;inhibitors\;needed\;for\;50\%\;inhibition)$ of the active fraction of the hydrolysates obtained from the treatment of complex enzyme and bromelain was 90 and $130 {\mu}g,$ respectively.

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Antidiabetes and Angiotensin Converting Enzyme Inhibitory Activity of Sonchus asper (L) Hill Extract (큰방가지똥 추출물의 항당뇨 및 항고혈압효과)

  • Xu, Ming-Lu;Wang, Lan;Xu, Gui-Fang;Wang, Myeong-Hyeon
    • Korean Journal of Pharmacognosy
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    • v.42 no.1
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    • pp.61-67
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    • 2011
  • In this study, we evaluated the bioactivities of methanol extract and its solvent fractions of Sonchus asper (L.) Hill. The EtOAc fraction of S. asper exhibited more strong antioxidant activity than other extracts as evidenced by the strongest 1,1-diphenyl-2-picryl hydrazyl (DPPH) radical scavenging activity with a $EC_{50}$ value at $33.55\;{\mu}g/mL$ and reducing power, the total polyphenol (180.71 mg GAE/g) and flavonoid contents (145.86 mg QE/g) of S. asper extract were higher than other extracts. The EtOAc fraction of the S. asper also showed 47.38% mushroom tyrosinase inhibition activity, 56.22% ${\alpha}$-glucosidase inhibition and 46.58% ${\alpha}$-amylase inhibition ratio at 1 mg/mL. Both methylene chloride and EtOAc fractions of methanol extract of S. asper effectively reduced of the 86.34% and 62.03% angiotensin I converting enzyme (ACE) activity at 2 mg/mL, respectively. These findings suggest that the EtOAc fraction of the S. asper could be a potential antioxidant in food additive, medicinal, and industry product.

ACE Inhibitory Lignan Glycosides Isolated from Eucommia ulmoides Oliver (두충으로부터 분리한 Iignan glycoside 의 ACE 활성 억제)

  • Joo, Ok-Soo;Nam, Sang-Hae
    • Journal of Life Science
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    • v.19 no.6
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    • pp.698-704
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    • 2009
  • To evaluate a potential possibility of Eucommia ulmoides Oliver as a functional food, ACE (angiotensin converting enzyme) inhibitory activities of leaf, bark, stem and 4 compounds isolated from E. ulmoides were tested. The 4 compounds were isolated and purified by silica gel column chromatography, thin layer chromatography and reverse phase column chromatography. Compound I was pinoresinol-4,4'di-O-${\beta}$-D-glucoside (PG) and compound II was dehydrodiconiferyl alcohol 4,${\gamma}$'-di-O-${\beta}$-D-glucopyranoside (DAG) originating from Eucommial Cortex. The highest amount of PC was present at raw and roasted bark as 135.13 mg% and 163.67 mg%, and the highest amount of DAG was present at raw and roasted leaf as 117.93 mg% and 133.93 mg% respectively. In an ACE inhibition test, 10 mg/ml of roasted leaf, raw and roasted bark extracts of E. ulmoides Oliver were 77.49%, 75.72% and 75.36% respectively, and 10mg/ml of PC and DAG were shown to be 78.51 and 81.20% respectively. $IC_{50}$ values of PG and DAG were 0.6${\pm}$0.2 and 0.5${\pm}$0.2 mg/ml respectively.

Antioxidant and Angiotensin Converting Enzyme I Inhibitory Activity on Different Parts of Germinated Rough Rice (발아 벼 부위별 추출물의 항산화활성과 Angiotensin Converting Enzyme I 저해활성)

  • Kim, Hyun-Young;Hwang, In-Guk;Kim, Tae-Myoung;Park, Dong-Sik;Kim, Jae-Hyun;Kim, Dae-Joong;Lee, Jun-Soo;Jeong, Heon-Sang
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.40 no.6
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    • pp.775-780
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    • 2011
  • We investigated the changes in antioxidant and angiotensin converting enzyme I (ACE) inhibitory activity in different parts of 'Ilpum' (Oryza sativa L.) rough rice before and after germination. Rough rice, either before or after germination, were separated into hull, brown rice, or sprout, and then extracted with distilled water and 70% ethanol. After germination, the total polyphenol contents of the distilled water extract of the brown rice was higher than before germination (5.84 and 1.67 mg/g, respectively). The DPPH radical scavenging activity on the unseparated rough rice ethanol extract increased from 22.95% before germination to 31.32% after germination, but it decreased in both the hull and brown rice extracts. The ABTS radical scavenging activity was highest in the sprout extract with a value of 4.41 mg AA eq/g. The reducing power of the brown rice ethanol extract increased from 0.32 before germination to 0.45 after germination. The ACE inhibitory activity of the in hull ethanol extract increased after germination. These results indicate that antioxidant capacity increases in the hull and sprout after germination could be considered having significant health benefits.

Antioxidant Activity, Fibrinolysis and Angiotensin I Converting Enzyme Inhibitory Activity of Pine Mushroom Juice (Tricholoma matsutake Sing) (송이즙의 항산화 활성, 혈전용해활성 및 Angiotensin I Converting Enzyme의 저해활성 검색)

  • Kim, Young-Eon;Kwon, Eun-Kyung;Han, Dae-Seok;Kim, In-Ho;Ku, Kyung-Hyung
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.37 no.5
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    • pp.535-541
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    • 2008
  • Pine mushroom (Tricholoma matsutake Sing.) is an expensive and highly prized delicacy in Korean and Japanese cuisines with its unique flavor and functional properties. The biological activities of pine mushroom juice (soluble solid contents $4.3^{\circ}$Brix) were evaluated using different tests; DPPH radical scavenging assay for its antioxidant activity, fibrin plate method for fibrinolysis and angiotensin I converting enzyme (ACE) inhibitory activity for anti-hypertensive effect. Free radical scavenging activity of the pine mushroom juice was $48.3{\pm}2.2%$ at the concentration of 1.0 mg/mL. The fibrinolytic activity of pine mushroom was about 2 times greater than that of plasmin used as positive control and the activity increased dose-dependently. The pine mushroom juice inhibited ACE activities dose-dependently and $IC_{50}$ value of ACE activity was $1.03^{\circ}$Brix. These results suggest that pine mushroom is a healthy delicacy.

Characteristics of Angiotensin-I Converting Enzyme Inhibitors Derived from Fermented Fish Product -2. Characteristics of Angiotensin-I Converting Enzyme Inhibitors of Fish Sauce Prepared from Sardine, Sardinops melanosticta- (수산발효식품 중의 Angiotensin-I 전환효소 저해제의 특성 -2. 정어리 어간장 중의 Angiotensin-I 전환효소 저해제의 특성-)

  • YEUM Dong-Min;LEE Tae-Gee;DO Jeong-Ryong;KIM Oi-Kyung;PARK Young-Beom;KIM Seon-Bong;PARK Young-Ho
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.26 no.5
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    • pp.416-423
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    • 1993
  • Fish sauces prepared from sardine, Sardinops melanosticta were tested for inhibitory activity against angiotensin-I converting enzyme(ACE). Three kinds of fish sauces were prepared from scrap(S), meat(M) and round(R) of sardine, respectively. ACE inhibitory activity of sardine sauce S and R decreased with the elapse of fermentation period, whereas that of sardine sauce M increased to 30 days and thereafter decreased. ACE inhibitory activity of sardine sauce M fermented with koji was higher than that without koji. And occurrence of $5\%$ TCA soluble peptide-nitrogen was similar to tendancy of the ACE inhibitory activity. The ACE inhibitory activity increased with an increment of amounts added and was stable at heat treatment in boiling water bath for 5hrs. $IC_{50}\%$ (Amounts of inhibitors need for $50\%$ inhibition) of the sardine sauce S, M and R fermented with(without) koji during 90 days was $125{\mu}g(140{\mu}g),\;200{\mu}g(100{\mu}g)$ and $125{\mu}g(135{\mu}g)$, respectively. From the profiles of fractionation of the sardine sauce R fermented without koji for 90 days, the molecular weight of most active fraction was about 1,400 and the amino acids of Glu, Ala, Leu and Lys were found in abundance.

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Effect of Sodium Caseinate Hydrolysates on Angiotensin-I Converting Enzyme Inhibition Activity (Sodium Caseinate 가수분해물의 Angiotensin-I Converting Enzyme 저해효과에 관한 연구)

  • Lee, Keon-Bong;Shin, Yong-Kook;Baick, Seung-Chun
    • Food Science of Animal Resources
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    • v.32 no.5
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    • pp.652-658
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    • 2012
  • This study was carried out to identify the ACE (Angiotensin converting enzyme) inhibitory activity of casein hydrolysates for development of anti-hypertensive hydrolysates. Sodium caseinate was treated with six kinds of commercial proteases such as Flavourzyme, Protamex, Neutrase 1.5, Alcalase, Protease M, and Protease S for 8 h individually, and was then treated with the enzyme combination for 4 h at $45^{\circ}C$. The hydrolysate which had the highest ACE inhibitory effect was then hydrolysed successively with three digestive enzymes: pepsin, trypsin, and ${\alpha}$-chymotrypsin, at $37^{\circ}C$ for 4 h under conditions mimicking those of the gastrointestinal tract. UF (ultra filtration) treatment was applied to one of the secondary hydrolysates to determine ACE inhibitory activity. When sodium caseinate was hydrolysed by commercial proteases, the degree of hydrolysis (DH) showed 2.54 to 4.25% and after secondary hydrolysis, DH showed 4.30 to 5.22%. ACE inhibitory activity and $IC_{50}$ values decreased, and inhibition rates increased during hydrolysis. Protamex treatment showed the lowest $IC_{50}$ value ($516{\mu}g/mL$) and Flavourzyme hydrolysate showed the highest $IC_{50}$value ($866{\mu}g/mL$). As the first hydrolysate was treated with Flavourzyme, the ACE inhibitory activity increased. Neutrase hydrolysate had the highest activity with an $IC_{50}$ value ($282{\mu}g/mL$). When Neutrase plus Flavourzyme treatment was hydrolyzed by digestive enzymes, the $IC_{50}$ value ($597{\mu}g/mL$) was decreased statistically (p<0.05). As Neutrase plus Flavourzyme hydrolysate is treated by UF with MW cut-off 10,000, permeate showed $273{\mu}g/mL$ of $IC_{50}$ value, showed no difference, but retentate which has over MW 10,000 showed statistically different $IC_{50}$ value, $635{\mu}g/mL$ (p<0.05).