• Title/Summary/Keyword: ACE-inhibitory activity

Search Result 377, Processing Time 0.031 seconds

Antioxidative activity, including Inhibitory activities of ACE, APN and $\alpha$-amylase, in Theaceae Plants Native to Jeju Island (제주도 자생 차나무과 식물의 ACE, APN, $\alpha$-amylase 저해 활성 및 항산화활성에 대한 연구)

  • Oh, Soon-Ja;Lee, Jin-Ho;Ko, Kwang-Sup;Shin, Dong-Bum;Koh, Seok-Chan
    • Korean Journal of Plant Resources
    • /
    • v.23 no.5
    • /
    • pp.406-414
    • /
    • 2010
  • Antioxidative activity, including inhibitory activities of angiotensin I converting enzyme(ACE), aminopeptidase N(APN) and $\alpha$-amylase, was investigated in the methanol extracts from Theaceae plants native to Jeju island, in order to select the plant species containing bioactive materials for functional food or medicines. ACE inhibitory activity was above 50% in Ternstroemia japonica(stem bark) and Cleyera japonica(leaf), and APN inhibitory activity was low to be positive only in C. japonica(leaf, stem bark) and T. japonica(stem bark). $\alpha$-Amylase inhibitory activity was above 30% in Camellia japonica(fruit), Eurya emarginata(stem), T. japonica(stem bark) and Thea sinensis(stem). The antioxidative activity, estimated by the DPPH radical scavenging capacity, was above 30% in C. japonica(stem bark), T. japonica(stem bark) and T. sinensis(leaf). Particularly, the antioxidative activity analyzed by dot-blot test was very high in C. japonica(stem bark) relatively to those of other plants, and remained high in the low concentration($1.25\;{\mu}g/m{\ell}$). From the TLC analysis of antioxidative compounds, EGC(Rf 0.26) was found to have high activity in stem bark of C. japonica and EGCG(Rf 0.09) was found to have high activity in stem bark of C. japonica, E. emarginata, and T. japonica. Five bands (Rf 0.54, 0.46,0.44, 0.16, 0.03) which were not identified as compared with catechins were detected as polyphenolic compounds on the TLC plates sprayed with the Folin-Ciocalteu solution or the Ferric chloride-alcohol solution. These results suggests that Theaceae plants except E. japonica could be potentially used as a resource of bioactive materials for functional foods or medicines and further research is reguired to identify the bioactive substances and determine the functions of them.

Isolation and Charaterization of Bioactive Peptides from Hwangtae (yellowish dried Alaska pollack) Protein Hydrolysate

  • Cho, San-Soon;Lee, Hyo-Ku;Yu, Chang-Yeon;Kim, Myong-Jo;Seong, Eun-Soo;Ghimire, Bimal Kumar;Son, Eun-Hwa;Choung, Myoung-Gun;Lim, Jung-Dae
    • Preventive Nutrition and Food Science
    • /
    • v.13 no.3
    • /
    • pp.196-203
    • /
    • 2008
  • Hwangtae, dried Alaska pollack, is a major storage product in the fish processing industry. Hwangtae is prepared by removing the internal organs and drying outdoors during the cold witner months by allowing it to thaw during the daytime and re-freeze at night under sub-zero ($-10^{\circ}C$) conditions and gradually dry from December until the next April for around 5 months from Myungtae. In this study, ground Hwangtae was hydrolyzed using two proteolytic enzymes (pepsin and alcalase) which produced five soluble active peptides from Hwangtae (yellowish dried Pollack, Theragra chalcogramma) protein. Two different peptides with strong antioxidative activity were isolated from the hydrolysate using consecutive chromatographic methods of Sephadex G-25 gel, ion-exchange chromatography on a Sepharose-Sephadex C-25 gel, and high-performance liquid chromatography. The isolated peptides, APO1 and APO2, were composed of 16 and 13 amino acid residues, respectively. Both peptides contained a Gly residue at the C-terminus and the repeating motif Gly-Pro-Hyp. The peptide with a molecular weight less than 1,000 Daltons (APACE) obtained from enzymatic hydrolysates of Hwangtae exhibited the highest ACE inhibitory activity. The APACE peptides was composed of 4 amino acid residues (Gly-Leu-Leu-Pro). These results suggest that Hwangtae hydrolysates could be a good source of peptides with ACE inhibitory activity. Biochemical analysis indicated that two 70 kDa peptides (APG1 and APG2) isolated from the hydrolysate had gelatinoytic activity, which was shown to be a calcium dependent protease type as showed by gelatin SDS PAGE.

Changes in Glucosinolate Content of Dolsan Leaf Mustard Kimchi during Fermentation and Correlation with Antioxidant, Antihypertensive, and Antidiabetic Activities (발효기간에 따른 돌산갓김치의 glucosinolates 함량변화와 항산화, 항고혈압 및 항당뇨활성과의 상관관계)

  • Oh, Sun-Kyung;Kim, Ki-Woong;Choi, Myeong-Rak
    • Journal of Life Science
    • /
    • v.28 no.11
    • /
    • pp.1290-1300
    • /
    • 2018
  • The glucosinolate content, antioxidant activity, and antihypertensive and antidiabetic activities were measured in a crude extract of Dolsan leaf mustard kimchi (DLMK). The glucosinolate content was low at 6.41 and 7.92 mg/g in leaves and stems of DLMK after 21 days of fermentation. The total polyphenol and total flavonoid contents were more than 2 times higher in the leaves (211.7 mg GAE/g, 158.8 mg QE/g) than in the stem (53.7 mg GAE/g, 85.2 mg QE/g) during the fermentation period. The 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) radical scavenging activity and electron donating ability (EDA) were similar to those of the control group after 14 days of fermentation, while the ferric reducing antioxidant power (FRAP) was higher in the leaves after 14 days of fermentation when compared to the control group. The angiotensin converting enzyme (ACE) inhibitory activity showed similar or higher inhibitory activity in the leaves when compared to the control group (0.01% captopril), and the ${\alpha}$-glucosidase inhibitory activity was higher in the leaves and stems when compared to the control group (0.05% acarbose). The glucosinolate content and the ABTS, ACE, and ${\alpha}$-glucosidase inhibitory activity were correlated, as determined by the observed straight line plot with a positive grade. During the fermentation period, the detected glucosinolates were sinigrin, glucobrasicin, glucotropeolin, and progoitrin. The DLMK extract is therefore expected to be valuable as a functional food because of its effective antioxidant, antihypertensive, and antidiabetic activities.

Screening of Mushrooms Having Angiotensin I-Converting Enzyme Inhibitor (각종 버섯류로부터 안지오텐신 전환효소 저해제의 탐색)

  • Lee, Dae-Hyoung;Kim, Jae-Ho;Cheong, Jong-Chun;Gong, Won-Shik;Yoo, Young-Bok;Park, Jeong-Sik;Yoo, Chang-Hyun;Lee, Jong-Soo
    • The Korean Journal of Mycology
    • /
    • v.31 no.3
    • /
    • pp.148-154
    • /
    • 2003
  • Extracts from 52 samples of mushrooms were prepared by using water, ethanol and methanol, and then yields and angiotensin I-converting enzyme(ACE) inhibitory activity were investigated. Sample mushrooms contained crude proteins of $7.1{\sim}56.5%$, curde lipids of $0.2{\sim}4.4%$ and carbohydrates of $30.3{\sim}86.6%$. Among 52 samples, the water extract from fruiting body of Pholiota spp. ASI 24027 showed the highest extraction yield of 68%. Water extract of Pholiota spp. ASI 24012 fruiting body had potential ACE inhibitory activity of 66%. The optimal extraction condition of the ACE inhibitor from the fruiting bodyies of Pholiota spp. ASI 24012 was In water at $30^{\circ}C$ for 1 hr and ACE inhibitory activity was 67.6% on the condition with 0.2 mg of $IC_{50}$.

The Biological Activity of Deer Antler Extract in vitro (In vitro에 의한 녹용 추출물의 생리 활성 효과)

  • Lee, Kyung-Ae;Chung, Hae-Young
    • The Korean Journal of Food And Nutrition
    • /
    • v.20 no.2
    • /
    • pp.114-119
    • /
    • 2007
  • Our research objective was to examine the in vitro biological activity of deer antler(Nogyong in Korean) extract, including the antioxidative, nitrite scavenging, and tyrosinase inhibitory effects, as well as the antithrombotic, and angiotensin I converting enzyme(ACE) inhibitory activities. The carbohydrate, protein, fat, and mineral contents of the deer antler were 7.6%, 65.3%, 3.2% and 23.9%, respectively. The electron donating ability(EDA) by the reduction of 2,2'-diphenyl-1-picrylhydrazyl(DPPH) was 67.1%, and the inhibition rate of lipid peroxidation by the thiocyanate method using linoleic acid was 92.1% in 100 mg/ml of extract. The nitrite scavenging effects were pH dependent, and were highest at pH 1.2 and lowest at pH 6.0. The sample inhibition rate against tyrosinase was above 64.0%. The platelet aggregation induced by ADP(adenosine-5'diphosphate) was inhibited up to 51.7%, and the inhibitory effect was dependent on the sample concentration. Lastly, the inhibition rate of ACE was 47.5% in 100 mg/ml of deer antler extract.

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
    • /
    • v.25 no.3
    • /
    • pp.229-235
    • /
    • 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.

  • PDF

Separation and Purification of Angiotensin I-converting Enzyme Inhibitory peptide from Mackerel (고등어 유래 항고혈압 peptide의 분리 정제)

  • DO Jeong-Ryong
    • Korean Journal of Fisheries and Aquatic Sciences
    • /
    • v.33 no.2
    • /
    • pp.153-157
    • /
    • 2000
  • Hydrolysate which inhibit the Angiotensin I-converting enzyme (ACE) was prepared from mackerel muscle by pretense. The ACE inhibitory activity of mackerel muscle hvdrolysate (MMH) was $967 {\mu}g of IC_(50)$. ACE inhibitory peptides were isolated by ultrafiltration, gel permeation column chromatography (GPC), reversed phase column chromatography(RPC), reversed phasehigh performance liquid chromatography (RP-HPLC), and gel permeation high performance liquid chromatography (GP-HPLC) from the MMH. The amino acid sequence of the ACE inhibitory peptides was Tyr-Val-Ala. The $IC_(50)$ of this peptide for ACE from rabbit lung was $1.4 {\mu}M$.

  • PDF

Nitrite Scavenging and Alcohol Metabolizing Activities of Hot Water Extract from Makgeoly and Its Angiotensin Converting Enzyme Inhibitory Effect (막걸리 열수 추출물의 아질산염 소거능, 알코올 분해능 및 angiotensin converting enzyme 저해 효과)

  • Cho, Eun-Kyung;Kim, Hee-Yeon;Byeon, Hyeon-Ji;Kim, Soo-Won;Choi, Young-Ju
    • Journal of Life Science
    • /
    • v.20 no.5
    • /
    • pp.768-774
    • /
    • 2010
  • In this study, we investigated the antioxidant activities, alcohol metabolizing activities, nitrite scavenging ability, angiotensin converting enzyme (ACE), and elastase inhibitory effects of hot water extract from Makgeoly (HWM). Antioxidant activities were measured by using 2,2.diphenyl.1.picryl.hydrazyl (DPPH) free radical scavenging activity and SOD (superoxide dismutase).like activity. The DPPH radical scavenging activity and SOD.like activity of HWM were remarkably increased in a dose.dependent manner and were 48.0% and 98.7% at 10 mg/ml, respectively. To determine the influence of HWM on alcohol metabolizing activity, the generating activities of reduced.nicotinamide adenine dinucleotide (NADH) by alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) were measured. The facilitating rates of ADH and ALDH activity by HWM were remarkably increased in a dose.dependent manner and were 70.2% and 64.1% at 10 mg/ml, respectively. The inhibitory activity against angiotensin converting enzyme (ACE) of HWM was increased in a dose.dependent manner and was 74.2% at 10 mg/ml. The nitrite scavenging ability of HWM showed the most remarkable effect at pH 1.2 and 2 mg/ml. These results indicated that HWM may have valuable biological properties owing to their antioxidant activities, ADH and ALDH activity, nitrite scavenging ability, and ACE inhibitory activity.

Angiotensin Converting Enzyme Inhibitory Activity in Peptic Hydrolysates of Cooking Discards from Anchovy Factory Ship (멸치 가공선 자숙폐액 Pepsin 가수분해물의 Angiotensin 전환효소 저해작용)

  • Ji, Cheong-Il;Lee, Ji-Hye;Park, Douck-Choun;Gu, Yeun-Suk;Kim, In-Soo;Lee, Tae-Gee;Jung, Kyoo-Jin;Park, Yeung-Ho;Kim, Seon-Bong
    • Korean Journal of Food Science and Technology
    • /
    • v.34 no.3
    • /
    • pp.529-532
    • /
    • 2002
  • The angiotensin converting enzyme (ACE) inhibitory activity in peptic hydrolysate of raw anchovy cooking discards was 51.3% at 1 mg of protein per $100\;{\mu}L$ sample solution. While, after the treatment of pepsin for 4 h, was 65.8%. The crude peptides fractionated through Bio-gel P-2 column chromatography consisted of five fractions $({P-1}{\sim}{P-5})$ and had maximum inhibitory activity in the fraction P-2 ($IC_{50}$=0.319 mg protein/mL). The fraction P-2 was rich in aspartic acid, glutamic acid, and glycine.