• Title/Summary/Keyword: Fibrinolytic activity

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The Antithrombotic and Fibrinolytic Effect of Natto in Hypercholesterolemia Rats

  • Park, Kum-Ju;Kang, Jung-Il;Kim, Tae-Seok;Yeo, Ik-Hyun
    • Preventive Nutrition and Food Science
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    • v.17 no.1
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    • pp.78-82
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    • 2012
  • Antithrombotic and fibrinolytic activity of natto was evaluated on platelet aggregation in vitro and in vivo. Natto showed inhibitory effects on platelet aggregation induced by adenosine 5’diphosphate (ADP) and collagen. Orally administered natto also showed fibrinolytic activity in hypercholesterolemia rats. Normal levels of natto, when administered for four weeks, shortened euglobulin clot lysis time (ECLT) and prolonged partial thromboplastin time (PATT) significantly compared to non-treated group. In addition, the natto treatment decreased total cholesterol in serum. These results showed that intake of normal levels of natto can elicit antithrombotic and fibrinolytic effects, suggesting its consumption may improve blood circulation.

Purification and Characterization of Fibrinolytic Enzyme Excreted by Bacillus subtilis K-54 Isolated from Chung Guk Jang. (청국장에서 분리한 Bacillus subtilis K-54가 분비하는 혈전용해효소의 정제 및 특성)

  • 유천권;서원상;이철수;강상모
    • Microbiology and Biotechnology Letters
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    • v.26 no.6
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    • pp.507-514
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    • 1998
  • The strain K-54, the best producer of fibrinolytic enzyme, was isolated from Korean traditional food Chung Guk Jang and identified as Bacillus subtilis. Fibrinolytic enzyme was purified and characterized, and its molecular weight was determined. The fibrinolytic enzyme activity was increased about 66.9 times via purification with recovery yield of 10.1%. The optimum pH and temperature of this enzyme were 11 and $65^{\circ}C$. The enzyme was stable within a pH range 8-12 and unstable at 9$0^{\circ}C$. The molecular weight was estimated to be 29,000 dalton in the form of monomer with no other subunit. The isoelectric point was calculated 8.67. N-terminal sequence was identified Ala-Gly-Ser-Val-Pro-Try-Gly-Ser. Km value of the enzyme for $\alpha$-casein was calculated to be 0.31 (3.1 mg/$m\ell$). The enzyme activity highly inhibited by PMSF at 1 nM.

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Purification and Biochemical Characterization of a Serine Protease with Fibrinolytic Activity from Maggots of Mimela splendems

  • Kwon Heun Young;Kim Tae Un
    • Biomedical Science Letters
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    • v.10 no.4
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    • pp.347-351
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    • 2004
  • Maggot fibrolase (MsMg-1) was purified from the maggots of Mimela splendems using ammonium sulfate fractionation, DEAE Affi-gel affinity chromatography. This protease had a molecular weight of 85 kDa as determined by SDS-polyacrylarnide gel electrophoresis under reducing conditions. It showed strong proteolytic and fibrinolytic activities. The purified enzyme was strongly inhibited by phenylmethanesulfonyl fluoride, Mn/sup 2+/, and Zn/sup 2+/ but it was not by EDTA, EGT, Mg/sup 2+/, Ca/sup 2+/, and Li/sup 2+/ ions. In these experimental results, we have speculated that MsMg-1 is a serine protease with a strong fibrinolytic activity.

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Biological activities of Solvent Fractions Isolated from Areca catechu L

  • Kim, Jun-Ho;Oh, Hae-Sook
    • Biomedical Science Letters
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    • v.16 no.4
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    • pp.271-277
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    • 2010
  • This study was conducted to investigate the biological activities of Areca catechu L. The antioxidative, fibrinolytic, thrombin inhibitory, and ${\alpha}$-glucosidase inhibitory activities of Areca catechu L extracted with hexane, $CHCl_3$, ethyl acetate, butanol, and water were measured. The water fraction showed the highest extraction yield at 3.65% (w/w). The butanol, $CHCl_3$, water, and ethyl acetate fractions showed strong antioxidative activities at 81.6%, 87.1%, 88.0%, and 89.5%, respectively. The fibrinolytic activity was strong only in the ethyl acetate fraction at 0.84 plasmin units/ml. The 100-fold dilution of the water fraction had the strongest thrombin inhibitory activity at 59.2%. The 100-fold dilution of butanol fraction displayed the strongest ${\alpha}$-glucosidase inhibitory activity at 88.6%. In conclusion, the extracts of Areca catechu L hold promise for use in the development of biofunctional foods to prevent cardiovascular diseases.

Fibrinolytic Activity and Characterization of Bacillus licheniformis HK-12 Isolated from Chungkook-Jang (청국장에서 분리한 세균인 Bacillus licheniformis HK-12의 혈전용해활성 및 특징)

  • Sohn, Byung-Hee;Song, Yu-Jin;Oh, Kye-Heon
    • KSBB Journal
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    • v.23 no.3
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    • pp.251-256
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    • 2008
  • The aim of this work was to investigate the fibrinolytic activity and characterization of Bacillus licheniformis HK-12, which produces the fibrinolytic enzyme excreted from naturally fermented Chungkook-Jang. Initially, the physiological and biochemical characteristics of strain HK-12 was examined. Both physiological analysis using BIOLOG system and phylogenetic analysis using 16S rRNA sequencing were performed to identify the strain, and the strain could be assigned to Bacillus licheniformis, designated as B. lichenformis HK-12, and registered in GenBank as [EU288193]. Phylogenetic analysis of B. licheniformis HK-12 was plotted based on 16S rRNA sequence comparisons. During the incubation period of B. licheniformis HK-12, the changes of bacterial growth, fibrinolytic activity, and pH were monitored. As the results, after 36 hours of incubation, the maximum fibinolytic activity was about 2.25 times than that of plasmin used as standard. Optimal conditions on the growth of B. licheniformis HK-12 associated with the fibrinolytic activity was initial pH 7.0 and 40$^{\circ}C$, respectively.

Isolation and Charaterization of the Fibrinolytic Enzyme Producing Bacterium isolated from Naturally Fermented Chungkookjang (청국장에서 분리한 혈전용해효소 생산세균의 분리 및 동정)

  • Sohn Byung-Hee;Oh Kye-Heon
    • Journal of the Korea Academia-Industrial cooperation Society
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    • v.7 no.3
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    • pp.476-482
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    • 2006
  • The aim of this work was to perform the screening and identification of the bacterium, MK-15 having the activity of fibrinolytic enzyme for the commercial use. Initially, strain MK-15 was enriched and isolated from naturally fermented soybean. Morphological and various physiological characteristics of the strain MK-15 was examined. The activity of fibrinolytic enzyme derived from supernatants of test culture MK-15 was performed by fibrin plate method for solid fibrinolytic activity. As the result, the fibrinolytic activity of MK-15 grown on the soybean media was about 2.7 times greater than that of plasmin used as stardard. 16S rRNA analyses revealed that strain MK-15 was 99.9% similar to Bacillus subtilis species cluster, and the bacterium was designated as Bacillus sp. MK-15. Strain MK-15 was registered in GenBank as [DQ163021].

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Fibrinolysis of Fermented Kimchi (김치의 혈전용해작용)

  • Jeong, Yong-Kee;Yang, Woong-Suk;Kang, Jeong-Ok;Kong, In-Soo;Kim, Jeong-Ok
    • Journal of Life Science
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    • v.5 no.4
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    • pp.203-210
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    • 1995
  • Fibrinolytic activity of fermented kimchi and ingredients used for the preparation were assayed by measuring the lysis area on plasminogen-rich fibrin plate. Fermented kimchi and picked fish sauces from changlan, prwan, and anchovy showed the activity, and the activity of pickled fish sauces were high in the order of pickled changlan, picked anchovy(pickled mulchi), and pickled prawn. However, the activity of kimchi may not be attributed to pickled fish sauce because kimchi containing fish sauce did not possess activities were determined from the samples heated for 30min at 100$\circ$C. There was no changes in activities before and after heat treatment indicating the agents may be components other than protein. Since major changes occur during kimchi fermentation were increased sour taste due to production of organic acids such as lactic, citric, oxalic, and succinic acids, the authentic organic acids present were examined for fibrinolytic activities. The results indicates that the major component posses the activity is lactic acid.

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Characterization and Production of Thermostable and Acid-stable Extracellular Fibrinolytic Enzymes from Cordyceps militaris

  • Kim, Seon-Ah;Son, Hong-Joo;Kim, Keun-Ki;Park, Hyun-Chul;Lee, Sang-Mong;Cho, Byung-Wook;Kim, Yong-Gyun
    • International Journal of Industrial Entomology and Biomaterials
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    • v.22 no.2
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    • pp.83-93
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    • 2011
  • Biochemical and enzymatic characterization for extracellular protease isolated from Cordyceps militaris cultivated on rice bran medium was investigated. C militaris produced proteolytic enzymes from 10 days after inoculation, maximum enzyme production was found at 25 days. The optimum temperature and pH of proteases production was at $25^{\circ}C$ and pH 7.0, respectively. The protease activity was observed in the four peaks (Pro-I, Pro-II, Pro-III, and Pro-IV) separated through Sephadex G-100 column chromatography. The separated protease was optimally active at $25^{\circ}C$. Optimum pH of the protease was between 7 and 8. Enzyme was also stable over at $30-80^{\circ}C$. The enzyme was highly stable in a pH range of 4-9. Protease activity was found to be slightly decreased by the addition of $Mg^{2+}$, $Mn^{2+}$, $Zn^{2+}$, $Fe^{2+}$ and $Cu^{2+}$, whereas inhibited by the addition of $Ca^{2+}$ and $Co^{2+}$ Protease activity was inhibited by protease inhibitor PMSF. On the other hand, the partially purified protease was investigated on proteolytic protease activity by zymogram gel electrophoresis using three substances (casein, gelatin and fibrin). Four active bands (F-I, FII, F-III, and F-IV) of fibrin degradation were revealed on fibrin zymogram gels. Both of F-II and FIII showed caseinolytic, fibrinolytic and gelatinolytic activities in three gels. Thermostability, pH stability, and pH-thermostability of the enzyme determined the residual fibrinolytic activity also displayed on fibrin zymogram gel. The only one enzyme (F-II) displayed over a broad range of temperature at $30-90^{\circ}C$. The FII displayed fibrinolytic activity in the pH range 3-5, but was inactivated in the range of pH 6-11. The F-I and F-III showed enzyme activity in the pH range of 6-11. In the pH-thermostability, the F-II only kept fibrinolytic activity after heating at $100^{\circ}C$ for 10, 20 and 30 min at pH 3 and pH 7, respectively. On the other hand, the F-II was retained activity until heating for 10 min under pH 11 condition. By using fibrin zymogram gel electrophoresis, extracellular fibrinolytic enzyme F-II from C. militaris showed unusual thermostable under acid and neutral conditions.

Screening of a New Fibrinolytic Substances-Producing Yeast (혈전용해활성이 우수한 효모의 탐색)

  • Jang, In-Taek;Kim, Young-Hun;Yi, Sung-Hun;Lim, Sung-Il;Lee, Jong-Soo
    • The Korean Journal of Mycology
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    • v.39 no.3
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    • pp.227-228
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    • 2011
  • Fibrinolytic activities of culture concentrates of various yeasts were investigated. The concentrates of the culture broth of Saccharomyces cerevisiae Y99-7 showed the strongest fibrinolytic activity of 25 mm (clear zone). The fibrinolytic activity of Saccharomyces cerevisiae Y99-7 was more high in the culture concentrates from PD broth rather than that of yeast extract-peptone dextrose cultures (clear zone : 22.7 mm).

Selection and Fermentation Characteristics of Cheongbukjang Strains (청국장 균주의 선발과 발효 특성)

  • Woo Seung-Mi;Kwon Joong-Ho;Jeong Yong-Jin
    • Food Science and Preservation
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    • v.13 no.1
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    • pp.77-82
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    • 2006
  • This study was carried out to investigate the Cheongbukjang fermentation characteristics and to select the strain showing a fibrinolytic activity. Fibrinolytic activity of 5 strains isolated from the commercial Chungkukjang was tested N2 strain showed the highest activity $(41.7\%)$ while N3 and N5 had similar activity $(27.8\%)$ compared to plasmin 1 unit/mL The selected N2 strain was determined as B. subtilis with $90.1\%$ homology by API kit analysis. Quality characteristics of Cheongbukjang fermented by 6 kinds of strains were tested Among 3 strains cultured, B. subtilis (KCTC 3014) showed the highest viscous substance, fibrinolytic activity and amino type nitrogen content. After isolated, B. subtilis N2 showed the highest viscous substance, fibrinolytic activity and amino type nitrogen content. Optimum steam-time for Cheongbukjang fermented by B. subtilis (KCTC 3014) and B. subtilis N2 was 45 min while optimum fermentation-time was 20 hr.