• The Korean Journal of Mycology
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• v.40 no.4
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• pp.296-298
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• 2012

In this study, the biological activities of 33 kinds of wild mushroom methanol extracts were investigated. Boletellus elatus showed the greatest fibrinolytic activity (1.08 plasmin units/mL) in a fibrin plate assay, and the activity of Heterobasidion insulasis was 0.89 plasmin units. The thrombin inhibitory activities of Boletellus elatus and Heterobasidion insulasis were 93.32% and 93.69%, respectively. In a ${\alpha}$-glucosidase inhibitory activity test, Laccaria amethystina showed the greatest inhibitory activity at 81.25%. The antioxidative activities of Gomphus sp. and Geastrum lageniforme were 91.37% and 90.42%, respectively. Since Boletellus elatus and Heterobasidion insulasis have strong fibrinolytic and thrombin inhibitory and antioxidative activities, the two mushrooms can be used as material for the development of biofunctional foods for cardiovascular diseases.

• The Korean Journal of Mycology
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• v.40 no.3
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• pp.159-163
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• 2012

This study was performed to investigate the biological activities of Hericium erinaceus fruiting body, including antioxidative, fibrinolytic, thrombin inhibitory and ${\alpha}$-glucosidase inhibitory activities. The water extract of H. erinaceus was fractionated into hexane, chloroform, ethyl acetate, butanol and water fractions, and each of these fractions was individually assayed. The water extract showed high antioxidative activity at 87.78%. The water fraction showed the highest extraction yield at 35.68% (w/w). In the fraction activity tests, butanol and water fractions showed strong antioxidative activities at 87.91% and 92.27%, respectively. Assays for fibrinolytic activity indicated that only the ethyl acetate fraction has significant efficacy at 2.96 plasmin units/mL. The 10-fold dilution of hexane fraction showed high thrombin inhibitory activity, and ${\alpha}$-glucosidase inhibitory activity at 77.67% and 90.53%, respectively. In conclusion, solvent fractions of H. erinaceus can be used as materials for the development of biofunctional foods to prevent cardiovascular diseases.

• The Korean Journal of Mycology
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• v.39 no.3
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• pp.189-193
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• 2011

To investigate the physiological activities of hot water extract and solvent fractions isolated from Pleurotus ferulea, antioxidative, fibrinolytic, thrombin inhibitory, and ${\alpha}$-glucosidase inhibitory activities were examined. Pleurotus ferulea, hot water extract was fractionated into hexane, chloroform, ethyl acetate, butanol and water fraction. Each of these was assayed individually. The antioxidative activities of ethyl acetate and butanol fractions were 86.79% and 87.82%, respectively. Using the fibrin plate method, only the ethyl acetate fraction showed a plasmin activity of 0.08 units/ml. Thrombin inhibitory activities of chloroform and ethyl acetate fractions were 74.90% and 71.08%, respectively. In the ${\alpha}$-glucosidase inhibitory activity test, butanol fraction showed the highest activity at 49.67%. From the above results, we anticipate that solvent fractions of Pleurotus ferulea can be used as a materials for the development of biofunctional foods for cardiovascular diseases.

• The Korean Journal of Mycology
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• v.42 no.3
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• pp.207-212
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• 2014

This study was conducted in order to investigate the physiological activities, including antioxidative, fibrinolytic, thrombin inhibitory, and ${\alpha}$-glucosidase inhibitory activities of the water extract and solvent fractions isolated from Pholiota adiposa. The antioxidative activities of the water extract and water fraction were 57.57% and 48.27%, respectively. The fibrinolytic activity was strong only in the ethyl acetate fraction at 0.70 plasmin units/mL. The ethyl acetate fraction showed high thrombin inhibitory activity, and a-glucosidase inhibitory activity at 77.67% and 89.32%, respectively. The ethyl acetate fraction hydrolyzed both $A{\alpha}$ and $B{\beta}$ subunits of human fibrinogen, but did not show reactivity for the ${\gamma}$ form of human fibrinogen. Fibrinolytic activity of the ethyl acetate fraction was not decreased by heating for 10 min at $100^{\circ}C$.

• 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.

• Microbiology and Biotechnology Letters
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• v.42 no.2
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• pp.184-189
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• 2014

Yeast strains demonstrating fibrinolytic activity were isolated from traditional fermented soybean in Gangwon province, Korea. The AFY-1 strain isolated from fermented soybean paste showed the highest fibrinolytic activity (3.5 U/mg protein) corresponding to a 1.75 fold higher fibrinolytic activity compared with the plasmin (2.0 U/mg protein). The optimum temperature for the growth of AFY-1 strain was $32^{\circ}C$. Analysis of 18S rRNA gene sequence and carbon source utilization pattern indicated that the AFY-1 strain shares the highest homology (99%) with Saccharomycetales sp.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.9 no.3
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• pp.800-806
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• 2008

The strain HK-12 was enriched and isolated from naturally fermented soybean for the production of fibrinolytic enzyme and the proteome of this enzyme induced during the incubation period was analyzed. The activity of fibrinolytic enzyme derived from supernatants of the HK-12 culture was performed by fibrin plate method for solid fibrinolytic activity. As the result, the fibrinolytic activity of HK-12 grown on the nutrient agar media was about 2.3 times greater than that of plasmin used as standard. The purified enzyme was prepared by a series of purification process including ammonium sulfate precipitation, DEAE-cellulose, Sephadex chromatography. The molecular weight of the enzyme was determined to approximately 23kDa with SDS-PAGE. In order to examine which strain HK-12 proteins increased or decreased during the incubation period, 2-DE analysis was performed. Protein spot #1 significantly expressed on the 2-DE gel of bacteria cultivated for 36-hrs was analysed. As the result of protein sequence analysis using MALDI-TOF MS, one protein was identified as serine protein kinase (PrkA).

• Biotechnology and Bioprocess Engineering:BBE
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• v.6 no.4
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• pp.279-283
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• 2001

Cationic lipid emulsion system consisting of 1, 2-dioleoyl-sn-slycero-3-trimethyl-ammonium-propane(DOTAP) and plasmin DNA with various counterions in the lipid headgroups were prepared. The transfection activity of the cationic lipid emulsion systems was then investigated in vitro and in vivo. The complex formation of plasmid DNA lipid emulsion was affected by the counterions through charged headgroup repulsion and also by the salt concen-tration in the media. As such , the transfection activity of the DOTAP emulsion system can be controlled by changing the counterions.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1994.04a
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• pp.279-279
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• 1994

Fibrinolytic proteases, piscivorase I (PI) and piscivorase II (PII), were isolated from Agkistrodon piscivorus piscivorus (eastern cotonmouth moccasin) venom using gel filtration on Bio-Gel P100 and ion-exchange chromatography on CM-Sepharose. The molecular welghts of two proteases were approximately 23400 and 29000. Their isoelectric points 6.6 and 8.5, respectively. The partial amino acid sequences of PI were characterized by tryptic digestion. PI readily cleaves the A${\alpha}$-and B${\beta}$-chaln of fibronogen, but PII rapidly cleaves A${\alpha}$-chain and more slowly the B${\beta}$-chain, They were activated by Ca$\^$2+/, Mg$\^$2+/ and Ba$\^$2+/, but inhibited by Zn$\^$2+/, Cu$\^$2+/ and Mn$\^$2+/. Two enzymes were also inhibited by cysten, ${\beta}$-mercapto -ethanol, and by metal chelators such as EDTA and EGTA, but not by benzamidine, PMSF, soybean trypsin inhibitor and aprotinin. They did not act like thrombin, plasmin and kallikrein, using specific chromogenllc substrates. Two protease did not induce platelet aggregation. PI showed low hemorrhagic activity at dosage of 50 $\mu\textrm{g}$.

• 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.