• Journal of the Korean Society of Food Science and Nutrition
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• v.39 no.12
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• pp.1832-1838
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• 2010

The objective of this study was to improve the flavor of Cheonggukjang prepared by the culture optimization of starter with the fibrinolytic activity. After 25 strains isolated from the commercial Cheonggukjang and Doenjang in different regions were compared, 7 Bacillus strains with proteolytic and slime-producing activities were selected. When the fibrin plate method for fibrinolytic activity was applied, CJJN-4 and 5 showed the higher activity in tripticase soy broth (TSB). All Cheonggukjang prepared with CJJN-4 and 5 also had the fibrinolytic activity, regardless of culture temperature or time. Especially, Cheonggukjang prepared at $40^{\circ}C$ showed higher activity than $45^{\circ}C$, and Cheonggukjang prepared with CJJN-4 for 48 hr at $40^{\circ}C$ showed the highest fibrinolytic activity. Although there was no significant difference in pH of Cheonggukjang prepared with CJJN-4 or 5 during 72 hr at $40^{\circ}C$, Cheonggukjang prepared with CJJN-4 at $45^{\circ}C$ had lower pH until 60 hr than $40^{\circ}C$ or CJJN-5. The total amino type nitrogen contents of Cheonggukjang were 1,139.6 (CJJN-4) and 1,027.6 mg% (CJJN-5) for 72 hr at $40^{\circ}C$, and their producing rates were also higher at $40^{\circ}C$ fermentation than $45^{\circ}C$. Meanwhile, the contents of ammonia type nitrogen induced unpleasant flavor were lower in Cheonggukjang with CJJN-4 and 5 at $40^{\circ}C$ than CJJN-5 at $45^{\circ}C$. Therefore, Cheonggukjang fermented with CJJN-4 starter at $40^{\circ}C$ had the improved flavor, such as change of amino or ammonia type nitrogen production, and higher fibrinolytic activity.

• Journal of Life Science
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• v.20 no.2
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• pp.183-189
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• 2010

A fibrinolytic enzyme producing Bacillus sp. J-19 was isolated from the popular Korean seasoning, pickled anchovy. The fibrinolytic enzyme was purified to homogeneity by chromatographic methods including ethanol precipitation and gel-filtration using Sephadex G-50. Compared to the crude enzyme extract, the specific activity of the enzyme increased 1021-fold with a recovery of 23%. The purified enzyme was estimated to be approximately 45 kDa by SDS-PAGE. Especially, the amidolytic activity in the presence of the synthetic substrate for serine protease (H-D-Ile-Pro-Arg-pNA, S-2288) represented approximately 17 U/mg. In addition, more than the 60% activity of the 45 kDa fibrinolytic activity was maintained in the presence of up to 30% (w/v) sodium chloride. These findings could provide a unique fibrinolytic enzyme, leading to a potential thrombolytic agent.

• Journal of the Korean Society of Food Science and Nutrition
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• v.34 no.6
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• pp.904-909
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• 2005

To produce functional food ingredient from the soybean curd residue (SCR), alkaline fermentation was performed with SCR from cold processed (D-SCR) or hot processed (P-SCR) tofu. The solid- state fermentation was performed by Bacillus firmus NA-1 at $42^{\circ}C$. The fermentation of heat-treated D- SCR resulted in higher production of peptides and fibrinolytic enzyme compared with D-SCR without heating. The P-SCR showed higher production of peptides, fibrinolytic enzyme, indicating alkaline pH after fermentation for 18 hr. When the moisture content of P-SCR was reduced to $60\%$, the production of peptides and fibrinolytic enzyme were enhanced. The P-SCR fortified with $10\%$ MFS (micronized full-fat soy flour) showed higher fibrinolytic enzyme activity and consistency index by fermentation of Bacillus firmus NA-1 Furthermore, the P- SCR fortified with $20\%$ MFS indicated relatively higher peptide content, fibrinolytic enzyme activity and enhanced flavor. By increasing the addition of MFS, the peptide content of fermented P-SCR was increased significantly, but fibrinolytic enzyme was slightly decreased.

• Applied Biological Chemistry
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• v.46 no.3
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• pp.176-182
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• 2003

An alkaline fibrinolytic protease-producing bacteria was isolated front Korean traditional soy sauce and identified as Bacillus subtilis K7 from the results of analyses of its morphological and physiological properties, $API^{\circledR}$, and Biolog system. The enzyme was purified by 75% ammonium sulfate fractionation, QAE-Sephadex anion and SP-Sephadex cation exchange column chromatography and Sephadex G-100 gel filtration. The specific activity of the purified enByme was 233.9 unit/mg protein and the yield of enzyme was 3.8%. The homogeneity of the purified enzyme was confirmed by polyacrylamide gel electrophoresis. Molecular mass of the enzyme was estimated about 21,500 Da by SDS-polyacrylamide get electrophoresis and gel chromatography. The optimum temperature and pH for the enzyme activity were $40^{\circ}C$ and 9.0, respectively. The enzyme was stable in a pH range of 5.0 to 12.0, and 60% of its activity was lost on heat treatment at $50^{\circ}C$ for 20 min. The activity of the purified enzyme was inhibited by the presence of $Fe^{2+},\;Ag^{2+},\;Cu6{2+}$, iodoacetate, ethylene diamine tetraacetic acid (EDTA), and trans-1,2-diaminocycloheane-N,N,N',N'-tetraacetic acid (CDTA). The results indicates that the enzyme requires a metal ion for its enzymatic activity.

• Journal of Life Science
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• v.23 no.12
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• pp.1525-1531
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• 2013

Baegilju is a famous traditional Korean wine made over the course of 100 days. The physiological functionalities of Baegilju were evaluated using different tests. The spectrophotometric method was used to determine the total concentration of polyphenolics and flavonoids and DPPH and ABTS radicals. A nitrite scavenging assay was used to evaluate antioxidant activity. The fibrin plate method was used for fibrinolysis and to evaluate angiotensin I converting enzyme (ACE) inhibitory activity; finally, the colorimetric determination method was used to evaluate acetylcholinesterase (AChE) inhibitory activity. The total polyphenolic content of non-sterilized Baegilju and sterilized Baegilju were 391.59 ${\mu}g$ and 401.33 ${\mu}g$ tannic acid equivalents/ml, respectively; and the flavonoids contents were 284.75 ${\mu}g$ and 308.35 ${\mu}g$ quercetin equivalents/ml, respectively. Baegilju exhibited more excellent antioxidant activities (DPPH and ABTS radicals, nitrite scavenging activity) than did Cheongju. In addition, the fibrinolytic activity and AChE inhibitory activity were found to be higher in Baegilju than they were in Cheongju. The ACE inhibitory activity of non-sterilized Baegilju, sterilized Baegilju, and Cheongju were 23.62%, 19.99%, and 38.91%, respectively. Therefore, these results suggest that Baegilju has potential as an antioxidant agent and anti-thrombosis agent.

• Journal of Life Science
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• v.19 no.10
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• pp.1468-1477
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• 2009

The comparative effects of the fibrinolytic, and tyrosinase inhibition activities and electrophoretical protein patterns with freeze-drying silkworm powder (FDSW), heating-drying silkworm powder (HDSW) and fermented silkworm powder by Bacillus subtilis or Lactobacillus hilgardii were investigated. When total protein patterns of FDSW, HDSW, both fermented SW, were analyzed by native- and SDS-polyacrylamide gel electrophoresis (PAGE), there were slightly varietal differences in electrophoretical protein patterns. Major minerals of FDSW and HDSW were K, Ca, Mg, and Zn. Major compositional amino acids of FDSW and HDSW were glycine, alanine, glutamic acid, aspartic acid, and serine. Major fatty acids of FDSW and HDSW were linolenic acid, oleic acid, and palmitic acid. Fibriolytic activity was the highest in the fermented FDSW by 5% B. subtilis among the various samples. Tyrosinase inhibition activity was higher in the water and 70% methanolic extract of FDSW than in HDSW. DPPH radical scavenging activity was slightly stronger in HDSW than in FDSW. In addition, DPPH radical scavenging activity was higher in FDSW or HDSW fermented by L. hilgardii than that fermented by B. subtilis, however, all samples exhibited a relatively low activity compared to the butylated hydroxytoluene (BHT). These results may provide the basic data to understand the biological activities of fermented SW.

• The Korean Journal of Mycology
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• v.36 no.2
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• pp.183-188
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• 2008

A fibrinolytic serine protease was purified from the fruiting bodies of an edible mushroom, Albatrellus confluens. The enzyme had a molecular mass of 30086.41 Da, as measured by MALDI-TOF mass spectrometry. The N-terminal amino acid sequence of the enzyme was Glu-Thr-Val-Thr-Glu-Thr-Thr-Ala -Pro-Trp-Gly-Leu-Ser-Arg-Ile. It displayed optimal activity at $50^{\circ}C$ and within a pH range of $8.0{\sim}10.0$, suggesting that the enzyme is an alkaline protease. The enzyme was stable up to $30^{\circ}C$. The enzyme displayed a strong substrate specificity for the synthetic peptide, N-Suc-Ala-Ala-Pro-Phe pNA. The enzyme activity was completely inhibited by addition of PMSF, indicating that the enzyme is a serine protease. No inhibition was observed following addition of E-64, pepstatin, or EDTA. The activity of the purified enzyme was decreased in the presence $Fe^{2+}$ or $Co^{2+}$, and the enzyme was completely inhibited by addition of $Hg^{2+}$. From these results, we propose that Albatrellus confluens could be used for biofunctional foods development and has potential therapeutic value for the treatment of vascular diseases.

• Journal of Chest Surgery
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• v.41 no.4
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• pp.484-488
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• 2008

During long-term anticoagulation treatment with using heparin in a pregnant patient with a mechanical mitral prosthesis, we observed several anticoagulation-related complications, including repeated prosthetic valve thrombosis. This was found to be caused by heparin resistance due to an anti-thrombin III deficiency. Thrombolytic therapy using urokinase or tissue plasminogen activator (tPA) was successful and safe for her as well as her baby.

• Proceedings of the SOHE Conference
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• 2004.12a
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• pp.90-90
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• 2004

• Microbiology and Biotechnology Letters
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• v.36 no.4
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• pp.291-298
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• 2008

The cardiovascular angiotensin I-converting enzyme inhibitory activity, fibrinolytic activity and bbb-secretase inhibitory activity of four kinds of red wine were investigated during fermentation and post-fermentation. After 10 days of fermentation, the antihypertensive angiotensin I-converting enzyme (ACE) inhibitory activities of all the red wines ranged from 38.6% to 58.8%. However, the ACE inhibitory activities increased with the prolongation of the post-fermentation period; moreover, in the Vitis hybrid red wine, the ACE inhibitory activity reached its highest value, 76.9%, after 120 days of post-fermentation. During the fermentation and post-fermentation of all the red wines, fibrinolytic activity was weak or not detected. After 10 days of fermentation, Vitis labrusca B red wine exhibited the greatest antidementia $\beta$-secretase inhibitory activity of 54.8%, though $\beta$-secretase inhibitory activity decreased significantly to less than 10% during 120 days of post-fermentation. In conclusion, we obtained a highly valuable Vitis hybrid red wine that was fermented for 10 days at $25^{\circ}C$ with Vitis hybrid and S. cerevisiae K-7 and then post-fermentation for 120 days at $4^{\circ}C$.