피브린 Zymographic Gel에서 Bacillus amyloliquefaciens G-13으로부터 혈전용해효소의 생성에 영향을 미치는 물리화학적 요인들의 비교Comparison of Physicochemical Factors Influencing the Production of Fibrinolytic Enzymes from Bacillus amyloliquefaciens G-13 in Fibrin Zymographic Gel
- Other Titles
- Comparison of Physicochemical Factors Influencing the Production of Fibrinolytic Enzymes from Bacillus amyloliquefaciens G-13 in Fibrin Zymographic Gel
- Authors
- 이현호; 차민지; 오계헌
- Issue Date
- 2020
- Publisher
- 한국생물공학회
- Keywords
- Bacillus amyloliqeufaciens G-13; fibrinolytic enzyme; fibrin zymograpy
- Citation
- Korean Society for Biotechnology and Bioengineering Journal, v.35, no.3, pp 199 - 207
- Pages
- 9
- Journal Title
- Korean Society for Biotechnology and Bioengineering Journal
- Volume
- 35
- Number
- 3
- Start Page
- 199
- End Page
- 207
- URI
- https://scholarworks.bwise.kr/sch/handle/2021.sw.sch/3396
- ISSN
- 1225-7117
2288-8268
- Abstract
- Our previous research demonstrated the characteristics and fibrinolytic activities of NaCl- and capsaicin-resistant bacterium Bacillus amyloliquefaciens G-13, isolated from mustard leaf kimchi [1]. In this study, we extended the work to the comparison of various physicochemical factors (e.g., temperature, pH, NaCl, capsaicin, metal ions, and inhibitors) influencing the production of fibrinolytic enzyme by strain G-13. Initially, a time course of the fibrinolytic activity of strain G-13 was measured by the fibrin plate assay, and after 84 hours of incubation, the maximum fibrinolytic activity was about 3.42 times that of plasmin used as the standard.
Through a fibrin zymographic assay, four bands (23, 34, 45, and 67 kDa) of fibrinolytic enzyme from strain G-13 were compared in fibrin zymographic gels. The strain could grow and produce the fibrinolytic enzyme in the presence of NaCl (1-10%) or capsaicin (0-300 µg/mL), respectively. The optimum pH and temperature for the enzymatic activity were 8 and 35o C. In the study of the effects of metal ions on fibrinolytic activity, K+ , Ca2+, and Mg2+ ions increased the activity and maintained it overall, but Fe3+, Zn2+, Ba2+, and Hg2+ ions rapidly decreased the activity of the fibrinolytic enzyme. The enzyme was completely inhibited by phenylmethanesulfonyl fluroide (PMSF), suggesting that it was a serine protease.
These results provide important clues for understanding the characteristics of fibrinolytic bacteria by confirming the effects of B. amyloliquefaciens G-13 on various physicochemical factors influencing the production of fibrinolytic enzymes through fibrin zymography
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