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Characterization of a 27 kDa Fibrinolytic Enzyme from Bacillus amyloliquefaciens CH51 Isolated from Cheonggukjang
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  • Characterization of a 27 kDa Fibrinolytic Enzyme from Bacillus amyloliquefaciens CH51 Isolated from Cheonggukjang
  • Characterization of a 27 kDa Fibrinolytic Enzyme from Bacillus amyloliquefaciens CH51 Isolated from Cheonggukjang
저자명
Kim. Gyoung-Min,Lee. Ae-Ran,Lee. Kang-Wook,Park. Ae-Yong,Chun. Ji-Yeon,Cha. Jae-Ho,Song. Young-Sun,Kim. Jeong-Hwan
간행물명
Journal of microbiology and biotechnology
권/호정보
2009년|19권 9호|pp.997-1004 (8 pages)
발행정보
한국미생물생명공학회
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정기간행물|ENG|
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

Bacillus amyloliquefancies CH51 isolated from cheonggukjang, a traditional Korean fermented soy food, has strong fibrinolytic activity and produces several fibrinolytic enzymes. Among four different growth media, tryptic soy broth was the best in terms of supporting cell growth and fibrinolytic activity of this strain. A protein with fibrinolytic activity was partially purified from the culture supernatant by CM-Sephadex and Phenyl Sepharose column chromatographies. Tandem mass spectrometric analysis showed that this protein is a homolog of AprE from B. subtilis and it was accordingly named AprE51. The optimum pH and temperature for partially purified AprE51 activity were 6.0 and $45^{circ}C$, respectively. A gene encoding AprE51, aprE51, was cloned from B. amyloliquefaciens CH51 genomic DNA. The aprE51 gene was overexpressed in heterologous B. subtilis strains deficient in fibrinolytic activity using an E. coli-Bacillus shuttle vector, pHY300PLK.