Characterization of a 27 kDa Fibrinolytic Enzyme from Bacillus amyloliquefaciens CH86-1 Isolated from Cheonggukjang

  • Lee, Ae Ran; 
  • Kim, Gyoung Min; 
  • Park, Jae-Yong; 
  • Jo, Hyeon Deok; 
  • Cha, Jaeho; 
  • 외 3명
Citations

WEB OF SCIENCE

13
Citations

SCOPUS

16

초록

Bacillus amyloliquefaciens CH86-1 isolated from cheonggukjang was found to have strong fibrinolytic activity when grown on Luria-Bertani medium, and this activity increased sharply when the cells entered the stationary phase. The major fibrinolytic enzyme, AprE86-1, was purified from culture supernatant and identified by tandem mass spectrometry. The molecular weight of the mature enzyme was determined to be 27 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The optimum pH of partially purified AprE86-1 was 6.0-7.0 and it was stable at up to 45 degrees C.

키워드

Bacillus amyloliquefaciens; cheonggukjang; fibrinolytic activity; proteases; IDENTIFICATION; PURIFICATION; EXPRESSION; CLONING; GENE
제목
Characterization of a 27 kDa Fibrinolytic Enzyme from Bacillus amyloliquefaciens CH86-1 Isolated from Cheonggukjang
저자
Lee, Ae Ran; Kim, Gyoung Min; Park, Jae-Yong; Jo, Hyeon Deok; Cha, Jaeho; Song, Young-Sun; Chun, Jiyeon; Kim, Jeong Hwan
DOI
10.3839/jksabc.2010.010
발행일
2010-02
유형
Article
저널명
Journal of the Korean Society for Applied Biological Chemistry
권
53
호
1
페이지
56 ~ 61