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Characterization of a 27 kDa Fibrinolytic Enzyme from Bacillus amyloliquefaciens CH86-1 Isolated from Cheonggukjang
- Authors
- Lee, Ae Ran; Kim, Gyoung Min; Park, Jae-Yong; Jo, Hyeon Deok; Cha, Jaeho; Song, Young-Sun; Chun, Jiyeon; Kim, Jeong Hwan
- Issue Date
- Feb-2010
- Publisher
- KOREAN SOC APPLIED BIOLOGICAL CHEMISTRY
- Keywords
- Bacillus amyloliquefaciens; cheonggukjang; fibrinolytic activity; proteases
- Citation
- JOURNAL OF THE KOREAN SOCIETY FOR APPLIED BIOLOGICAL CHEMISTRY, v.53, no.1, pp 56 - 61
- Pages
- 6
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- JOURNAL OF THE KOREAN SOCIETY FOR APPLIED BIOLOGICAL CHEMISTRY
- Volume
- 53
- Number
- 1
- Start Page
- 56
- End Page
- 61
- ISSN
- 1738-2203
2234-344X
- Abstract
- 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.
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