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

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.