PURIFICATION AND CHARACTERIZATION OF A NOVEL FIBRINOLYTIC ENZYME FROMBACILLUS SP. KA38 ORIGINATED FROM FERMENTED FISH

A Bacillus sp. producing a new fibrinolytic enzyme was screened from a fermented fish known as Jeot-Gal in Korea. The enzyme was purified to electrophoretic homogeneity using consecutive procedures including am monium sulfate fractionation and column chromatography. The enzyme was highly specific toward fibrin clots and directly degraded them. The m olecular weight was 41 kDa and the first 10 amino acids of the N-termi nal sequence was Val-Tyr-Pro-Phe-Pro-Gly-Pro-Ile-Pro-Asn. Optimal fibr inolytic activity was observed at pH 7.0 and 40 degrees C, and the spe cific activity was above 1.4 U/mg when determined with plasmin as a st andard. The fibrinolytic activity was stimulated with zinc ions and re pressed by various metalloprotease inhibitors, which indicates that th e enzyme is a novel metalloprotease.