Purification and characterization of fibrinolytic alkaline protease from Fusarium sp. BLB |
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Authors: | Mitsuhiro Ueda Toshihiro Kubo Kazutaka Miyatake Takumi Nakamura |
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Affiliation: | (1) Laboratory of Biocycle Engineering, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Sakai Osaka, 599-8531, Japan;(2) SODX Corporation, 1-3-14, Techno stage, Izumi Osaka, 594-1144, Japan |
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Abstract: | Fusarium sp. BLB, which produces a strongly fibrinolytic enzyme, was isolated from plant leaf (Hibiscus). Fibrinolytic alkaline protease was purified from a culture filtrate of Fusarium sp. BLB by precipitation with (NH4)2SO4 and column chromatography with CM-Toyopearl 650M and Superdex 75. The purified enzyme was homogeneous on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The molecular weight was 27,000 by SDS-PAGE. Maximum activity of protease was observed at pH 9.5 and 50°C. Purified protease was active between pH 2.5 and 11.5 and was found to be stable up to 50°C. The enzyme derived from Fusarium sp. BLB is useful for thrombolytic therapy because this enzyme showed pH resistance. The activity was inhibited by diisopropylfluorophosphate and phenylmethylsulfonyl fluoride. The N-terminal amino acid sequence of the enzyme showed a similarity to those of proteases from Fusarium sp., Streptomyces griseus, Bos taurus bovine, Katsuwo pelamis digestive tract, and Lumbricus rubellus. |
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Keywords: | Fibrinolytic activity Alkaline serine protease Fusarium sp |
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