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KMID : 0545119990090050675
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Journal of Microbiology and Biotechnology
1999 Volume.9 No. 5 p.675 ~ p.678
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Purification and Characterization of Metalloproteases from Pleurotus sajor-caju
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Shin Hyun-Hee
Choi Hye-Seon
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Abstract
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Fibrinolytic protease activity was detected in the fruit body of Pleurotus sajor-caju using a fibrin plate method. Two fibrinolytic activities (FPI and Ⅱ) were found at the regions of 14.5 and 86.0kDa by using gel-filtration column chromatography. FPII was identified as an alkaline protease, whereas FPI was a neutral protease. Both were inhibited by phenanthroline and EDTA, suggesting that they are metalloproteases. Inactivated enzyme activities were restored by adding Co^2+ or Zn^2+. lodoacetate inhibited FPI, but not FPII. Both enzymes cleaved B_β and γ chains of the human fibrinogen. FPII showed a preference to hydrophobic and bulky residues of nitroanilidine compounds as substrates, whereas FPI preferred positively charged residues.
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