Purification and Characterization of Organic Solvent-Stable Protease from Organic Solvent-Tolerant Pseudomonas aeruginosa PST-01

概要

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An organic solvent-stable protease(PST-01 protease) in a culture broth of organic solvent-tolerant Pseudomonas aeruginosa PST-01 was purified by successive hydrophobic interaction chromatography using Butyl-Toyopearl gels. The purified enzyme was homogeneous as determined by SDS-polyacrylamide gel electrophoresis. PST-01 protease had a molecular mass of 38 kDa. The optimum temperature and pH for casein hydrolysis were 55℃ and 8.5, respectively. PST-01 protease was stable at pH8-12 and below 50℃ and was determined to be a metalloprotease which was inhibited by EDTA, 1, 10-phenanthroline, and phosphoramidon. PST-01 protease inhibited by EDTA was reactivated completely by the addition of zinc or cobalt ions. The stability of PST-01 protease in solutions containing water-soluble organic solvents or alcohols was higher that in the absence of organic solvent. Furthermore, in general, PST-01 protease was more stable than commercially available proteases, namely, subtilisin Carlsberg, thermolysin, and α-chymotrypsin, in the presence of water-soluble organic solvents or alcohols.
社団法人日本生物工学会の論文
1999-01-25