Separation and Comparative Characterization of the Cationic Protease and Anionic Protease from the Culture Medium ofThermoactinomyces vulgaris

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Abstract
The anionic protease component which frequently contaminates preparations of routinely isolated cationic protease (thermitase) from T. vulgaris was purified, virtually to homogeneity, by rechromatography on controlled pore glass (CPG-10). Starting materials were column eluates with anionic protease, contaminated with residual thermitase activity. The purified anionic enzyme shares several properties with thermitase, such as size, sensitivity against phenylmethanesulfonyl fluoride and Hg2+, UV spectral, immunological and pH behavior. The isoelectric point (at pH 6.5), temperature dependence (more heat stable) and enzymatic activity (less active) of anionic protease differ significantly from thermitase. At pH 8 or 6 and 25 or 4.degree. C anionic protease is hydrolyzed completely by thermitase. Like other protein substrates, anionic protease simultaneously acts as a stabilizer for thermitase. In contrast to thermitase, the anionic enzyme partially changes spontaneously during long-term storage at 4.degree. C and pH to a cationic protein species endowed with proteolytic activity.

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