Abstract
An organism capable of producing an alkaline proteinase was isolated and identified as Pseudomonas maltophilia.
By simple Sephadex-gel chromatographies, the alkaline proteinase was purified to homogeneity with a specific activity 74-fold higher than that of the culture broth. The purified enzyme had a molecular weight of 46, 000 consisting of 19, 000 and 27, 000 molecular subunits. The optimum pH and temperature were pH 10.5 and 55°C, respectively. Calcium ion activated and stabilized the enzyme activity. The enzyme was inhibited by ethylenediaminetetraacetate, phenylmethylsulfonyl fluoride and chymostatin, indicating that the enzyme was a serine metalloenzyme.
