Purification and Some Properties of Alkaline Proteinase Produced by Pseudomonas maltophilia

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.