Purification and Some Properties of an Alkalophilic Proteinase of a Streptomyces Species

Abstract

An alkalophilic proteinase was isolated in a crystalline state from the culture filtrate of a Streptomyces sp. which was screened as an organism to grow on the media of pH values above 9.5. The proteinase was inactivated by DFP. It was also inactivated by EDTA at temperatures above 25°C but, was not inactivated by the reagent at temperatures lower than 20°C. The proteinase showed its optimal pH at 12 or higher than 12 and the proteolytic action occurred even in solutions containing 0.2 m sodium hydroxide. The enzyme exhibited its maximum activity at 60°C. The present paper employs a new definition for a unit of the so called proteinase activity.