Purification and Some Properties of a Protease from Streptomyces cellulosae

Abstract

Weselected Streptomyces cellulosae bacause it secreted an unusual protease into the culture broth. The protease formed more turbidity in a 16% soybean protein hydrolysate in the initial stage of the reaction than α-chymotrypsin did, when the proteolytic activity of the protease was same as that of α-chymotrypsin. The protease was purified 564-fold from culture broth in 5.8% yield. The precipitated product from the soybean protein hydrolysate was a protein-like compoundcontaining mainly hydrophobic amino acids.