Proteolytic Enzymes from Bacterium Linens

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Abstract
An extracellular proteinase (specific activity 23.3 to 78.7 mg. of casein hydrolyzed in 1.5 hrs. per mg. of enzyme protein) was recovered from the medium after 2 days'' growth of B. linens 450, by ammonium sulfate precipitation (52 to 100% saturation). Of the proteins tested, only casein and a bovine seminal protein prepn. were attacked. The product of proteinase action is a polypeptide. No polypeptidase, and little peptidase, activity was found in the proteinase prepn. With beta-casein as the substrate, a proteolytic action superficially similar to that of rennin was observed.

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