Purification and characterization of an extracellular protease from Flavobacterium arborescens

An extracellular protease from Flavobacterium arborescens has been purified to an apparent homogeneity and characterized. The enzyme is most active at pH 8-10.5, requires no metal cofactor, and is inhibited by diisopropyl fluorophosphate. The protease is nonspecific, is active at temperatures up to 60 degrees C, and is completely free of nucleases. The ease of purification and freedom from nucleolytic contaminants make the protease a useful deproteinizing agent in DNA and RNA manipulations.