Studies on Bacterial Protease

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Abstract
Some physical and chemical properties and substrate specificity were investigated of the neutral protease obtained from B. amylosacchariticus, a strain of saccharogenic α-amylase producing Bacillus subtilis. The molecular weight and sedimentation coefficient of the protease were estimated to be 33,800 and 3.02, respectively, by ultracentrifugal analyses, and alanine was identified as an amino-terminal amino acid of the enzyme by the Sanger’s method. The enzyme showed more broad specificity than the neutral protease of liquefying α-amylase-producing B. subtilis, when tested with synthetic peptides, and hippuryl-l-leucinamide was the best substrate among 42 compounds tested. On a long incubation, the enzyme hydrolyzed several proteins in a degree of 10 to 25% as peptide bond cleavage.

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