Among 128 proteolytic bacterial isolates, Brevibacterium otitidis,
CBS-76 was choosen on the basis of secreted protease. Analysis of
purified protease revealed an apparent molecular weight of 47 KDa with
15.2% glutamic acid content. The purified protease showed the maximum
activity after 68h at 35°C and pH 7.2. The purified enzyme was inhibited
in the presence of EDTA but maximally activated in the presence of
sodium arsenate. LD50 on mice was 8 μg /100 g body weight. Histological
study using transmission electron microscope revealed that nuclei of
treated mice hepatocytes appeared with inactive heterochromatin and the
nucleoli tend to disintegrate. While the cytoplasm contains swollen
mitochondria and some destructed mitochondria lost their inner cristae.
And fat droplets accumulated in the cytoplasm in the form of empty
vacuoles(steatosis). On studying, novel inhibitors derived from common
drugs derivatives of saccharin sodium, compound 6 and 9 showed the
maximum percentage of enzyme inhibition.