The protease was active on a variety of modified (azocasein) or
natural proteins. The protease exhibited the highest activity on
casein (Fig. 3a). The substrate specificity studies revealed that the
protease activity was higher when casein was used as substrate
followed by peptone, BSA, azocasein and hemoglobin respectively,
but a weak activity found with elastin and tryptone. It can be suggested
that this protease is able to digest different protein sources
converting them to small peptides and amino acids, indicating that
this is a type of protease with a broad range of substrate specificity
and ability for unlimited proteolysis.