Protease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Protease from Streptomyces griseus is a mixture of at least three proteolytic activities including an extracellular serine protease. Serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid.
This product is a mixture of at least three caseinolytic activities and one aminopeptidase activity.
The caseinolytic enzymes were named as Streptomyces griseus
Protease A, Streptomyces griseus
Protease B and Streptomyces griseus
Trypsin. This product may be used when extensive or complete degradation of protein is required. This protease mixture is highly nonspecific and can digest casein to the extent of >70% as mono-amino acids.