Serine protease with chymotryptic, collagenolytic and SANA activities. Hydrolysis of proteins, with broad specificity for peptide bonds. Native collagen is cleaved about 75% of the length of the molecule from the N-terminus. Low activity on small molecule substrates of both trypsin and chymotrypsin. Optimum pH is 7-8. Optimum temperature is 30 degrees Celsius. Monomer. Belongs to the peptidase S1 family.