Elastase

The inactive  proelastase  is activated by trypsin to the active form elastase. Elastase attacks  peptide  bonds  next  to  the  small amino  acid residues such  3s  glycine, alanine and  serine and has a  broader  specificity than  the other  two enzymes.

All  the  three  enzymes viz.  trypsin,  chymotrypsin  and  elastase are endopeptidases (a subclass of peptide hydrolases that hydrolyse the more centrally situated peptide bonds). You have already seen that pepsin is also an endopeptidase.