Chymotrypsin from shrimp, Penaeus californiensis, was compared to Bos taurus chymotrypsin, and its
structure–function relationship was studied. Catalytic efficiency toward synthetic substrate is lower,
but it has a broad specificity and higher activity toward protein substrates, including collagen. It is active
at pH 4–10 and fully active up to 50 C for 2 h and at least nine days at room temperature. The activation
peptide is twice as long as bovine chymotrypsinogen, has less disulfide bridges, and is a single polypeptide.
Only one activation step is necessary from chymotrypsinogen to the mature enzyme. Postmortem
implications in muscle softening and melanisation, resistance to temperature and pH and efficiency with
proteinaceous substrates make chymotrypsin useful as a biotechnological tool in food processing. This
makes shrimp processing wastes useful as a material for production of fine reagents.