Trypsin-Chymotrypsin is the co-crystal of Chymotrypsin and Trypsin so it has the properties of both.

The activity of hydrolyzing casein is as much as Chymotrypsin. But the activity of its Chemotrypsin to hydrolyze N-Benzoyl-L-tyrosine ethyl ester(BTEE)is three times higher than Chemotrypsin.The activity of hydrolyze ester bond similar to that of Trypsin. It is stable when dry and easy to be inactivated in solutions.

Chymotrypsin is the endopeptidase extracted and separated from the fresh pancreas of cows (or pigs).
Primary structure and spatial structure of α- Chymotrypsin have been clearly explained, which is a single peptide chain composed of 245 amino acid residues, with 5 pairs of disulfide linkage in the molecule.

Chymotrypsin is white and light yellow crystal or amorphous powder, and easily soluble in the water, but insoluble in organic solvent. Relative molecular mass is 24000, and the optimum PH is 8~9. 

Chymotrypsin is stable at a dry state, but will be quickly deactivated in water solution, most stable in the
water solution with PH3~4. When it acts on the protein, Chymotrypsin will hydrolyze the peptide bond
formed by the carboxyl of L-tyrosine and L-phenylalanine in priority.