Answer:
The aromatic amino acids; Phenylalanine, Tryptophan, Tyrosine
Amino acids with bulky side chains; Leucine and Methionine
Step-by-step explanation:
Chymotrypsin is a member of the serine proteases, which is family of enzymes that hydrolyze peptide bonds through the action of an active site serine.
Chymotrypsin cleaves peptide bonds on the C-terminal of aromatic amino acids or amino acids with bulky hydrophobic sides chains such as phenylalanine, tyrosine and tryptophan, leucine and methionine. This specificity for aromatic amino acids is due to its large hydrophobic pocket and due to the complementary nature of these amino acids when they bind to the pocket.