Which of the following is not secreted by the pancreas

Pancreatic juice is secreted most abundantly in response to the presence of chyme in the upper portions of the small intestine, and the characteristics of the pancreatic juice are determined to some extent by the types of food in the chyme. (The pancreas also secretes insulin, but this is not secreted by the same pancreatic tissue that secretes intestinal pancreatic juice. Instead, insulin is secreted directly into the blood-not into the intestine-by  the  islets of Langerhans that occur in islet patches throughout the pancreas). The most important of the pancreatic enzymes for digesting proteins are trypsin, chymotrypsin, and carboxypolypeptidase. By far the most abundant of these is trypsin. Trypsin and chymotrypsin split whole and partially digested proteins into peptides of various sizes but do not cause  release  of  individual  amino  acids. However,  carboxypolypeptidase splits  some peptides into individual amino acids, thus completing digestion of some proteins all the way to the amino acid state. The pancreatic enzyme for digesting carbohydrates is  pancreatic  amylase, which hydrolyzes starches, glycogen, and most other carbohydrates  (except cellulose) to form mostly disaccharides and a few trisaccharides.The main enzymes for fat digestion are (1) pancreatic lipase, which is capable of hydrolyzing neutral fat into  fatty  acids  and  monoglycerides;  (2) cholesterol esterase, which causes hydrolysis of cholesterol esters;and  (3)  phospholipase,  which splits fatty acids  from phospholipids. When first synthesized in the pancreatic cells, the proteolytic digestive enzymes are in the inactive forms trypsinogen, chymotrypsinogen, and procarboxypolypeptidase, which are all inactive enzymatically. They become activated only after they are secreted into the intestinal tract. Trypsinogen is activated by an enzyme called enterokinase, which is secreted by the intestinal mucosa when chyme comes in contact with the mucosa. Also, trypsinogen can be autocatalytically activated by trypsin that has already been formed from previously secreted trypsinogen.  Chymotrypsinogen is  activated by trypsin to form chymotrypsin, and procarboxypolypeptidase is activated in a similar manner.