Pancreatic lipase is the most important lipolytic enzyme in the gastrointestinal tract and is essential for fat digestion. 
Pancreatic lipase is secreted from acinar cells in the pancreas and its secretion, with the pancreatic juice to the small intestine, is stimulated by hormones. These hormones are induced in the stomach by hydrolysed products in gastric digestion. 
The pancreatic lipase is secreted to the small intestine where it is most active, at pH 7-7,5.
Pancreatic lipase hydrolyses triglycerides and diglycerides by cleaving acyl chains at the sn-1 and sn-3 position
and releases free fatty acids and 2-monoglycerides.
The pancreatic lipase consists of 465 amino acids. Schematic picture of pancreatic lipase is shown in figure 2.  Pancreatic and gastric lipases share little homology but have the same hydrophobic region at the active site, which is important for the lipolytic activity. The hydrophobic region has the hexapeptide sequence Val-Gly-His-Ser-Gln-Gly and is at Ser153 in pancreatic lipases but Ser152 in gastric lipases.