Pankreaslipase

Pankreaslipase, also known as pancreatic lipase, is a major digestive enzyme produced by the exocrine pancreas. It is secreted into the small intestine as part of pancreatic juice, where it catalyzes the hydrolysis of dietary triglycerides (triacylglycerols) into absorbable products.

In the intestinal lumen, pancreatic lipase cleaves triglycerides at the sn-1 and sn-3 positions, yielding free fatty acids and 2-monoacylglycerol. These products are taken up by enterocytes for resynthesis into triglycerides and incorporation into chylomicrons. The presence of bile salts emulsifies fats and increases the surface area available for lipolysis. Colipase, a cofactor secreted as procolipase and activated by trypsin, anchors lipase to the lipid–water interface and helps preserve activity in the presence of bile salts.

Secretion and activity are regulated by digestive signals, with optimal activity in the neutral to slightly alkaline pH of the small intestine. Pancreatic lipase functions alongside other lipases and brush-border enzymes in the overall process of fat digestion, and its activity is supported by pancreatic bicarbonate and bile acids.

Clinical significance includes pancreatic lipase's role as a marker of pancreatic exocrine function; reduced activity due to pancreatic insufficiency can cause fat malabsorption and steatorrhea. Pancreatic lipase levels in serum can rise during acute pancreatitis, aiding diagnosis. Therapeutically, the lipase inhibitor orlistat reduces fat absorption by inhibiting pancreatic lipase and is used in obesity management.