Pancreatic lipase
Digestive enzyme found in humans
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Function
Pancreatic lipase is one of the main digestive enzymes, ultimately converting triglyceride substrates found in ingested oils to monoglycerides and free fatty acids.
- Triacylglycerol + 2 H2O 2-monoacylglycerol + 2 fatty acid anions
Bile salts secreted from the liver and stored in gallbladder are released into the duodenum, where they coat and emulsify large fat droplets into smaller droplets, thus increasing the overall surface area of the fat, which allows the lipase to break apart the fat more effectively. The resulting monomers (2 free fatty acids and one 2-monoacylglycerol) are then moved by way of peristalsis along the small intestine to be absorbed into the lymphatic system by a specialized vessel called a lacteal. This protein belongs to the pancreatic lipase family.
Unlike some pancreatic enzymes that are activated by proteolytic cleavage (e.g., trypsinogen), pancreatic lipase is secreted in its final form. However, it becomes efficient only in the presence of colipase in the duodenum.
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Medical significance
Diagnostic value
Pancreatic lipase is secreted from acinar cells into the duodenum through the duct system of the pancreas. Its concentration in serum is normally very low. Under extreme disruption of pancreatic function, such as pancreatitis or pancreatic adenocarcinoma, the pancreas may begin to autolyse and release pancreatic enzymes including pancreatic lipase into serum. Thus, through measurement of serum concentration of pancreatic lipase, acute pancreatitis can be diagnosed.
Inhibitors
Lipase inhibitors such as orlistat have been used as a treatment for obesity.

