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Pancreatic lipase, also known as human pancreatic lipase (PNLIP), is the primary enzyme responsible for digesting dietary triglycerides in the small intestine, hydrolyzing them into monoglycerides and free fatty acids for absorption.[1][3][7] It belongs to the alpha/beta hydrolase superfamily and employs a catalytic triad of serine, histidine, and aspartic acid to perform interfacial activation at the oil-water boundary, requiring colipase as a cofactor to function optimally amid bile salts.[1][2][3] Secreted by the pancreas into the duodenum, it processes 50-70% of ingested fats, playing a central role in lipid metabolism and energy homeostasis.[5][7] Dysregulation or deficiency leads to fat malabsorption in pancreatic insufficiency, while serum elevations serve as a key biomarker for acute pancreatitis.[1][3] Therapeutically, it is targeted via replacement therapies like pancrelipase in conditions such as cystic fibrosis or chronic pancreatitis, though high doses pose risks like fibrotic bowel changes.[1] As part of broader lipase families, it exemplifies serine hydrolases critical for digestion across organisms, with industrial microbial analogs used in biocatalysis.[1][2]
Inhibition of interfacial activation at oil-water interface (for some microbial lipases used industrially); Catalytic triad (Ser-His-Asp) hydrolysis of triglycerides requiring colipase cofactor in bile salts; Exogenous lipase supplementation hydrolyzes undigested dietary triglycerides in pancreatic insufficiency
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