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The pancreatic lipase–colipase complex is the primary enzymatic system responsible for the digestion of dietary triacylglycerols in the human small intestine [1, 6]. Pancreatic triacylglycerol lipase (PNLIP) is a member of the lipase family that hydrolyzes triglycerides into 2-monoacylglycerols and free fatty acids [3, 8]. However, its activity is inhibited by bile salts, which are necessary for emulsifying fats [2, 4]. Colipase (CLPS) acts as a crucial protein cofactor that anchors the lipase to the lipid-water interface of bile salt-coated fat droplets, thereby restoring and enhancing its catalytic activity [2, 7]. This complex is a major therapeutic target for the treatment of obesity, where drugs like orlistat covalently inhibit the lipase to reduce fat absorption [10, 13]. Conversely, in conditions like exocrine pancreatic insufficiency, the complex is administered as part of pancreatic enzyme replacement therapy (PERT) to restore normal digestion [8]. Monitoring serum lipase levels is a standard diagnostic biomarker for acute pancreatitis, reflecting the release of the enzyme into the bloodstream during pancreatic injury [3].
Covalent inhibition of the active site serine residue within the lipase subunit to prevent the hydrolysis of dietary fats [1, 10]; or enzyme replacement to restore digestive function in cases of deficiency [8].
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