lipasas

Lipases are a family of enzymes that catalyze the hydrolysis of triglycerides into glycerol and free fatty acids. They are serine hydrolases found in many organisms, from bacteria to humans, and play central roles in lipid digestion, transport, and metabolism.

Most lipases share a catalytic triad of serine, histidine, and aspartate within an alpha/beta hydrolase fold. They often possess a lid domain that covers the active site and enables interfacial activation, becoming active when in contact with lipid–water interfaces. The canonical reaction is the hydrolysis of ester bonds at the sn-1 and sn-3 positions of triglycerides, producing di- and monoacylglycerols and free fatty acids; water participates to complete the reaction.

Major physiological lipases include pancreatic lipase, secreted by the pancreas into the small intestine where bile salts and colipase support digestion of dietary fats; gastric lipase, active in the stomach; lipoprotein lipase, anchored to capillary endothelium and hydrolyzing triglycerides in circulating lipoproteins; and hepatic lipase, acting on intermediate-density and high-density lipoproteins.

Clinically, serum lipase is a diagnostic marker for pancreatitis. Lipase activity can be inhibited by compounds such as orlistat, used to reduce fat absorption in obesity treatment. Industrially, lipases are employed in detergents, food processing, and biodiesel production, owing to their ability to operate under mild conditions and with diverse lipid substrates.

Microbial lipases from species such as Candida rugosa and Thermomyces lanuginosus are widely used in biotechnological applications due to stability and substrate versatility.