Other lipase enzymes, such as pancreatic lipases, are secreted into extracellular spaces where they serve to process dietary lipids into more simple forms that can be more easily absorbed and transported throughout the body.
Fungi and bacteria may secrete lipases to facilitate nutrient absorption from the external medium (or in examples of pathogenic microbes, to promote invasion of a new host).
Certain wasp and bee venoms contain phospholipases that enhance the effects of injury and inflammation delivered by a sting.
Some lipases are expressed and secreted by pathogenic organisms during an infection. In particular, Candida albicans has many lipases, possibly reflecting broad-lipolytic activity, which may contribute to the persistence and virulence of C. albicans in human tissue.
Pancreatic lipase related protein 1 is very similar to PLRP2 and PL by amino acid sequence (all three genes probably arose via gene duplication of a single ancestral pancreatic lipase gene). However, PLRP1 is devoid of detectable lipase activity and its function remains unknown, even though it is conserved in other mammals.
In the commercial sphere, lipases are widely used in laundry detergents. Several thousand tons per year are produced for this role.
Lipases are catalysts for hydrolysis of esters and are useful outside of the cell, a testament to their wide substrate scope and ruggedness. The ester hydrolysis activity of lipases has been well evaluated for the conversion of triglycerides into biofuels or their precursors.
Lipases are of course chiral, which means that they can be used for the enantioselective hydrolysis prochiral diesters. Several procedures have been reported for applications in the synthesis of fine chemicals.
Lipases are generally animal sourced, but can also be sourced microbially.
Blood tests for lipase may be used to help investigate and diagnose acute pancreatitis and other disorders of the pancreas. Measured serum lipase values may vary depending on the method of analysis.
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