Lipases are involved in diverse biological processes which range from routine metabolism ofdietarytriglycerides tocell signaling[12] andinflammation.[13] Thus, some lipase activities are confined to specific compartments withincells while others work in extracellular spaces.
Other lipase enzymes, such aspancreatic lipases, are secreted intoextracellular 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 containphospholipases that enhance the effects of injury and inflammation delivered by a sting.
Some lipases are expressed and secreted by pathogenic organisms during aninfection. In particular,Candida albicans has many lipases, possibly reflecting broad-lipolytic activity, which may contribute to the persistence and virulence ofC. albicansin human tissue.[17]
Pancreatic lipase related protein 1 is very similar to PLRP2 and PL by amino acid sequence (all three genes probably arose viagene 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 othermammals.[22][23]
In the commercial sphere, lipases are widely used in laundry detergents. Several thousand tons per year are produced for this role.[4]
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.[24][25][26][27]
Lipases are chiral, which means that they can be used for the enantioselective hydrolysis prochiral diesters.[28] Several procedures have been reported for applications in the synthesis of fine chemicals.[29][30][31]
Lipases are generally animal sourced, but can also be sourced microbially.[citation needed]
Blood tests for lipase may be used to help investigate and diagnoseacute pancreatitis and other disorders of the pancreas.[32] Measured serum lipase values may vary depending on the method of analysis.[citation needed]
^Brady, L.; A. M. Brzozowski; Z. S. Derewenda; E. Dodson; G. Dodson; S. Tolley; J. P. Turkenburg; L. Christiansen; B. Huge-Jensen; L. Norskov; et al. (1990). "A serine protease triad forms the catalytic centre of a triacylglycerol lipase".Nature.343 (6260):767–70.Bibcode:1990Natur.343..767B.doi:10.1038/343767a0.PMID2304552.S2CID4308111.
^Girod A, Wobus C, Zádori Z, Ried M, Leike K, Tijssen P, Kleinschmidt J, Hallek M (2002). "The VP1 capsid protein of adeno-associated virus type 2 is carrying a phospholipase A2 domain required for virus infectivity".J Gen Virol.83 (Pt 5):973–8.doi:10.1099/0022-1317-83-5-973.PMID11961250.
^Hube B, Stehr F, Bossenz M, Mazur A, Kretschmar M, Schafer W (2000). "Secreted lipases of Candida albicans: cloning, characterisation and expression analysis of a new gene family with at least ten members".Arch. Microbiol.174 (5):362–374.Bibcode:2000ArMic.174..362H.doi:10.1007/s002030000218.PMID11131027.S2CID2231039.
^Gilbert B, Rouis M, Griglio S, de Lumley L, Laplaud P (2001). "Lipoprotein lipase (LPL) deficiency: a new patient homozygote for the preponderant mutation Gly188Glu in the human LPL gene and review of reported mutations: 75 % are clustered in exons 5 and 6".Ann Genet.44 (1):25–32.doi:10.1016/S0003-3995(01)01037-1.PMID11334614.
^De Caro J, Carriere F, Barboni P, Giller T, Verger R, De Caro A (1998). "Pancreatic lipase-related protein 1 (PLRP1) is present in the pancreatic juice of several species".Biochim Biophys Acta.1387 (1–2):331–41.doi:10.1016/S0167-4838(98)00143-5.PMID9748646.
^Gupta R, Gupta N, Rathi P (2004). "Bacterial lipases: an overview of production, purification and biochemical properties".Appl Microbiol Biotechnol.64 (6):763–81.doi:10.1007/s00253-004-1568-8.PMID14966663.S2CID206934353.
^Ban K, Kaieda M, Matsumoto T, Kondo A, Fukuda H (2001). "Whole cell biocatalyst for biodiesel fuel production utilizingRhizopus oryzae cells immobilized within biomass support particles".Biochem Eng J.8 (1):39–43.Bibcode:2001BioEJ...8...39B.doi:10.1016/S1369-703X(00)00133-9.PMID11356369.
^Harding, K.G; Dennis, J.S; von Blottnitz, H; Harrison, S.T.L (2008). "A life-cycle comparison between inorganic and biological catalysis for the production of biodiesel".Journal of Cleaner Production.16 (13):1368–78.Bibcode:2008JCPro..16.1368H.doi:10.1016/j.jclepro.2007.07.003.
^Guo Z, Xu X (2005). "New opportunity for enzymatic modification of fats and oils with industrial potentials".Org Biomol Chem.3 (14):2615–9.doi:10.1039/b506763d.PMID15999195.
^Theil, Fritz (1995). "Lipase-Supported Synthesis of Biologically Active Compounds".Chemical Reviews.95 (6):2203–2227.doi:10.1021/cr00038a017.
^P. Kalaritis, R. W. Regenye (1990). "Enantiomerically Pure Ethyl (R)- And (S)- 2-Fluorohexanoate by Enzyme-Catalyzed Kinetic Resolution".Org. Synth.69: 10.doi:10.15227/orgsyn.069.0010.
^Leo A. Paquette, Martyn J. Earle, Graham F. Smith (1996). "(4R)-(+)-tert-Butyldimethylsiloxy-2-cyclopenten-1-one".Org. Synth.73: 36.doi:10.15227/orgsyn.073.0036.{{cite journal}}: CS1 maint: multiple names: authors list (link)
25. Gulzar, Bio-degradation of hydrocarbons using different bacterial and fungal species. Published in international conference on biotechnology and neurosciences. CUSAT (cochin university of science and technology), 2003
