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Lipase

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Lipase
A computer-generated image of a type of pancreatic lipase (PLRP2) from the guinea pig. PDB: 1GPL​
Pronunciation/ˈlaɪpeɪs, ˈlaɪpeɪz/ LY-payss, LY-payz
Test ofPancreatitis
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Lipases are a type of enzyme that break down fats. More specifically, lipases use water (as hydrolases) to remove fatty acids from fat molecules, especially triglycerides[1][2][3] or its derivatives.[4][5] In humans and other animals, lipases have a variety of roles in the body, from helping digest dietary fats like pancreatic lipase,[6] to synthesizing fat-based hormones like diglyceride lipases.[4]

What counts as a lipase is not consistently defined across sources,[7][6] and some only consider enzymes to be lipases if they are activated by oil-water interfaces.[7]

Many specific lipases can also catalyze other reactions. For example, carboxyl ester lipase is able to remove fatty acids that are attached to cholesterol, while endothelial lipase can remove fatty acids from phospholipids (a major component of cell membranes).[6]

Structure and catalytic mechanism

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Classically, lipases catalyse the hydrolysis of triglycerides:[citation needed]

Lipases are serine hydrolases, i.e. they function by transesterification generating an acyl serine intermediate. Most lipases act at a specific position on the glycerol backbone of a lipid substrate (A1, A2 or A3). For example, human pancreatic lipase (HPL),[8] converts triglyceride substrates found in ingested oils to monoglycerides and two fatty acids.

A diverse array of genetically distinct lipase enzymes are found in nature, and they represent several types of protein folds and catalytic mechanisms. However, most are built on an alpha/beta hydrolase fold[9][10][11][12] and employ a chymotrypsin-like hydrolysis mechanism using a catalytic triad consisting of a serine nucleophile, a histidine base, and an acid residue, usually aspartic acid.[13][14]

Physiological distribution

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Lipases are involved in diverse biological processes which range from routine metabolism of dietary triglycerides to cell signaling[15] and inflammation.[16] Thus, some lipase activities are confined to specific compartments within cells while others work in extracellular spaces.

  • In the example of lysosomal lipase, the enzyme is confined within an organelle called the lysosome.
  • 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.
  • As biological membranes are integral to living cells and are largely composed of phospholipids, lipases play important roles in cell biology.
  • Malassezia globosa, a fungus thought to be the cause of human dandruff, uses lipase to break down sebum into oleic acid and increase skin cell production, causing dandruff.[17]

Genes encoding lipases are even present in certain viruses.[18][19]

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.[20]

Human lipases

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NameGeneLocationDescriptionMutation-caused Disorder(s)
gastric lipaseLIPFgastric juiceDigestive enzyme produced in the stomach. Functions in the infant at a near-neutral pH to aid in the digestion of lipids–
pancreatic lipasePNLIPpancreatic juiceDigestive enzyme which is the main enzyme that breaks down triglycerides and diglycerides in the human digestive system, mainly producing monoglycerides and free fatty acids.[8] Requires the protein colipase for optimal efficiency.[21]Pancreatic lipase deficiency (PNLIPD)[22]
bile salt-dependent lipaseCEL or "BSDL"pancreatic juice, breast milkDigestive enzyme with a broader range of target molecules compared to PNLIP. It's the main enzyme that breaks down cholesterol esters and is also responsible for up to 40% of the break down of monoglycerides.[6][23] Maturity-onset diabetes of the young, type 8 (MODY8)[24]
lysosomal lipaseLIPAinterior space of organelle: lysosomeAlso referred to as lysosomal acid lipase (LAL or LIPA) or acid cholesteryl ester hydrolaseCholesteryl ester storage disease (CESD) and Wolman disease[25]
hepatic lipaseLIPCendotheliumHepatic lipase acts on the remaining lipids carried on lipoproteins in the blood to regenerate LDL (low density lipoprotein).Hepatic lipase deficiency[26]
lipoprotein lipaseLPL or "LIPD"endotheliumLipoprotein lipase functions in the blood to act on triacylglycerides carried on VLDL (very low density lipoprotein) so that cells can take up the freed fatty acids.Lipoprotein lipase deficiency[27][28]
endothelial lipaseLIPGendotheliumFunctions more strongly as a phospholipase than a triglyceride lipase. Preferentially breaks down High Density Lipoproteins (HDL) compared to other lipoproteins.[29]–
adipose triglyceride lipase PNPLA2intracellularBreaks down triglycerides in adipocytes, initializing first step of lipolysis.[30]Neutral lipid storage disease[30]
hormone-sensitive lipaseLIPEintracellularPreferentially breaks down diglycerides. Functions to extract free fatty acids from stored fats in adipocytes. Also involved in the production of steroid hormones by converting cholesterol esters to free cholesterol.[31]Lipodystrophy[31]
pancreatic lipase related protein 2PNLIPRP2 or "PLRP2"pancreatic juiceCan function as both a lipase and a galactolipase, but gene is frequently broken in certain ethnicities (30-50% of alleles).[32]–

Other traditional triglyceride lipases (EC 3.1.1.3) include Lipase member N, DDHD2, PNLIPRP3, PNPLA4, and PNPLA5.[1] In addition, there are various other non-traditional lipases including Monoacylglycerol lipases (eg: MGLL, ABHD2, and ABHD6),[5] and Diacylglycerol lipases (eg: DAGLA, DAGLB, and ABHD11).[4]

Not all lipase-family proteins function as lipases in humans. Some like Lipase member H and Lipase member I function as phospholipases,[33][34] while others like pancreatic lipase related protein 1 (PNLIPRP1),[35] LIPJ,[36] LIPK,[37] and LIPM[38] do not (yet) have a well established function as an enzyme.

Uses

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In the commercial sphere, lipases are widely used in laundry detergents. Several thousand tons per year are produced for this role.[7]

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.[39][40][41][42]

Lipases are chiral, which means that they can be used for the enantioselective hydrolysis prochiral diesters.[43] Several procedures have been reported for applications in the synthesis of fine chemicals.[44][45][46]

Lipases are generally animal sourced, but can also be sourced microbially.[citation needed]

Biomedicine

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Blood tests for lipase may be used to help investigate and diagnose acute pancreatitis and other disorders of the pancreas.[47] Measured serum lipase values may vary depending on the method of analysis.[citation needed]

In patients with exocrine pancreatic insufficiency, pancreatic enzyme replacement therapy (PERT) is used to replace the various enzymes that are produced by the pancreas the supplementation of pancreatic enzymes to treat. Enzyme mixtures used for PERT will include lipase, amylase, and protease.[48]

See also

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References

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  1. 1 2 "ENZYME entry: EC 3.1.1.3". enzyme.expasy.org. SIB Swiss Institute of Bioinformatics. Retrieved 2026-09-04.
  2. ↑ "ENZYME entry: EC 3.1.1.34". enzyme.expasy.org. SIB Swiss Institute of Bioinformatics. Retrieved 2026-09-04.
  3. ↑ "ENZYME entry: EC 3.1.1.79". enzyme.expasy.org. SIB Swiss Institute of Bioinformatics. Retrieved 2026-09-04.
  4. 1 2 3 "ENZYME entry: EC 3.1.1.116". enzyme.expasy.org. SIB Swiss Institute of Bioinformatics. Retrieved 2026-09-04.
  5. 1 2 "ENZYME entry: EC 3.1.1.23". enzyme.expasy.org. SIB Swiss Institute of Bioinformatics. Retrieved 2026-09-04.
  6. 1 2 3 4 Lim SY, Steiner JM, Cridge H (2022-08-01). "Lipases: it's not just pancreatic lipase!". American journal of veterinary research. 83 (8). doi:10.2460/ajvr.22.03.0048.
  7. 1 2 3 Sharma, Rohit; Chisti, Yusuf; Banerjee, Uttam Chand (2001). "Production, purification, characterization, and applications of lipases". Biotechnology Advances. 19 (8): 627–662. doi:10.1016/S0734-9750(01)00086-6. PMID 14550014. S2CID 18615547.
  8. 1 2 Winkler FK; D'Arcy A; W Hunziker (1990). "Structure of human pancreatic lipase". Nature. 343 (6260): 771–774. Bibcode:1990Natur.343..771W. doi:10.1038/343771a0. PMID 2106079. S2CID 37423900.
  9. ↑ Winkler FK; D'Arcy A; W Hunziker (1990). "Structure of human pancreatic lipase". Nature. 343 (6260): 771–774. Bibcode:1990Natur.343..771W. doi:10.1038/343771a0. PMID 2106079. S2CID 37423900.
  10. ↑ Schrag J, Cygler M (1997). "Lipases and hydrolase fold". Lipases, Part A: Biotechnology. Methods in Enzymology. Vol. 284. pp. 85–107. doi:10.1016/S0076-6879(97)84006-2. ISBN 978-0-12-182185-2. PMID 9379946.
  11. ↑ Egmond, M. R.; C. J. van Bemmel (1997). "Impact of structural information on understanding lipolytic function". Lipases, Part A: Biotechnology. Methods in Enzymology. Vol. 284. pp. 119–129. doi:10.1016/S0076-6879(97)84008-6. ISBN 978-0-12-182185-2. PMID 9379930.
  12. ↑ Withers-Martinez C; Carriere F; Verger R; Bourgeois D; C Cambillau (1996). "A pancreatic lipase with a phospholipase A1 activity: crystal structure of a chimeric pancreatic lipase-related protein 2 from guinea pig". Structure. 4 (11): 1363–74. doi:10.1016/S0969-2126(96)00143-8. PMID 8939760.
  13. ↑ 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. PMID 2304552. S2CID 4308111.
  14. ↑ Lowe ME (1992). "The catalytic site residues and interfacial binding of human pancreatic lipase". J Biol Chem. 267 (24): 17069–73. doi:10.1016/S0021-9258(18)41893-5. PMID 1512245.
  15. ↑ Spiegel S; Foster D; R Kolesnick (1996). "Signal transduction through lipid second messengers". Current Opinion in Cell Biology. 8 (2): 159–67. doi:10.1016/S0955-0674(96)80061-5. PMID 8791422.
  16. ↑ Tjoelker LW; Eberhardt C; Unger J; Trong HL; Zimmerman GA; McIntyre TM; Stafforini DM; Prescott SM; PW Gray (1995). "Plasma platelet-activating factor acetylhydrolase is a secreted phospholipase A2 with a catalytic triad". J Biol Chem. 270 (43): 25481–7. doi:10.1074/jbc.270.43.25481. PMID 7592717.
  17. ↑ Genetic Code of Dandruff Cracked – BBC News
  18. ↑ Afonso C, Tulman E, Lu Z, Oma E, Kutish G, Rock D (1999). "The Genome of Melanoplus sanguinipes Entomologists". J Virol. 73 (1): 533–52. doi:10.1128/JVI.73.1.533-552.1999. PMC 103860. PMID 9847359.
  19. ↑ 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. PMID 11961250.
  20. ↑ 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. PMID 11131027. S2CID 2231039.
  21. ↑ Lowe ME (2002). "The triglyceride lipases of the pancreas". J Lipid Res. 43 (12): 2007–16. doi:10.1194/jlr.R200012-JLR200. PMID 12454260.
  22. ↑ "P16233 · LIPP_HUMAN". uniprot.org. UniProt consortium. Retrieved 2026-09-06.
  23. ↑ Lombardo, Dominique (2001). "Bile salt-dependent lipase: its pathophysiological implications". Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1533 (1): 1–28. doi:10.1016/S1388-1981(01)00130-5. PMID 11514232.
  24. ↑ "MATURITY-ONSET DIABETES OF THE YOUNG, TYPE 8, WITH EXOCRINE DYSFUNCTION; MODY8". omim.org. Johns Hopkins University. Retrieved 2026-09-06.
  25. ↑ Omim – Wolman Disease
  26. ↑ "HEPATIC LIPASE DEFICIENCY". omim.org. Johns Hopkins University. Retrieved 2026-09-06.
  27. ↑ Familial lipoprotein lipase deficiency – Genetics Home Reference[link removed]
  28. ↑ 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. PMID 11334614.
  29. ↑ "Q9Y5X9 · LIPG_HUMAN". uniprot.org. UniProt consortium. Retrieved 2026-09-06.
  30. 1 2 "Q96AD5 · PLPL2_HUMAN". uniprot.org. UniProt consortium. Retrieved 2026-09-06.
  31. 1 2 "Q05469 · LIPS_HUMAN". uniprot.org. UniProt consortium. Retrieved 2026-09-06.
  32. ↑ Zhu G, Fang Q, Zhu F, Huang D, Yang C (2021-07-05). "Structure and function of pancreatic lipase-related protein 2 and its relationship with pathological states". Frontiers in Genetics. 12. doi:10.3389/fgene.2021.693538. PMC 8287333.
  33. ↑ "Lipase member H". uniprot.org. UniProt consortium. Retrieved 2026-09-10.
  34. ↑ "Lipase member I". uniprot.org. UniProt consortium. Retrieved 2026-09-10.
  35. ↑ "Inactive pancreatic lipase-related protein 1". uniprot.org. UniProt consortium. Retrieved 2026-09-10.
  36. ↑ "Lipase member J". uniprot.org. UniProt consortium. Retrieved 2026-09-10.
  37. ↑ "Lipase member K". uniprot.org. UniProt consortium. Retrieved 2026-09-10.
  38. ↑ "Lipase member M". uniprot.org. UniProt consortium. Retrieved 2026-09-10.
  39. ↑ 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. PMID 14966663. S2CID 206934353.
  40. ↑ Ban K, Kaieda M, Matsumoto T, Kondo A, Fukuda H (2001). "Whole cell biocatalyst for biodiesel fuel production utilizing Rhizopus 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. PMID 11356369.
  41. ↑ 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.
  42. ↑ 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. PMID 15999195.
  43. ↑ Theil, Fritz (1995). "Lipase-Supported Synthesis of Biologically Active Compounds". Chemical Reviews. 95 (6): 2203–2227. doi:10.1021/cr00038a017.
  44. ↑ 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.
  45. ↑ 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)
  46. ↑ "(4R)-(+)-tert-BUTYLDIMETHYLSILOXY-2-CYCLOPENTEN-1-ONE". Organic Syntheses. 73: 36. 1996. doi:10.15227/orgsyn.073.0036.
  47. ↑ "Lipase – TheTest". Lab Tests Online. Retrieved 12 May 2014.
  48. ↑ Venkatesh, Priyanka; Kasi, Anup (2026), "Pancrelipase Therapy", StatPearls, Treasure Island (FL): StatPearls Publishing, PMID 30521237, retrieved 2026-06-17

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

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