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Information on EC 3.1.1.3 - triacylglycerol lipase and Organism(s) Thermomyces lanuginosus and UniProt Accession O59952
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3.1.1.3 triacylglycerol lipaseIUBMB Comments
The enzyme is found in diverse organisms including animals, plants, fungi, and bacteria. It hydrolyses triglycerides into diglycerides and subsequently into monoglycerides and free fatty acids. The enzyme is highly soluble in water and acts at the surface of oil droplets. Access to the active site is controlled by the opening of a lid, which, when closed, hides the hydrophobic surface that surrounds the active site. The lid opens when the enzyme contacts an oil-water interface (interfacial activation). The pancreatic enzyme requires a protein cofactor, namely colipase, to counteract the inhibitory effects of bile salts.
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Word Map
- 3.1.1.3
- amylase
- lipoprotein
- pancreas
- triacylglycerols
-
lipolytic
- phospholipid
- antarctica
- esterification
- obesity
- abdominal
- hdl
-
biocatalyst
-
apolipoproteins
- pain
-
exocrine
- adipocytes
-
oleic
- milk
-
cholesteryl
- droplet
- palmitate
- meal
- phosphatidylcholine
-
high-density
- p-nitrophenyl
-
hormone-sensitive
- olive
-
acinar
- duodenal
-
enantioselectivity
-
obese
- hypertriglyceridemia
-
interfacial
-
phosphatidic
-
esterify
-
micelle
- juice
-
arachidonic
-
emulsify
- oleate
-
postprandial
-
endoscopic
- cholecystokinin
-
reusable
- lecithin
- hexane
-
endocannabinoids
-
hdl-cholesterol
- taurocholate
- trypsinogen
- detergent
- synthesis
- paper production
- nutrition
- food industry
- environmental protection
- biofuel production
- medicine
- biotechnology
The taxonomic range for the selected organisms is: Thermomyces lanuginosus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
lipase, acyltransferase, pancreatic lipase, hepatic lipase, adipose triglyceride lipase, cholesterol esterase, lipase b, triglyceride lipase, tgl, diacylglycerol lipase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
amano AP
-
-
-
-
amano B
-
-
-
-
amano CE
-
-
-
-
amano CES
-
-
-
-
amano P
-
-
-
-
amno N-AP
-
-
-
-
BAL
-
-
-
-
Bile-salt-stimulated lipase
-
-
-
-
BSSL
-
-
-
-
butyrinase
-
-
-
-
cacordase
-
-
-
-
CALB
-
-
-
-
capalase L
-
-
-
-
Carboxyl ester lipase
-
-
-
-
cholesterol esterase
-
-
-
-
Cytotoxic T lymphocyte lipase
-
-
-
-
EDL
-
-
-
-
endothelial cell-derived lipase
-
-
-
-
endothelial-derived lipase
-
-
-
-
GA 56 (enzyme)
-
-
-
-
Gastric lipase
-
-
-
-
GEH
-
-
-
-
glycerol ester hydrolase
-
-
-
-
glycerol-ester hydrolase
-
-
-
-
heparin releasable hepatic lipase
-
-
-
-
hepatic lipase
-
-
-
-
hepatic monoacylglycerol acyltransferase
-
-
-
-
Lingual lipase
-
-
-
-
lipase
lipase, triacylglycerol
-
-
-
-
lipazin
-
-
-
-
liver lipase
-
-
-
-
meito MY 30
-
-
-
-
meito Sangyo OF lipase
-
-
-
-
Pancreatic lipase
-
-
-
-
Pancreatic lysophospholipase
-
-
-
-
PGE
-
-
-
-
PL-RP2
-
-
-
-
post-heparin plasma protamine-resistant lipase
-
-
-
-
PPL
-
-
-
-
Pregastric esterase
-
-
-
-
Pregastric lipase
-
-
-
-
salt-resistant post-heparin lipase
-
-
-
-
steapsin
-
-
-
-
Sterol esterase
-
-
-
-
takedo 1969-4-9
-
-
-
-
teenesterase
-
-
-
-
tiacetinase
-
-
-
-
tibutyrin esterase
-
-
-
-
triacylglycerol ester hydrolase
-
-
-
-
Triacylglycerol lipase
-
-
-
-
tributyrase
-
-
-
-
tributyrinase
-
-
-
-
triglyceridase
-
-
-
-
triglyceride hydrolase
-
-
-
-
triglyceride lipase
-
-
-
-
triolein hydrolase
-
-
-
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tween hydrolase
-
-
-
-
tween-hydrolyzing esterase
-
-
-
-
Tweenase
-
-
-
-
lipase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
triacylglycerol + H2O = diacylglycerol + a carboxylate
activity required deprotonation of the catalytic His residue
triacylglycerol + H2O = diacylglycerol + a carboxylate
the catalytic triad consists of Ser, His, and Asp residues, as for serine proteases
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
triacylglycerol acylhydrolase
The enzyme is found in diverse organisms including animals, plants, fungi, and bacteria. It hydrolyses triglycerides into diglycerides and subsequently into monoglycerides and free fatty acids. The enzyme is highly soluble in water and acts at the surface of oil droplets. Access to the active site is controlled by the opening of a lid, which, when closed, hides the hydrophobic surface that surrounds the active site. The lid opens when the enzyme contacts an oil-water interface (interfacial activation). The pancreatic enzyme requires a protein cofactor, namely colipase, to counteract the inhibitory effects of bile salts.
CAS REGISTRY NUMBER
COMMENTARY
9001-62-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
enzyme does not possess protease activity and does not hydrolyze peptide bonds, no activity with N-benzoyl-L-tyrosine 4-nitroanilide
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
palm olein water content above 3.6% (v/v) inhibits the activity of lipase
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km-value: 14.2 mg/ml for trilaurin
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
broad optimum, influence of pH on catalytic mechanism, overview
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10.5
pH profile, the enzyme is active under acidic conditions and shows 70.6% of maximal activity at pH 4.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LIP_THELA
291
0
31807
Swiss-Prot
Secretory Pathway (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
conversion of plant oil to 92-97% of biodiesel is feasible at 1% enzyme load (24 h, 35°C) using the feedstocks containing 2-20% of water, 0-10% of glycerol, 0-20% of free fatty acids. The enzyme can be collected in a narrow white layer settled between biodiesel and glycerol-water phases,containing also free fatty acids and monoglycerides. The lipase can be then reused after compensation for 5-10% loss of the enzyme. The main contaminants in the produced biodiesel are free fatty acids (2-6%) and monoglycerides (1-3%). Major amounts of free fatty acids and monoglycerides are removed after brief mixing of biodiesel with alkali (2-5% of 5 M NaOH) and centrifugation
synthesis
-
ethanolysis of soybean oil in a solvent-free system for synthesis of biodiesel. The optimal conditions are: 31.5°C, 7 h reaction time, substrate molar ratio 7.5:1 ethanol:soybean oil, enzyme content 15% (g enzyme/g oil), 4% added water/g oil. The experimental yield conversion is 96%
synthesis
-
immobilization and stabilization of lipase on aldehyde-Lewatit. Over 90% of lipase activity is recovered after the immobilization, the immobilized enzyme is 10fold more thermostable than the commercial preparation, Lipozyme TL-IM. The stabilized preparation catalyzes enzymatic transesterification of ethanol and soybean oil. With 7.5:1 molar ratio of ethanol:soybean oil, 15% immobilized enzyme and 4% water at 30°C in the presence of n-hexane, the transesterification reaches 100% conversion, while in solvent-free system the yield is 75%. At stoichiometric molar ratio, the yield is 70% conversion after 10 h of reaction in both systems. A two step ethanolysis produces 100% conversion after 10 h of reaction in both solvent and solvent-free systems
synthesis
-
solubilization in sodium bis-(2-ethylhexyl)sulfosuccinate-stabilized water-in-oil microemulsions in n-heptane and analysis of hydrolysis and condensation activity. Condensation activity is essentially independent of temperature over the range 5 to 37°C. The stability over a 30-day period is very good at all pH levels (6.1, 7.2, 9.3) and R values studied (5, 7.5, 10, 20), except when high pHs and low R values are combined
synthesis
-
synthesis of biodiesel from canola oil. Enzyme immobilized on epoxy-functionalized silica reaches to 100% yield at 10% tert-butanol. Presence of water significantly increases fatty acid methyl ester yield. 95% residual activity after 16 reaction cycles
synthesis
-
synthesis of biodiesel from palm olein by ethanolysis using protein-coated microcrystals. Addition of tert-butanol markedly increases the biocatalyst activity and stability. Optimized reactions (20%, w/w protein-coated microcrystal-lipase to triacylglycerol and 1:4 fatty acid equivalence/ethanol molar ratio) lead to the production of alkyl esters from palm olein at 89.9% yield on molar basis after incubation at 45°C for 24 h in the presence of tert-butanol at a 1:1 molar ratio to triacylglycerol. Crude palm oil and palm fatty acid distillate are also converted to biodiesel with 82.1 and 75.5% yield, respectively
synthesis
-
use of enzyme as biocatalyst to obtain a second generation biodiesel-like biofuel by the conversion of sunflower oil into a blend of fatty acid ethyl esters (FAEE), monoacylglycerols (MG) and diacylglycerols (DG). pH, molar ratio of ethanol to oil and water content influence the conversion in the systems. Low temperatures (20°C), high pH values (close to 12), and an oil/ethanol volume ratios of 3.4/1 provide conversions around 70% and kinematic viscosities about 8.5 mm2/s after 1 h reaction
synthesis
-
use of enzyme immobilized on styrene-divinylbenzene beads for the synthesis of butyl butanoate using n-hexane as solvent. The enzyme presents high initial reaction rates up to 1.0 M butanoic acid, and allows a productivity of 14.5 mmol/g/h
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Che Omar, I.; Hayashi, M.; Nagai, S.
Purification and some properties of a thermostable lipase from Humicola lanuginosa No. 3
Agric. Biol. Chem.
51
37-45
1987
Thermomyces lanuginosus, Thermomyces lanuginosus No. 3
-
Maruyama, T.; Nakajima, M.; Kondo, H.; Kawasaki, K.; Seki, M.; Goto, M.
Can lipases hydrolyze a peptide bond?
Enzyme Microb. Technol.
32
655-657
2003
Bacillus subtilis, Diutina rugosa, Fusarium solani, Homo sapiens, Thermomyces lanuginosus, Rhizomucor miehei, Rhizopus arrhizus, Rhizopus japonicus, Sus scrofa, Chromobacterium viscosum, Alcaligenes ssp., Bacillus subtilis 168 BsL
-
Poulsen, K.R.; Snabe, T.; Petersen, E.I.; Fojan, P.; Neves-Petersen, M.T.; Wimmer, R.; Petersen, S.B.
Quantization of pH: evidence for acidic activity of triglyceride lipases
Biochemistry
44
11574-11580
2005
Fusarium solani, Rhizomucor miehei, Thermomyces lanuginosus (O59952), Thermomyces lanuginosus, Burkholderia cepacia (P22088), Burkholderia cepacia
Chew, Y.H.; Chua, L.S.; Cheng, K.K.; Sarmidi, M.R.; Aziz, R.A.; Lee, C.T.
Kinetic study on the hydrolysis of palm olein using immobilized lipase
Biochem. Eng. J.
39
516-520
2008
Thermomyces lanuginosus
-
Martins, A.B.; Friedrich, J.L.; Cavalheiro, J.C.; Garcia-Galan, C.; Barbosa, O.; Ayub, M.A.; Fernandez-Lafuente, R.; Rodrigues, R.C.
Improved production of butyl butyrate with lipase from Thermomyces lanuginosus immobilized on styrene-divinylbenzene beads
Biores. Technol.
134
417-422
2013
Thermomyces lanuginosus
Crooks, G.E.; Rees, G.D.; Robinson, B.H.; Svensson, M.; Stephenson, G.R.
Comparison of hydrolysis and esterification behavior of Humicola lanuginosa and Rhizomucor miehei lipases in AOT-stabilized water-in-oil microemulsions II. Effect of temperature on reaction kinetics and general considerations of stability and productivit
Biotechnol. Bioeng.
48
190-196
1995
Thermomyces lanuginosus, Rhizomucor miehei (P19515), Rhizomucor miehei
Verdugo, C.; Luna, D.; Posadillo, A.; Sancho, E.; Rodriguez, S.; Bautista, F.; Luque, R.; Marinas, J.; Romero, A.
Production of a new second generation biodiesel with a low cost lipase derived from Thermomyces lanuginosus Optimization by response surface methodology
Catal. Today
167
107-112
2011
Thermomyces lanuginosus
-
Rodrigues, R.; Volpato, G.; Ayub, M.; Wada, K.
Lipase-catalyzed ethanolysis of soybean oil in a solvent-free system using central composite design and response surface methodology
J. Chem. Technol. Biotechnol.
83
849-854
2008
Thermomyces lanuginosus
-
Babaki, M.; Yousefi, M.; Habibi, Z.; Mohammadi, M.; Brask, J.
Effect of water, organic solvent and adsorbent contents on production of biodiesel fuel from canola oil catalyzed by various lipases immobilized on epoxy-functionalized silica as low cost biocatalyst
J. Mol. Catal. B
120
93-99
2015
Moesziomyces antarcticus, Thermomyces lanuginosus, Rhizomucor miehei
-
Firdaus, M.; Brask, J.; Nielsen, P.; Guo, Z.; Fedosov, S.
Kinetic model of biodiesel production catalyzed by free liquid lipase from Thermomyces lanuginosus
J. Mol. Catal. B
133
55-64
2016
Thermomyces lanuginosus
-
Rodrigues, R.; Pessela, B.; Volpato, G.; Fernandez-Lafuente, R.; Guisan, J.; Ayub, M.
Two step ethanolysis A simple and efficient way to improve the enzymatic biodiesel synthesis catalyzed by an immobilized-stabilized lipase from Thermomyces lanuginosus
Process Biochem.
45
1268-1273
2010
Thermomyces lanuginosus
-
Raita, M.; Champreda, V.; Laosiripojana, N.
Biocatalytic ethanolysis of palm oil for biodiesel production using microcrystalline lipase in tert-butanol system
Process Biochem.
45
829-834
2010
Thermomyces lanuginosus
-
EXTERNAL LINKS (specific for EC-Number 3.1.1.3)
Transporter Classification Database (TCDB): 8.A.178.1.1, 1.A.115.1.1
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