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Information on EC 3.1.1.3 - triacylglycerol lipase and Organism(s) Rhizomucor miehei and UniProt Accession P19515
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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: Rhizomucor miehei
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
-
-
-
-
tween hydrolase
-
-
-
-
tween-hydrolyzing esterase
-
-
-
-
Tweenase
-
-
-
-
lipase
-
-
-
-
triglyceride lipase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
triacylglycerol + H2O = diacylglycerol + a carboxylate
Phe94 is involved in substrate binding and is responsible for accommodating the acyl chain length of the substrate
-
triacylglycerol + H2O = diacylglycerol + a carboxylate
the catalytic triad consists of Ser, His, and Asp residues, as for serine proteases, enzyme contains the alpha-helical lid structure
-
triacylglycerol + H2O = diacylglycerol + a carboxylate
activity required deprotonation of the catalytic His residue
-
triacylglycerol + H2O = diacylglycerol + a carboxylate
ping pong bi bi kinetic mechanism
-
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
(4S)-4-tert-butyl-2-phenyl-1,3-oxazol-5(4H)-one + butanol
butyl (2S)-2-(benzoylamino)3,3-dimethylbutanoate
-
-
-
-
?
1,2-O-dilauryl-rac-glycero-3-glutaric acid resorufin ester + H2O
?
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
low activity
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
low activity
-
?
4-nitrophenyl tetradecanoate + H2O
4-nitrophenol + tetradecanoate
-
best 4-nitrophenyl ester substrate for wild-type enzyme and mutant F94R
-
?
glycerol + (R)-mandelic acid methyl ester + H2O
?
-
about 300fold lower activity compared to phenylpropionic acid ethyl ester
-
-
?
glycerol + (S)-mandelic acid methyl ester + H2O
?
-
about 300fold lower activity compared to phenylpropionic acid ethyl ester
-
-
?
glycerol + phenylacetic acid methyl ester + H2O
?
-
about 5fold lower activity compared to phenylpropionic acid ethyl ester
-
-
?
glycerol + phenylmalonic acid dimethyl ester + H2O
glyceryl monomethylphenylmalonate + ethanol
-
about 5fold lower activity compared to phenylpropionic acid ethyl ester
-
-
?
glycerol + phenylpropionic acid ethyl ester + H2O
glyceryl phenylpropionic ester + ethanol
-
the immobilized lipase exhibits the highest activity towards phenylpropionic acid ethyl ester. 90% of glycerol is the optimum amount to perform the transesterification reaction
the maximum product yield is achieved after 4 h (78%)
-
?
trioleoylglycerol + succinic acid
1,2-dioleoyl-3-succinoylglycerol + 2-oleoyl-1,3-succinoylglycerol
-
-
-
-
?
tripalmitoylglycerol + succinic acid
1,2-dipalmitoyl-3-succinoylglycerol + 2-palmitoyl-1,3-disuccinoylglycerol
-
-
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
-
low activity
-
?
tributyrin + H2O
dibutyrin + butyrate
-
best triacylglyceride substrate for the wild-type enzyme
-
?
additional information
?
-
-
enzyme does not possess protease activity and does not hydrolyze peptide bonds, no activity with N-benzoyl-L-tyrosine 4-nitroanilide
-
?
additional information
?
-
-
immobilized enzyme performs the transesterification reaction that replaces pamitic acid in palm oil with stearic acid
-
?
additional information
?
-
-
substrate chain length specificity of wild-type and mutant enzymes
-
?
additional information
?
-
-
synthesis of pentyl butanoate using two-step addition of acid substrate with immobilized lipase, overview, substrate polarity has an effect on the lipase-catalyzed synthesis of aroma esters in solvent-free systems, solvent-free synthesis enzyme inactivation by acid substrate
-
-
?
NATURAL SUBSTRATE
NATURAL 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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Triton X-100
-
enhances the enzyme production in vivo by 50fold compared to olive oil alone in the medium
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
34.04
benzoic acid
-
chitosan-chitin nanowhiskers supported lipase, pH not specified in the publication, 50°C
138.28
eugenol
-
chitosan-chitin nanowhiskers supported lipase, pH not specified in the publication, 50°C
1.53
4-nitrophenyl octanoate
mutant T18K/T22I/S56C/N63C/V189C/E230I/D238C, pH 8.0, 60°C
2.01
4-nitrophenyl octanoate
mutant T18K/T22I/E230I, pH 8.0, 55°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.67
eugenol
-
chitosan-chitin nanowhiskers supported lipase, pH not specified in the publication, 50°C
42.34
4-nitrophenyl octanoate
mutant T18K/T22I/E230I, pH 8.0, 55°C
43.71
4-nitrophenyl octanoate
mutant T18K/T22I/S56C/N63C/V189C/E230I/D238C, pH 8.0, 60°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
21.1
4-nitrophenyl octanoate
mutant T18K/T22I/E230I, pH 8.0, 55°C
28.6
4-nitrophenyl octanoate
mutant T18K/T22I/S56C/N63C/V189C/E230I/D238C, pH 8.0, 60°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
438.6
eugenol
-
chitosan-chitin nanowhiskers supported lipase, pH not specified in the publication, 50°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10.5
-
pH profile, the enzyme is active under acidic conditions and shows 22.4% of maximal activity at pH 4.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
60
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_RHIMI
363
1
39602
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization at a concentration of 26.0 mg/ml and 2.0 M sodium phosphate at pH 4.9 by the batch technique or with 10.0 mg/ml protein and 2.8 M phosphate at pH 7.8 using the hanging drop technique. Both crystallization conditions give isomorphous crystals during 2-4 weeks and room temperature
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F94E
-
site-directed mutagenesis, altered substrate chain length specificity
F94Q
-
site-directed mutagenesis, altered substrate chain length specificity
F94R
-
site-directed mutagenesis, altered substrate chain length specificity
T18K/T22I/E230I
thermostable mutant, melting temperature is 10 degrees higher than wild-type
T18K/T22I/S56C/N63C/V189C/E230I/D238C
thermostable mutant, residues S56C/N63C and V189C/D238C may form additional disulfide bonds. Melting temperature is 14.3 degrees higher than wild-type and half-life at 70°C is 12.5fold increased
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
120 min, 13% residual activity for wild-type, 95% for mutant T18K/T22I/E230I
70
wild-type, half-life 2.2 min, mutant T18K/T22I/S56C/N63C/V189C/E230I/D238C, half-life 27.5 min
73
melting temperature, mutant T18K/T22I/S56C/N63C/V189C/E230I/D238C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
when the lipase is immobilized in hydroxy(propylmethyl) cellulose gels it retains its activity from 20-65°C independently of the microemulsion used, in the case of agar microemulsion-based organogels the enzyme loses its activity above 50°C, either partly (20% loss in respect to the maximum activity observed for lecithin-agar gels) or completely (100% loss for AOT-agar gels)
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
subcloning of plasmids encoding mutant enzymes in Escherichia coli XLIB, expression of mutants in Pichia pastoris GS115
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
solubilization in sodium bis-(2-ethylhexyl)sulfosuccinate-stabilized water-in-oil microemulsions in n-heptane and analysis of hydrolysis and condensation activity. Esterification activity shows only a slight dependence on temperature over the studied range and an apparent activation energy of 20 kJ/mol for octyl decanoate synthesis. The enzyme shows good stability over a 30-day period in R = 7.5 and R = 10 microemulsions, pH 6.1
synthesis
synthesis
-
immobilized enzyme is used for the transesterification reaction that replaces pamitic acid in palm oil with stearic acid
synthesis
-
production of (S)-ester amide, which is useful as a lipophilic, hindered component of peptides. The amino acids are also useful building blocks for a number of chiral auxiliaries and ligands
synthesis
-
the lipase from Rhizomucor miehei may be used as a means to prepare fatty acid concentrates rich in docosahexaenoic acid
synthesis
-
synthesis of biodiesel by Rhizomucor miehei lipase immobilized on macroporous anion exchange resins using an ethanolysis process of sunflower oil. Quantitative conversions of triglycerides to fatty acid ethyl esters is obtained under mild reaction conditions that correspond to the transformation of triglycerides in a mixture of two moles of fatty acid ethyl esters and a mole of monoglyceride, thus avoiding the glycerol production. Reaction can be carried out under standard conditions with oil/ethanol volume ratio 12/3.5 ml at 40°C and 40 mg of immobilized enzyme
synthesis
-
synthesis of biodiesel from canola oil. Adding tert-butanol to the reaction medium increases the conversion of oil to fatty acid methyl ester for the enzyme immobilized on epoxy-functionalized silica, 50 wt.% tert-butanol by substrate weight gives the best yield. Presence of water significantly increases fatty acid methyl ester yield. 85% residual activity after 16 reaction cycles
synthesis
-
synthesis of eugenyl benzoate by esterification of eugenol and benzoic acid catalyzed by the chitosan-chitin nanowhiskers supported lipase. Under optimum conditions, a maximum conversion yield of 66% at 50°C in 5 h using 3 mg/ml of lipase, and a substrate molar ratio (eugenol: benzoic acid) of 3:1 is obtained. The lipase is reusable up to 8 esterification cycles and shows higher thermal stability than free enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Derewenda, U.; Brzozowski, A.M.; Lawson, D.M.; Derewenda, Z.S.
Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase
Biochemistry
31
1532-1541
1992
Rhizomucor miehei
Sharma, R.; Chisti, Y.; Banerjee, U.C.
Production, purification, characterization, and applications of lipases
Biotechnol. Adv.
19
627-662
2001
Acinetobacter calcoaceticus, Aspergillus niger, Aspergillus oryzae, Geobacillus stearothermophilus, Bacillus sp. (in: Bacteria), Burkholderia cepacia, Burkholderia sp., Moesziomyces antarcticus, Diutina rugosa, Rhizomucor miehei, Penicillium roqueforti, Hyphopichia burtonii, Proteus vulgaris, Pseudomonas sp., Pseudomonas aeruginosa, Pseudomonas alcaligenes, Pseudomonas oleovorans, Rhizopus arrhizus, Rhodotorula glutinis, Staphylococcus epidermidis, Penicillium wortmanii, Penicillium roqueforti IAM7268, Bacillus sp. (in: Bacteria) J33, Acinetobacter calcoaceticus BD 413, Geobacillus stearothermophilus L1, Pseudomonas sp. KM1-56
Oh, S.W.; Gaskin, D.J.H.; Kwon, D.Y.; Vulfson, E.N.
Properties of recombinant Rhizomucor miehei lipase with amino acid substitutions of Phe94 in the substrate binding domain
Biotechnol. Lett.
23
563-568
2001
Rhizomucor miehei
-
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
-
Turner, N.J.; Winterman, J.R.; McCague, R.; Parratt, J.S.; Taylor, S.J.C.
Synthesis of homochiral L-(S)-tert-leucine via a lipase catalysed dynamic resolution process
Tetrahedron Lett.
36 (7)
1113-1116
1995
Rhizomucor miehei
-
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
Bezbradica, D.; Mijin, D.; Siler-Marinkovic, S.; Knezevic, Z.
The effect of substrate polarity on the lipase-catalyzed synthesis of aroma esters in solvent-free systems
J. Mol. Catal. B
45
97-101
2007
Rhizomucor miehei, Sus scrofa
-
Zoumpanioti, M.; Parmaklis, P.; de Maria, P.D.; Stamatis, H.; Sinisterra, J.V.; Xenakis, A.
Esterification reactions catalyzed by lipases immobilized in organogels: effect of temperature and substrate diffusion
Biotechnol. Lett.
30
1627-1631
2008
Rhizomucor miehei
Utsugi, A.; Kanda, A.; Hara, S.
Lipase specificity in the transacylation of triacylglycerin
J. Oleo Sci.
58
123-132
2009
Aspergillus niger, Burkholderia cepacia, Diutina rugosa, Mucor javanicus, Rhizomucor miehei, Penicillium camemberti, Penicillium roqueforti, Pseudomonas fluorescens, Rhizopus arrhizus, Rhizopus niveus, Sus scrofa
Acosta, A.; Filice, M.; Fernandez-Lorente, G.; Palomo, J.M.; Guisan, J.M.
Kinetically controlled synthesis of monoglyceryl esters from chiral and prochiral acids methyl esters catalyzed by immobilized Rhizomucor miehei lipase
Biores. Technol.
102
507-512
2011
Rhizomucor miehei
Vasel, B.; Hecht, H.J.; Schmid, R.D.; Schomburg, D.
3D-structures of the lipase from Rhizomucor miehei at different temperatures and computer modelling of a complex of the lipase with trilaurylglycerol
J. Biotechnol.
28
99-115
1993
Rhizomucor miehei
Bispo, P.; Batista, I.; Bernardino, R.J.; Bandarra, N.M.
Preparation of triacylglycerols rich in omega-3 fatty acids from sardine oil using a Rhizomucor miehei lipase: focus in the EPA/DHA ratio
Appl. Biochem. Biotechnol.
172
1866-1881
2014
Rhizomucor miehei
Attya, M.; Russo, A.; Perri, E.; Sindona, G.
Endogenous lipase catalyzed transesterification of olive oil fats. The formation of isomeric and oligomeric triacyleglycerols
J. Mass Spectrom.
47
1247-1253
2012
Rhizomucor miehei
Li, G.; Fang, X.; Su, F.; Chen, Y.; Xu, L.; Yan, Y.
Enhancing the thermostability of Rhizomucor miehei lipase with a limited screening library by rational-design point mutations and disulfide bonds
Appl. Environ. Microbiol.
84
e02129-17
2018
Rhizomucor miehei (A0A2D3HJ61), Rhizomucor miehei
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
Manan, F.M.A.; Attan, N.; Zakaria, Z.; Keyon, A.S.A.; Wahab, R.A.
Enzymatic esterification of eugenol and benzoic acid by a novel chitosan-chitin nanowhiskers supported Rhizomucor miehei lipase Process optimization and kinetic assessments
Enzyme Microb. Technol.
108
42-52
2018
Rhizomucor miehei
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
-
Calero, J.; Verdugo, C.; Luna, D.; Sancho, E.D.; Luna, C.; Posadillo, A.; Bautista, F.M.; Romero, A.A.
Selective ethanolysis of sunflower oil with Lipozyme RM IM, an immobilized Rhizomucor miehei lipase, to obtain a biodiesel-like biofuel, which avoids glycerol production through the monoglyceride formation
New Biotechnol.
31
596-601
2014
Rhizomucor miehei
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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