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Information on EC 3.1.1.3 - triacylglycerol lipase and Organism(s) Diutina rugosa and UniProt Accession P32947

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.3 triacylglycerol lipase
IUBMB 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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Diutina rugosa
UNIPROT: P32947
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Word Map
The taxonomic range for the selected organisms is: Diutina rugosa
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Candida rugosa lipase
-
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
-
-
-
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GEH
-
-
-
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glycerol ester hydrolase
-
-
-
-
glycerol-ester hydrolase
-
-
-
-
heparin releasable hepatic lipase
-
-
-
-
hepatic lipase
-
-
-
-
hepatic monoacylglycerol acyltransferase
-
-
-
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Lingual lipase
-
-
-
-
lipase
lipase AY
-
-
lipase AYS
-
-
lipase MY
-
-
lipase OF
-
-
lipase, triacylglycerol
-
-
-
-
lipazin
-
-
-
-
liver lipase
-
-
-
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meito MY 30
-
-
-
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meito Sangyo OF lipase
-
-
-
-
Pancreatic lipase
-
-
-
-
Pancreatic lysophospholipase
-
-
-
-
PGE
-
-
-
-
PL-RP2
-
-
-
-
post-heparin plasma protamine-resistant lipase
-
-
-
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PPL
-
-
-
-
Pregastric esterase
-
-
-
-
Pregastric lipase
-
-
-
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salt-resistant post-heparin lipase
-
-
-
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steapsin
-
-
-
-
Sterol esterase
-
-
-
-
takedo 1969-4-9
-
-
-
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teenesterase
-
-
-
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tiacetinase
-
-
-
-
tibutyrin esterase
-
-
-
-
triacylglycerol ester hydrolase
-
-
-
-
Triacylglycerol lipase
-
-
-
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tributyrase
-
-
-
-
tributyrinase
-
-
-
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triglyceridase
-
-
-
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triglyceride hydrolase
-
-
-
-
triglyceride lipase
-
-
-
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triolein hydrolase
-
-
-
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tween hydrolase
-
-
-
-
tween-hydrolyzing esterase
-
-
-
-
Tweenase
-
-
-
-
type VII lipase
-
-
additional information
the enzyme belongs to the CRL multigne family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
triacylglycerol + H2O = diacylglycerol + a carboxylate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
transesterification
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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 hide
9001-62-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
?
1,2-O-dilauryl-rac-glycero-3-glutaric resorufin ester + H2O
?
show the reaction diagram
-
commercial chromogenic lipase substrate
-
-
?
2-(4-chlorophenoxy)acetic acid ethyl ester + H2O
?
show the reaction diagram
-
the enantioselectivity of the hydrolysis of the 2-substituted-aryloxyacetic ester is increased by addition of isopropanol or DMSO as co-solvents
-
-
?
2-n-butyl-2-(4-chlorophenoxy)acetic acid ethyl ester + H2O
?
show the reaction diagram
-
the enantioselectivity of the hydrolysis of the 2-substituted-aryloxyacetic ester is increased by addition of isopropanol or DMSO as co-solvents
-
-
?
2-phenyl-2-(4-chlorophenoxy)acetic acid ethyl ester + H2O
?
show the reaction diagram
-
the enantioselectivity of the hydrolysis of the 2-substituted-aryloxyacetic ester is increased by addition of isopropanol or DMSO as co-solvents
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
show the reaction diagram
good substrate
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
show the reaction diagram
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
show the reaction diagram
good substrate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
show the reaction diagram
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
show the reaction diagram
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
show the reaction diagram
canola oil + H2O
?
show the reaction diagram
-
-
-
-
?
dextran T40 + vinyl acetate
?
show the reaction diagram
-
when vinyl acetate is used as acyl donor, percent modification of DexT40 increases from 31.8% to 60.5% in the presence of enzyme
-
-
?
dextran T40 + vinyl acrylate
?
show the reaction diagram
-
acylation with vinyl crotonate to DexT40 in DMSO demonstrates modification of 74.3% with addition of enzyme, compared to 25.5% without biocatalyst
-
-
?
dextran T40 + vinyl crotonate
?
show the reaction diagram
-
acylation with vinyl crotonate to DexT40 in DMSO demonstrates modification of 25.0% with addition of enzyme, compared to 0% without biocatalyst
-
-
?
dextran T40 + vinyl decanoate
?
show the reaction diagram
-
native lipase, pH-adjusted lipase, pH-adjusted lipase co-lyophilized with 18-crown-6 ether, and the lipase stepwise addition reaction display 3%, 49%, 64% and 96% conversion, respectively
-
-
?
dextran T40 + vinyl laurate
?
show the reaction diagram
-
enzymatic modification of DexT40 causes notably high extent of modification between 40 and 50%, as compared to less than 3% without enzyme
-
-
?
dextran T40 + vinyl methacrylate
?
show the reaction diagram
-
acylation with vinyl crotonate to DexT40 in DMSO demonstrates modification of 51.2% with addition of enzyme, compared to 1.7% without biocatalyst
-
-
?
dextran T40 + vinyl pivalate
?
show the reaction diagram
-
-
-
-
?
dextran T40 + vinyl propionate
?
show the reaction diagram
-
the enzyme accelerates the reaction with vinyl propionate up to 58.6% compared to 8.2% without enzyme
-
-
?
glycerol + caprylate
?
show the reaction diagram
-
esterification
-
-
?
high linoleic sunflower oil + H2O
?
show the reaction diagram
-
-
-
-
?
high oleic sunflower oil + H2O
?
show the reaction diagram
-
-
-
-
?
olive oil + H2O
?
show the reaction diagram
-
-
-
-
?
rac 2-(4-chlorophenoxy)propanoic acid + n-butanol
?
show the reaction diagram
-
esterification reaction, in n-heptane
-
?
racemic butyl 2-(4-ethylphenoxy)propionate + H2O
2-(4-ethylphenoxy)propionate + butanol
show the reaction diagram
-
modified enzyme shows reduced activity and 15fold increased enantioselectivity
-
?
soybean oil + H2O
?
show the reaction diagram
-
-
-
-
?
sulcatol + fatty acid
?
show the reaction diagram
-
esterification reaction, in toluene
-
?
triacetin + H2O
diacetin + acetic acid
show the reaction diagram
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
show the reaction diagram
tricaprylin + H2O
dicaprylin + caprylate
show the reaction diagram
-
-
-
-
?
triolein + H2O
diolein + oleate
show the reaction diagram
-
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
tributyrin + H2O
dibutyrin + butyrate
show the reaction diagram
-
-
-
-
r
triolein + H2O
diolein + oleate
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
enzyme regulation
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
2.3fold activation at 10 mM
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Brij
slight inhibition of wild-type enzyme, and slight activation of the mutant N-fused enzyme at 1 mM
-
CHAPS
complete inhibition of both wild-type and mutant N-fused enzymes at 1 mM
PMSF
about 40% inhibition at 10 mM, 20% at 1 mM
SDS
complete inhibition of both wild-type and mutant N-fused enzymes at 0.1 mM
sodium taurocholate
55% inhibition of wild-type enzyme and slight activation of the mutant N-fused enzyme at 1 mM
Triton X-100
strong inhibition of both wild-type and mutant N-fused enzymes at 1 mM
Tween 20
over 90% inhibition of both wild-type and mutant N-fused enzymes at 1 mM
Tween 80
about 30% inhibition of both wild-type and mutant N-fused enzymes at 1 mM
ethanol
-
-
oleic acid
-
inhibits enzyme production, product inhibition
SDS
98% inhibition at 0.1% w/v
sodium deoxycholate
-
isozymes Lip3 and Lip1, inhibition kinetics
Tween 20
18-19% inhibition at 0.1-1.0% w/v
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Brij
slight inhibition of wild-type enzyme, and slight activation of the mutant N-fused enzyme at 1 mM
-
sodium taurocholate
55% inhibition of wild-type enzyme and slight activation of the mutant N-fused enzyme at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00017 - 0.274
4-nitrophenyl palmitate
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
67.5
purified recombinant modified N-fused LIP3, substrate 4-nitrophenyl butyrate, pH 7.0, 37°C
82.6
purified recombinant wild-type LIP3, substrate 4-nitrophenyl butyrate, pH 7.0, 37°C
1030
-
purified Lip3 dimer
13.75
-
immobilized on Duolite A7, at 60°C
1500
-
purified Lip1 dimer
22.84
-
immobilized on Celite 545, at 60°C
4.32
-
free enzyme, at 60°C
5.79
-
immobilized on Sephadex G-25, at 60°C
6.4
recombinant enzyme in culture medium
7200
purified recombinant enzyme, substrate 4-nitrophenyl laurate
910
-
purified Lip3 monomer
974
-
commercially available purified enzyme preparation
additional information
-
activity of immobilized enzyme using different immobilization agents, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9
-
assay at
7 - 8.5
-
immobilized enzyme dependent on the immobilization agent, overview
7.4
-
assay at
8
-
free enzyme
8.5
-
Al2O3-immobilized enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9
inactive at pH 10.0, pH profile, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
30
-
assay at
35
-
free enzyme
40 - 50
-
immobilized enzyme dependent on the immobilization agent, overview
45
-
lipase AYS
55
-
immobilized enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
-
Lip3 monomer, isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LIP3 precursor; i.e. Candida cylindracea, gene lip3, isozyme LIP3
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
submerged batch culture
Manually annotated by BRENDA team
additional information
-
expression analysis of different isozymes
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LIP3_DIURU
549
0
58755
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
117000
-
dimeric Lip3, gel filtration
43000
-
monomeric Lip3, gel filtration
60000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 60000, recombinant enzyme, SDS-PAGE
dimer
-
2 * 60000, Lip3, SDS-PAGE
monomer
-
1 * 60000, Lip3, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
isozymes are glycoproteins, major glycosylation site is Asn351, other sites are Asn291 and Asn314, dependent on the isozyme, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N314Q
-
site-sirected mutagenesis, the mutation of the glycosylation site destabilizes the enzyme and affects the enzyme activity
N351Q
-
site-sirected mutagenesis, the mutation of the glycosylation site destabilizes the enzyme and affects the enzyme activity
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9
16 h, 37°C, purified recombinant enzyme, 54% of maximal activity at pH 3.0, 52.5% at pH 9.0, inactivation at pH 10.0, completely stabel at pH 8.0, overview
680279
4 - 6
14 h, 95-100% remaining activity
665288
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 90
10 min
30 - 40
10 min, recombinant enzyme, pH 7.0, stable at, inactivation above
5 - 70
-
the free enzyme shows full activity after 1 h at 5°C, about 80% activity at 25-35°C, about 65% activity at 40-45°C, about 50% activity at 50°C and is completely inactive after 1 h at 60°C. The immobilized lipase holds approximately 30% activity at 55°C, while the free lipase remains less than 10%
55
-
free enzyme at 55°C shows a half-life of 0.38 h, maintaining 20% of its original activity after 1 h, whereas the half-life of the immobilized lipase at this temperature is 0.82 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
following immobilization by covalent attachment on hydrous niobium oxide, the enzyme exhibits improved storage stability and performs better at higher incubation temperatures. In addition, the enzyme retains most of its catalytic efficiency after successive operational cycles. For the esterification reaction of butanol with butyric acid (24 h, 37°C), a slow decrease in the esterification activity is verified (25%) after ten recycles (240 h), which corresponds to a half-life of 406 h
-
the hydrolytic activity improves significantly upon immobilization, immobilization on Celite 545 produces the highest increase in hydrolytic activity
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
n-heptane
-
the purified enzyme is less active in dry n-heptane than the crude preparation, but the addition of a small amount of water dramatically activates the purified enzyme but not the crude one
toluene
-
catalyzes the esterification of sulcatol and fatty acids in toluene
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, Al2O3-immobilized lipase in 50 mM phosphate buffer (pH 8.0), the immobilized lipase retains 90% of its catalytic activity
-
4°C, free enzyme in 50 mM phosphate buffer (pH 8.0), over a period of 4 months, the activity o the free enzyme gradually decreases to 50%
-
4°C, niobium oxide-immobilized enzyme, 60 days, the activity decreases by 80%
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type LIP3 10.3fold and genetically modified, active codon-optimized LIP3 16.1fold from Pichia pastoris strain SMD168H
purification isozymes from commercial preparations
-
recombinant secreted enzyme 25.6fold from Pichia pastoris by hydrophobic interaction chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene lip3, subcloning in Escherichia coli strain DH5alpha, expression of wild-type enzyme and of genetically modified, active codon-optimized LIP3 lipase in Pichia pastoris strain SMD168H
expressed in Pichia pastoris, removal of the N-terminus and the regional codon optimization of the lip2 gene fragment at the 5' end can greatly increase the expression level of recombinant LIP2 in the Pichia pastoris pastoris system
-
expression of LIP gene encoded wild-type and mutant isozymes in Saccharomyces cerevisiae and Pichia pastoris
-
gene lip1, expression in Pichia pastoris, culture condition and codon optimization for improved expression, secretion of the recombinant enzyme, overview
isozyme gene lip1, synthetically synthesized in an optimized nucleotide sequence to avoid the interference that occurs in heterologous expression of the native gene due to unusual codon usage, functional overexpression in Pichia pastoris of the synthetic gene, expression in Candida maltosa, a related yeast with the same codon usage, secretion in active form to the culture medium
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
removal of the N-terminus and the regional codon optimization of the lip2 gene fragment at the 5' end can greatly increase the expression level of recombinant LIP2 in the Pichia pastoris pastoris system
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biofuel production
-
Candida rugosa lipase immobilized on hydrous niobium oxide to be used in the biodiesel synthesis
biotechnology
-
the enzyme can be used for hydrolysis and synthesis of various esters, mutagenic modification and optimization of Candida rugosa isozymes for enantioselective, substrate-specific biocatalysis, improvement of thermostability, enantioselectivity, and substrate specificity, possible reactions are hydrolysis, direct esterification, acidolysis, alcoholysis, ester-interchange, and glycerolysis, overview
nutrition
-
the enzyme of nonpathogenic Candida rugosa can be used for hydrolysis and synthesis of various esters in food application, mutagenic modification and optimization of isozymes for enantioselective, substrate-specific biocatalysis, improvement of thermostability, enantioselectivity, and substrate specificity, overview
paper production
-
removal of pitch, i.e. triglycerides and waxes, from the pulp produced for paper making
synthesis
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
Ueji, S.i.; Ueda, A.; Tanaka, H.; Watanabe, K.; Okamoto, T.; Ebara, Y.
Chemical modification of lipases with various hydrophobic groups improves their enantioselectivity in hydrolytic reactions
Biotechnol. Lett.
25
83-87
2003
Diutina rugosa
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
Pernas, M.A.; Lopez, C.; Rua, M.L.; Hermoso, J.
Influence of the conformational flexibility on the kinetics and dimerization process of two Candida rugosa lipase isoenzymes
FEBS Lett.
501
87-91
2001
Diutina rugosa
Manually annotated by BRENDA team
Chang, S.W.; Lee, G.C.; Shaw, J.F.
Codon optimization of Candida rugosa lip1 gene for improving expression in Pichia pastoris and biochemical characterization of the purified recombinant LIP1 lipase
J. Agric. Food Chem.
54
815-822
2006
Diutina rugosa (P20261), Diutina rugosa
Manually annotated by BRENDA team
Akoh, C.C.; Lee, G.C.; Shaw, J.F.
Protein engineering and applications of Candida rugosa lipase isoforms
Lipids
39
513-526
2004
Diutina rugosa
Manually annotated by BRENDA team
Perez, V.H.; da Silva, G.S.; Gomes, F.M.; de Castro, H.F.
Influence of the functional activating agent on the biochemical and kinetic properties of Candida rugosa lipase immobilized on chemically modified cellulignin
Biochem. Eng. J.
34
13-19
2007
Diutina rugosa
-
Manually annotated by BRENDA team
Ammazzalorso, A.; Amoroso, R.; Bettoni, G.; De Filippis, B.; Fantacuzzi, M.; Giampietro, L.; Maccallini, C.; Tricca, M.L.
Candida rugosa lipase-catalysed kinetic resolution of 2-substituted-aryloxyacetic esters with dimethylsulfoxide and isopropanol as additives
Chirality
20
115-118
2008
Diutina rugosa
Manually annotated by BRENDA team
Chang, S.W.; Lee, G.C.; Shaw, J.F.
Efficient production of active recombinant Candida rugosa LIP3 lipase in Pichia pastoris and biochemical characterization of the purified enzyme
J. Agric. Food Chem.
54
5831-5838
2006
Diutina rugosa (P32947), Diutina rugosa
Manually annotated by BRENDA team
Pinheiro, R.C.; Soares, C.M.; de Castro, H.F.; Moraes, F.F.; Zanin, G.M.
Response surface methodology as an approach to determine optimal activities of lipase entrapped in sol-gel matrix using different vegetable oils
Appl. Biochem. Biotechnol.
146
203-214
2008
Diutina rugosa
Manually annotated by BRENDA team
Lumor, S.E.; Akoh, C.C.
Esterification and hydrolytic activities of Candida rugosa lipase isoform 1 (LIP1) immobilized on Celite 545, Duolite A7, and Sephadex G-25
J. Agric. Food Chem.
56
10396-10398
2008
Diutina rugosa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Yesiloglu, Y.; Sit, L.
Biochemical properties of free and immobilized Candida rugosa lipase onto Al2O3: a comparative study
Artif. Cells Blood Substit. Immobil. Biotechnol.
39
247-251
2011
Diutina rugosa
Manually annotated by BRENDA team
Miranda, M.; Urioste, D.; Andrade Souza, L.T.; Mendes, A.A.; de Castro, H.F.
Assessment of the morphological, biochemical, and kinetic properties for Candida rugosa lipase immobilized on hydrous niobium oxide to be used in the biodiesel synthesis
Enzyme Res.
2011
216435
2011
Diutina rugosa
Manually annotated by BRENDA team
Chang, S.W.; Li, C.F.; Lee, G.C.; Yeh, T.; Shaw, J.F.
Engineering the expression and biochemical characteristics of recombinant Candida rugosa LIP2 lipase by removing the additional N-terminal peptide and regional codon optimization
J. Agric. Food Chem.
59
6710-6719
2011
Diutina rugosa
Manually annotated by BRENDA team
Kaewprapan, K.; Wongkongkatep, J.; Panbangred, W.; Phinyocheep, P.; Marie, E.; Durand, A.; Inprakhon, P.
Lipase-catalyzed synthesis of hydrophobically modified dextrans: activity and regioselectivity of lipase from Candida rugosa
J. Biosci. Bioeng.
112
124-129
2011
Diutina rugosa
Manually annotated by BRENDA team