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4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
1,2-O-dilauryl-rac-glycero-3-glutaric resorufin ester + H2O
?
-
commercial chromogenic lipase substrate
-
-
?
2-(4-chlorophenoxy)acetic acid ethyl ester + H2O
?
-
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
?
-
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
?
-
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
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
good substrate
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
good substrate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
canola oil + H2O
?
-
-
-
-
?
dextran T40 + vinyl acetate
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
-
-
-
?
dextran T40 + vinyl propionate
?
-
the enzyme accelerates the reaction with vinyl propionate up to 58.6% compared to 8.2% without enzyme
-
-
?
glycerol + caprylate
?
-
esterification
-
-
?
high linoleic sunflower oil + H2O
?
-
-
-
-
?
high oleic sunflower oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
rac 2-(4-chlorophenoxy)propanoic acid + n-butanol
?
-
esterification reaction, in n-heptane
-
?
racemic butyl 2-(4-ethylphenoxy)propionate + H2O
2-(4-ethylphenoxy)propionate + butanol
-
modified enzyme shows reduced activity and 15fold increased enantioselectivity
-
?
soybean oil + H2O
?
-
-
-
-
?
sulcatol + fatty acid
?
-
esterification reaction, in toluene
-
?
triacetin + H2O
diacetin + acetic acid
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
tricaprylin + H2O
dicaprylin + caprylate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
r
additional information
?
-
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
preferred substrate of lipase A
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
best substrate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
preferred substrate of lipase B
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
lower activity
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
r
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
?
-
-
enzyme regulation
-
-
?
additional information
?
-
-
substrate specificities of wild-type and mutant isozymes, possible reactions are hydrolysis, direct esterification, acidolysis, alcoholysis, ester-interchange, and glycerolysis
-
-
?
additional information
?
-
-
the enantioselectivity of the hydrolysis of three different 2-substituted-aryloxyacetic esters is increased by addition of isopropanol or DMSO
-
-
?
additional information
?
-
-
in the conversion of babassu oil into alkyl esters, butanol gives the highest conversion (79.35%). Babassu oil consists of 3.5% caprylic, 4.5% capric, 44.7% lauric, 17.5% myristic, 9.7% palmitic, 3.1% stearic, 15.2% oleic, and 1.8% linoleic acid
-
-
?
additional information
?
-
-
lipase AY has the loose regioselectivity toward 2-OH and 3-OH in the glucose unit of dextran
-
-
?
additional information
?
-
-
the enzyme uses olive oil as substrate
-
-
?
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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
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
no inhibition by Tween 80, Brij35, Triton X-100, 3-[(3-cholamidopropyl)dimethylammonio]-1-propane sulfonic acid, and sodium taurocholate at 0.1-1.0% w/v
-
additional information
-
no inhibition by Tween 80, Brij35, Triton X-100, 3-[(3-cholamidopropyl)dimethylammonio]-1-propane sulfonic acid, and sodium taurocholate at 0.1-1.0% w/v
-
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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
the 18 nonuniversal serine codons of the lip3 gene are converted into universal serine codons by means of an overlap extension PCR-based multiple-site-directed mutagenesis to express an active recombinant LIP3 in Pichia pastoris, removal of additional N-terminal peptide in front of the lip3 gene by PCR, production yield of codon-optimized N-fused lip3 is 69fold increased compared to the non-codon-optimized enzyme
additional information
-
the 18 nonuniversal serine codons of the lip3 gene are converted into universal serine codons by means of an overlap extension PCR-based multiple-site-directed mutagenesis to express an active recombinant LIP3 in Pichia pastoris, removal of additional N-terminal peptide in front of the lip3 gene by PCR, production yield of codon-optimized N-fused lip3 is 69fold increased compared to the non-codon-optimized enzyme
additional information
-
lipase is modified by substitution with diverse side chain groups, overview, lipase MY modified with a benzyloxycarbonyl group, modified enzyme shows reduced activity and 15fold increased enantioselectivity
additional information
construction of a regional synthetic lip1 gene for improved expression in Pichia pastoris, overview
additional information
-
construction of a regional synthetic lip1 gene for improved expression in Pichia pastoris, overview
additional information
-
conversion by site-directed mutagenesis of most leucine triplets to serine, because the yeast cells do not use universal codons for leucine coding, which hinders improvement of isozymes for specific biocatalysis, overview
additional information
-
the enzyme is immobilized on chemically modified wood cellulignin from Eucaliptus grandis by covalent binding using different activating agents such as carbonyldiimidazole, glutaraldehyde and sodium metaperiodate, method development and immobilization reaction mechanisms, overview
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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
-
synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
synthesis
-
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
additional information
codon optimization for improved expression of LIP1 in Pichia pastoris for uuse of the enzyme in industrial processes
additional information
-
codon optimization for improved expression of LIP1 in Pichia pastoris for uuse of the enzyme in industrial processes
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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
brenda
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
brenda
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
-
brenda
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
brenda
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
brenda
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
brenda
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
-
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda