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(+-)-2-hydroxy-4-phenylbutyric acid ethyl ester + H2O
?
-
enantioselectivity of the immobilized enzyme in this reaction is increased 40fold by presence of 0.1% CTAB
-
-
?
(+/-)-trans-3-(4'-methoxy-phenyl)-glycidyl methyl ester + H2O
(2R,3S)-3-(4-hydroxyphenyl)oxirane-2-carboxylic acid + methyl (2S,3R)-3-(4-hydroxyphenyl)oxirane-2-carboxylate + methanol
-
50% conversion yield after 4 h in 100 mM potassium phosphate buffer, pH 7.5, at 30 °C
-
-
?
(3aR,6aS)-2-oxo-3,3a,4,6a-tetrahydro-2H-cyclopenta[b]furan-3-yl acetate + H2O
(3S,3aR,6aS)-2-oxo-3,3a,4,6a-tetrahydro-2H-cyclopenta[b]furan-3-yl acetate + (3R,3aS,6aS)-3-hydroxy-3,3a,4,6a-tetrahydro-2H-cyclopenta[b]furan-2-one + acetate
-
-
-
-
?
(4S)-4-tert-butyl-2-phenyl-1,3-oxazol-5(4H)-one + butanol
butyl (2S)-2-(benzoylamino)3,3-dimethylbutanoate
-
-
-
-
?
(5R,6R)-6-hydroxy-5,6-dihydro-1,10-phenanthrolin-5-yl acetate + vinyl acetate
(5S,6S)-6-hydroxy-5,6-dihydro-1,10-phenanthrolin-5-yl acetate + (5R,6R)-5,6-dihydro-1,10-phenanthroline-5,6-diyl diacetate + ethenol
-
-
-
-
?
(R)-2-ethylhexanoic acid ethyl ester + H2O
(R)-2-ethylhexanoate + ethanol
-
-
-
-
?
(R)-3,5,5-trimethylhexanoic acid ethyl ester + H2O
(R)-3,5,5-trimethylhexanoate + ethanol
-
-
-
-
?
(R,S)-1-phenylethylamine + ethyl methoxyacetate
(S)-1-phenylethylamine + 2-methoxy-N-[(1R)-1-phenylethyl]acetamide + ethanol
-
-
-
-
?
(R,S)-2-O-butyryl-2-phenylacetate + H2O
(R)-2-O-butyryl-2-phenylacetate + (2S)-hydroxy(phenyl)ethanoic acid + butyrate
-
Enantioselectivity of the reaction can be obtained with various methods of enzyme immoblisation and reaction conditions
-
-
?
(R,S)-flurbiprofen ethyl ester + H2O
(S)-flurbiprofen + ethanol
(R,S)-flurbiprofen ethyl ester + H2O
(S)-flurbiprofen ethyl ester + (R)-flurbiprofen + ethanol
(R,S)-ibuprofen + 1-propanol
(S)-ibuprofen n-propyl ester + (R)-ibuprofen
(R,S)-mandelonitrile + vinyl acetate
(S)-cyano(phenyl)methyl acetate + (R)-mandelonitrite
-
transesterification
-
-
?
(R,S)-naproxen 2,2,2-trifluoroethyl thioester
(S)-naproxen + 2,2,2-trifluorothioethanol + (R)-naproxen 2,2,2-trifluoroethyl thioester
-
(R,S)-profen 2,2,2-trifluoroethyl thioester
-
-
?
(R,S)-[4-[4a,6b(E)]]-6-[4,4-bis(4-fluorophenyl)-3-(1-methyl-1H-tetrazol-5-yl)-1,3-butadienyl]-tetrahydro-4-hydroxy-2H-pyran-2-one + isopropenyl acetate
(R)-(+)-[4-[4a,6b(E)]]-6-[4,4-bis(4-fluorophenyl)-3-(1-methyl-1H-tetrazol-5-yl)-1,3-butadienyl]-tetrahydro-4-hydroxy-2H-pyran-2-one + (S)-(-)-[4-[4a,6b(E)]]-6-[4,4-bis(4-fluorophenyl)-3-(1-methyl-1H-tetrazol-5-yl)-1,3-butadienyl]-tetrahydro-4-acetyloxy-2H-pyran-2-one + prop-1-en-2-ol
-
-
-
-
?
(R/S)-ibuprofen methoxyethyl ester + H2O
(R)-ibuprofen methoxyethyl ester + (S)-ibuprofen + 2-methoxyethanol
Candida cyclindraceae
-
-
-
-
?
(RS)-1-phenylethanol + vinyl acetate
(R)-1-phenylethyl acetate + acetaldehyde + (S)-1-phenylethanol
(RS)-1-phenylethanol + vinyl acetate
(S)-1-phenylethyl acetate + acetaldehyde + (R)-1-phenylethanol
-
-
-
-
?
(RS)-1-phenylethyl acetate + H2O
(R)-1-phenylethanol + acetate + (R)-1-phenylethyl acetate
-
enzyme hydrolyzes mainly the R-enantiomer, temperature-dependent, the enantioselectivity decreases with increasing temperature
-
?
(S)-2-ethyl hexanoic acid ethyl ester + H2O
?
-
-
-
-
?
(S)-3,5,5-trimethylhexanoic acid ethyl ester + H2O
(S)-3,5,5-trimethylhexanoate + ethanol
-
-
-
-
?
(S)-glycidol + vinyl n-butyrate
(2R)-oxiran-2-yl-methyl butanoate + ethenol
-
transesterification
-
-
?
(S,R)-acetic acid 2-methyl-4-oxo-3-prop-2-ynyl-cyclopent-2-enyl ester + H2O
(R)-4-hydroxy-3-methyl-2-prop-2-ynyl-cyclopent-2-enone + (S)-acetic acid 2-methyl-4-oxo-3-prop-2-ynyl-cyclopent-2-enyl ester + acetate
-
-
-
-
?
1,2 di-O-lauryl-rac-glycero-3-(glutaric acid 6-methyl) resorufin ester + H2O
?
-
-
-
-
?
1,2,3-trihexaicosanoylglycerol + H2O
1,2-dihexaicosanoylglycerol + hexaicosanoate
-
-
-
-
?
1,2,3-trioleoyl-glycerol + H2O
?
-
-
-
?
1,2-di-O-lauryl-rac-glycero-3-glutaric acid 6'-methylresorufin ester + H2O
?
chromogenic substrate
-
-
?
1,2-didecanoyl-1-thioglycerol + H2O
?
-
-
-
?
1,2-didecanoyl-rac-glycerol + H2O
?
1,2-dilauryl-rac-glycero-3-glutaric acid resorufinester + H2O
?
1,2-dilinoleoyl-3-oleoyl-rac-glycerol + H2O
?
-
-
-
?
1,2-dioctanoyl-sn-glycero-3-phosphocholine + H2O
?
1,2-dioctanoyl-sn-glycero-3-phosphoglycol + H2O
?
-
-
-
?
1,2-dioleoylglycerol + H2O
oleic acid + ?
1,2-dipalmitin + H2O
?
-
-
-
-
?
1,2-O-dilauryl-rac-glycero-3-glutaric acid resorufin ester + H2O
?
-
-
-
?
1,2-O-dilauryl-rac-glycero-3-glutaric resorufin ester + H2O
?
-
commercial chromogenic lipase substrate
-
-
?
1,2-sn-dicaprin + H2O
?
-
regio- and stereoselective reaction
-
-
?
1,3-diolein + H2O
1-oleoyl-sn-glycerol + oleate
low activity
-
-
?
1,3-dioleoyl-2-palmitoyl-glycerol + H2O
?
-
not BTID-A
-
?
1,3-dipalmitoyl-2-oleoyl-glycerol + H2O
?
-
-
-
?
1-caprin + H2O
glycerol + caprate
-
-
-
-
?
1-monopalmitin + H2O
palmitic acid + glycerol
-
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
1-naphthyl butyrate + H2O
1-naphthol + butyrate
-
18.8% activity compared to rice bran oil
-
-
?
1-naphthyl octanoate + H2O
1-naphthol + octanoate
-
-
-
-
?
1-olein + H2O
glycerol + oleate
-
-
-
-
?
1-phenylethanol + vinyl butanoate
?
-
-
-
-
?
1-phenylethanol + vinyl caproate
?
-
-
-
-
?
1-phenylethanol + vinyl octanoate
?
-
-
-
-
?
1-stearoyl-2-arachidonoyl-sn-glycerol + H2O
?
-
-
-
?
2 triolein + H2O
3 oleic acid + 2-monoolein + 1,3-diolein
-
1,3-specificity for triolein
-
-
?
2,3-dibutyrylthio-1-propyl oleate + H2O
2,3-dibutyrylthiopropyl alcohol + oleate
-
chromogenic detection using 5,5'-dithio-bis-(2-nitrobenzoic acid) as chromogen or the 6-methylresorufin ester of 1-O,2-dilauryl-rac-glycero-3-glutaric acid, substrate synthesis, assay development, optimization, and method comparison, overview
-
-
?
2,3-dimercapto-1-propanol tributyrate + H2O
?
2,3-dimercaptopropan-1-ol tributyrate + H2O
?
2,3-sn-dicaprin + H2O
?
-
regio- and stereoselective reaction
-
-
?
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-ethylhexanoic acid ethyl ester + H2O
?
-
lowest activity
-
-
?
2-hexandecanoylthio-ethane-1-phosphocholine + H2O
?
2-methyldecanoic acid 4-nitrophenyl ester + H2O
(S)-2-methyldecanoate + 4-nitrophenol + (R)-2-methyldecanoic acid 4-nitrophenyl ester
-
model substrate, enantioselectivity in the asymmetric hydrolysis with preference for the S-enantiomer
-
-
?
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-naphthyl acetate + H2O
2-naphthol + acetate
-
-
-
-
?
2-naphthyl caprylate + H2O
2-naphthol + caprylate
-
-
-
-
?
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
-
-
?
2-[2-(2,4-difluoro-phenyl)-allyl]-propane-1,3-diol + vinyl acetate
(S)-acetic acid 4-(2,4-difluoro-phenyl)-2-hydroxymethyl-pent-4-enyl ester + acetic acid 2-acetoxymethyl-4-(2,4-difluoro-phenyl)-pent-4-enyl-ester
-
-
-
-
?
3 triolein + 3 H2O
1,3-diolein + 1,2-diolein + 2,3-diolein + 3 oleate
-
-
shows random positional specificity for triolein hydrolysis
-
?
3-(4-methoxyphenyl)glycidic acid methyl ester + H2O
(2R,3S)-3-(4-methoxyphenyl)glycidic acid methyl ester + (2S,3R)-3-(4-methoxyphenyl)glycidic acid + methanol
3-acetoxy beta-lactam + H2O
?
4 triolein + H2O
6 oleic acid + 1,3-diolein + 1,2-diolein + 1-monoolein + 2-monoolein
-
about 115% activity compared to olive oil
oleic acid is the major product
-
?
4-hydroxy-3-methyl-2-(2-propenyl)-2-cyclopenten-1-one acetate + H2O
?
-
50% conversion
-
-
?
4-methylumbelliferyl butyrate + H2O
4-methylumbelliferol + butyrate
4-methylumbelliferyl butyrate + H2O
4-methylumbelliferone + butyrate
4-methylumbelliferyl ester + H2O
4-methylumbelliferone + fatty acid
-
with fatty acids of different length in decreasing order, medium chain, long chains, short chains
-
-
?
4-methylumbelliferyl oleate + H2O
4-methylumbelliferone + oleate
4-methylumbelliferyl oleate + H2O
4-methylumbelliferone + oleic acid
-
-
-
-
?
4-nitrophenol butyrate + H2O
4-nitrophenol + butyrate
4-nitrophenyl 2-(4-methylphenyl)propanoate + H2O
4-nitrophenol + 2-(4-methylphenyl)propanoate
-
55.6% conversion, (S)-selectivity
-
-
?
4-nitrophenyl 2-benzylpropanoate + H2O
4-nitrophenol + 2-benzylpropanoate
-
80.3% conversion, (S)-selectivity
-
-
?
4-nitrophenyl 2-ethylhexanoate + H2O
4-nitrophenol + 2-ethylhexanoate
-
75.3% conversion, (S)-selectivity
-
-
?
4-nitrophenyl 2-methyldecanoate + H2O
?
-
kinetic resolution of enantioselectivity, overview
-
-
?
4-nitrophenyl 2-methylheptanoate + H2O
4-nitrophenol + 2-methylheptanoate
-
80.7% conversion, (S)-selectivity
-
-
?
4-nitrophenyl 2-phenylbutanoate + H2O
4-nitrophenol + 2-phenylbutanoate
-
17% conversion, (R)-selectivity
-
-
?
4-nitrophenyl 2-phenylpentanoate + H2O
4-nitrophenol + 2-phenylpentanoate
-
88.1% conversion, (R)-selectivity
-
-
?
4-nitrophenyl 2-phenylpropanoate + H2O
4-nitrophenol + 2-phenylpropanoate
-
38% conversion, (S)-selectivity
-
-
?
4-nitrophenyl 4-cyclohexyl-2-methylbuta-2,3-dienoate + H2O
?
-
reaction via R-tetrahedral intermediate and S-tetrahedral intermediate, overview, the wild-type lipase and the mutant L162F show preference for the (+)-enantiomer, the mutant shows high enantioselectivity, kinetic resolution of enantioselectivity, overview
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
4-nitrophenyl formate + H2O
4-nitrophenol + formate
-
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
4-nitrophenyl oleate + H2O
4-nitrophenol + oleate
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
4-nitrophenyl palmitate + H2O
palmitate + 4-nitrophenol
-
the immobilized enzyme PAL PCMC works as better catalyst for hydrolysis of pNPP in n-heptane medium
-
-
?
4-nitrophenyl pentanoate + H2O
4-nitrophenol + pentanoate
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
4-nitrophenyl tetradecanoate + H2O
4-nitrophenol + tetradecanoate
-
best 4-nitrophenyl ester substrate for wild-type enzyme and mutant F94R
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
4-nitrophenylbutyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-phenyl-[1,3]-dioxolan-2-one + H2O
?
-
9.6% conversion
-
-
?
5-bromo-4-chloro-3-indoxyl palmitate + H2O
?
-
-
-
-
?
6-azido-5,6-dihydro-1,10-phenanthrolin-5-ol + vinyl acetate
(5S,6S)-6-azido-5,6-dihydro-1,10-phenanthrolin-5-ol + (5R,6R)-6-azido-5,6-dihydro-1,10-phenanthrolin-5-yl acetate + ethenol
-
-
-
-
?
acylglycerol + H2O
glycerol + a carboxylate
alpha-naphthyl acetate + H2O
alpha-naphthol + acetate
Cephaloleia presignis
-
-
-
?
alpha-naphthyl butyrate + H2O
alpha-naphthol + butyrate
alpha-naphthyl caprylate + H2O
alpha-naphthol + caprylate
alpha-naphthyl laurate + H2O
alpha-naphthol + laurate
-
-
-
?
alpha-naphthyl stearate + H2O
alpha-naphthol + stearate
-
equally active with both isomers
-
?
amyl acetate + H2O
?
-
7% activity compared to olive oil
-
-
?
amyl butyrate + H2O
?
-
550% activity compared to olive oil
-
-
?
amyl propionate + H2O
?
-
40% activity compared to olive oil
-
-
?
benzyl butyrate + H2O
?
-
highest activity, 1120% activity compared to olive oil
-
-
?
benzyl propionate + H2O
benzyl alcohol + propionate
benzyl salicylate + H2O
?
-
100% activity compared to olive oil
-
-
?
beta-naphthyl butyrate + H2O
beta-naphthol + butyrate
-
58% of the activity with the alpha-isomer
-
?
beta-naphthyl caprylate + H2O
beta-naphthol + caprylate
-
-
-
?
beta-naphthyl laurate + H2O
beta-naphthol + laurate
-
62.5% of the activity with the alpha-isomer
-
?
beta-naphthyl stearate + H2O
beta-naphthol + stearate
-
equally active with both isomers
-
?
butanol + butanoate
butyl butanoate + H2O
-
-
-
-
?
butyl butyrate + H2O
butane + butyrate
-
-
-
-
?
cane molasse + H2O
?
-
-
-
-
?
canola oil + H2O
?
-
-
-
-
?
cholesterol oleate + H2O
cholesterol + oleic acid
-
-
-
-
?
cis-3-(acetyloxy)-4-phenyl-2-azetidinone + H2O
(3R,4S)-cis-3-(acetyloxy)-4-phenyl-2-azetidinone + (3S,4R)-cis-3-hydroxy-4-phenyl-2-azetidinone + acetate
-
-
-
-
?
corn steep liquor + 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
-
-
?
diacylglycerol + H2O
acylglycerol + a carboxylate
diacylglycerol + H2O
fatty acid + acylglycerol
-
-
-
?
diacylglycerol-N,N,N-trimethylhomoserine + H2O
?
-
-
-
-
?
dicaprin + H2O
caprin + caprate
diethyl 3-phenylglutarate + H2O
(S)-ethyl phenylglutarate + (R)-ethyl phenylglutarate + ethanol
-
-
-
-
?
diethyl malate + H2O
?
-
-
-
-
?
diethyl tartrate + H2O
?
-
-
-
-
?
digalactosyldiacylglycerol + H2O
?
-
-
-
-
?
dimethyl succinate + H2O
?
-
high activity
-
-
?
diolein + H2O
1-oleoyl-sn-glycerol + oleate
diolein + H2O
monoolein + oleate
-
-
-
-
?
diolein + H2O
oleic acid + ?
-
-
-
-
?
DL-alpha-palmitin + H2O
?
-
-
-
?
DL-alpha-stearin + H2O
?
-
-
-
?
ethanol + soybean oil
?
-
transesterification reaction
-
-
?
ethyl 2-arylpropanoate + H2O
ethanol + (R)-2-arylpropanoate
ethyl butyrate + H2O
?
-
245% activity compared to olive oil
-
-
?
ethyl butyrate + H2O
ethane + butyrate
-
-
-
-
?
ethyl L-lactate + H2O
ethanol + L-lactate
-
-
-
-
?
ethyl laurate + H2O
ethanol + lauric acid
-
-
-
-
?
ethyl myristate + H2O
ethanol + myristic acid
ethyl palmitate + H2O
ethanol + palmitic acid
-
-
-
-
?
eugenol + benzoic acid
eugenyl benzoate
-
-
-
-
?
fenoprofen + H2O
?
-
(R,S)-profen 2,2,2-trifluoroethyl thioester
-
-
?
flax seed oil + H2O
?
-
-
-
?
flurbiprofen + H2O
?
-
(R,S)-profen 2,2,2-trifluoroethyl thioester
-
-
?
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 + 1,8-octanediol + adipic acid
?
-
polycondensation
-
-
?
glycerol + caprylate
?
-
esterification
-
-
?
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%)
-
?
glyceryl triacetate + H2O
glyceryl diacetate + acetic acid
-
-
?
glyceryl tributanoate + H2O
glycerol + butanoate
-
-
-
?
glyceryl tributyrate + H2O
glyceryl dibutyrate + butyric acid
-
-
?
glyceryl tricaproate + H2O
glyceryl dicaproate + caproic acid
-
-
?
glyceryl tricaprylate + H2O
glyceryl dicaprylate + caprylic acid
-
-
?
glyceryl trioctanoate + H2O
glycerol + octanoate
glyceryl trioleate + 3 H2O
glycerol + 3 oleate
glyceryl trioleate + H2O
glycerol 1,2-dioleate + oleate
-
-
-
?
glycidyl butyrate + H2O
?
-
49% conversion
-
-
?
hexadecyl butyrate + H2O
hexadecanol + butyric acid
hexadecyl formate + H2O
hexadecanol + formic acid
hexadecyl propionate + H2O
hexadecanol + propionic acid
high linoleic sunflower oil + H2O
?
high oleic sunflower oil + H2O
?
ibuprofen + H2O
?
-
(R,S)-profen 2,2,2-trifluoroethyl thioester
-
-
?
isoamyl alcohol + acetic acid
isoamyl acetate
-
after 72 h of reaction a conversion yield of 34.4% and 16.2% of isoamyl acetate is obtained using cellite-immobilized and free enzyme, respectively
-
-
?
isononanoic acid ethyl ester + H2O
isononanoic acid + ethanol
-
-
-
-
?
isophthalate + 2-butanol
isophthalic acid mono(1-methylpropyl)ester + isophthalic acid di(1-methylpropyl)ester + H2O
-
-
the yield is 34% monoester and 46% diester in 1-butyl-3-methyl imidazolium tetrafluoroborate buffer
-
?
isophthalate + cyclohexanol
isophthalic acid monocyclohexyl ester + H2O
-
-
the yield is 7% monoester, no formation of diester in 1-butyl-3-methyl imidazolium tetrafluoroborate buffer
-
?
isophthalate + cyclopentanol
isophthalic acid monocyclopentyl ester + H2O
-
-
the yield is 5% monoester, no formation of diester in 1-butyl-3-methyl imidazolium tetrafluoroborate buffer
-
?
isophthalate + ethanol
isophthalic acid monoethyl ester + isophthalic acid diethyl ester + H2O
-
-
the yield is 74% monoester and no diester in 1-butyl-3-methyl imidazolium tetrafluoroborate buffer and 38% monoester and 24% diester in 1-butyl-3-methyl imidazolium hexafluorophosphate buffer respectively
-
?
isophthalate + n-butanol
isophthalic acid monobutyl ester + H2O
-
-
the yield is 14% for the monoester, no formation of diester in 1-butyl-3-methyl imidazolium tetrafluoroborate buffer
-
?
ketoprofen + H2O
?
-
(R,S)-profen 2,2,2-trifluoroethyl thioester
-
-
?
L-alpha-phosphatidylcholine + H2O
?
L-lysine ethyl ester + H2O
L-lysine + ethanol
-
-
-
-
?
lauric acid + 1-propanol
propyl laurate + H2O
-
-
-
-
?
linseed oil + H2O
?
-
major acyl groups are oleic and linoleic acid
-
?
liprocil + H2O
?
-
-
-
-
?
long-chain triacylglycerol + H2O
diacylglycerol + a carboxylate
methyl (R)-mandelate + H2O
(R)-mandelic acid + methanol
methyl acetate + H2O
?
-
25% conversion
-
-
?
methyl acetate + H2O
methanol + acetate
Cephaloleia presignis
-
-
-
?
methyl beta-D-glucopyranoside + H2O
methanol + beta-D-glucose
-
regioselective deacetylation of preacylated substrate
-
?
methyl butyrate + H2O
methanol + butyrate
methyl caprate + H2O
methanol + caprate
-
best substrate
-
?
methyl caproate + H2O
methanol + caproate
-
-
-
?
methyl caprylate + H2O
methanol + caprylate
methyl icosanoate + H2O
methanol + icosanoate
-
-
-
?
methyl laurate + H2O
methanol + laurate
methyl linoleate + H2O
methanol + linoleate
-
-
-
?
methyl linoleate + H2O
methanol + linolic acid
methyl linolenate + H2O
methanol + linoleic acid
methyl linolenate + H2O
methanol + linolenate
-
-
-
?
methyl mandelate + H2O
?
-
33% conversion
-
-
?
methyl myristate + H2O
methanol + myristate
methyl myristate + H2O
methanol + myristic acid
methyl oleate + H2O
methanol + oleate
methyl oleate + H2O
methanol + oleic acid
methyl palmitate + H2O
methanol + palmitate
methyl propionate + H2O
methanol + propionate
methyl ricinoleate + H2O
methanol + ricinoleic acid
-
-
-
-
?
methyl stearate + H2O
methanol + stearate
methyl(RS)-2-methyldecanoate + H2O
(R)-2-methyldecanoic acid + methanol
-
enzyme hydrolyzes mainly the R-enantiomer, temperature-dependent, the enantioselectivity decreases with increasing temperature
-
?
methylbutyrate + H2O
methanol + butyric acid
-
-
-
-
?
monoacetylglycerol + H2O
acetic acid + glycerol
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
?
monoolein + H2O
oleic acid + glycerol
-
-
-
-
?
monooleoylglycerol + H2O
?
-
-
-
-
?
n-butyl palmitate + H2O
n-butanol + palmitic acid
-
-
-
-
?
n-hexyl laurate + H2O
n-hexanol + lauric acid
-
-
-
-
?
n-propyl myristate + H2O
n-propanol + myristic acid
-
-
-
-
?
naproxen methyl ester + H2O
?
-
41% conversion
-
-
?
neem oil + H2O
?
-
major acyl groups are palmitic, stearic and oleic acid
-
?
octanol + decanoate
octyl decanoate + H2O
-
-
-
?
oleate + methanol
oleic acid methyl ester
-
-
-
?
oleic acid + n-butanol
?
-
-
-
-
?
olein + H2O
glycerol + oleate
-
low activity with isozyme LIP II, residual activity with isozyme LIP I
-
-
?
oleoyl 2-naphthyl ester + H2O
oleic acid + 2-naphthol
-
-
-
-
?
oleoyl 2-naphthylamide + H2O
oleic acid + 2-naphthylamine
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetic acid
-
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
-
-
-
?
p-nitrophenyl caprate + H2O
p-nitrophenol + caprate
palm oil + H2O
?
-
77.7% activity compared to rice bran oil
-
-
?
palm olein + H2O
?
-
28% conversion in 6 h
-
-
?
palm olein + H2O
oleic acid + ?
palmitic acid + isopropanol
isopropyl palmitate + H2O
-
-
-
-
?
palmitin + H2O
glycerol + palmitate
-
low activity with isozyme LIP II, residual activity with isozyme LIP I
-
-
?
phosphatidic acid + H2O
?
-
-
-
-
?
phosphatidylcholine + H2O
?
phosphatidylethanolamine + H2O
?
phosphatidylglycerol + H2O
?
phosphatidylserine + H2O
?
-
-
-
-
?
phosphocholine + H2O
?
-
-
-
-
?
phthalate + ethanol
phthalic acid monoethyl ester + phthalic acid diethyl ester + H2O
-
-
the yield is 49% monoester and 30% diester in 1-butyl-3-methyl imidazolium tetrafluoroborate buffer and 67% monoester and 33% diester in 1-butyl-3-methyl imidazolium hexafluorophosphate buffer respectively
-
?
polyethylene sorbitan monooleate + H2O
?
R-ketoprofen + H2O
?
-
lipase B is stereoselective for the R-isomer in an antichiral solvent such as isopentyl methyl ketone or S(+)-carvone
-
?
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
-
?
rape seed oil + H2O
?
-
-
-
?
retinyl palmitate + H2O
retinol + palmitate
rice bran oil
?
-
100% activity
-
-
?
safflower oil + H2O
?
-
-
-
?
soybean bran + H2O
?
-
-
-
-
?
sulcatol + fatty acid
?
-
esterification reaction, in toluene
-
?
terephthalate + ethanol
terephthalic acid monoethyl ester + terephthalic acid diethyl ester + H2O
-
-
the yield is 44% monoester and no diester in 1-butyl-3-methyl imidazolium tetrafluoroborate buffer and 39% monoester and 51% diester in 1-butyl-3-methyl imidazolium hexafluorophosphate buffer respectively
-
?
tert-butyl octanoate + H2O
tert-butanol + octanoate
-
preferred substrate, high activity with
-
?
tetradecyl acetate + H2O
tetradecanol + acetic acid
-
-
-
-
?
tetradecyl butyrate + H2O
tetradecanol + butyric acid
trans-3-(4'-methoxyphenyl) glycidic acid methyl ester + H2O
?
-
60% conversion
-
-
?
trans-3-(4-methoxyphenyl) glycidic acid methyl ester + H2O
?
triacetin + H2O
?
-
120% activity compared to rice bran oil
-
-
?
triacetin + H2O
diacetin + acetate
triacetin + H2O
diacetin + acetic acid
-
-
-
?
triacetylglycerol + H2O
acetic acid + ?
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
triarachidin + H2O
arachidonic acid + ?
-
-
-
-
?
tributyrin + 3 H2O
glycerol + 3 butyrate
tributyrin + H2O
butyric acid + ?
tributyrin + H2O
dibutyrin + butyrate
tributyrin + H2O
dibutyrin + butyric acid
tricaprin + H2O
dicaprin + caprate
tricaprin + H2O
dicaprin + capriate
tricaprin + H2O
dicaprin + capric acid
-
-
-
?
tricaprin + H2O
dicaprin + decaprate
tricaproin + H2O
dicaproin + caproate
tricaproin + H2O
dicaproin + caproic acid
tricaprylin + 3 H2O
3 octanoate + glycerol
the apparent rate of hydrolysis correlates with the degree of micellar formation. Consistent with observations from other lipases, the lid conformation may change from the closed to the open form in the presence of lipid interface. Together with the evidence of the lid structure in in this enzyme, it is classified as a lipase rather than as a carboxylesterase
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
tricaprylin + H2O
dicaprylin + caprylic acid
-
-
-
?
tridecanin + H2O
didecanin + decanoate
tridecanoate + H2O
?
-
-
-
?
tridodecanin + H2O
didodecanin + dodecanoate
Penicillium candidum
-
-
-
?
trieicosenoin + H2O
?
-
-
-
-
?
trielaidin + H2O
dielaidin + elaidiate
-
trans C18:1
-
?
trielaidin + H2O
dielaidin + elaidic acid
Geotrichum marinum
-
lower activity
-
-
?
trierucin + H2O
eicosanoic acid + ?
-
-
-
-
?
triethyl citrate + H2O
?
-
-
-
-
?
trihexanin + H2O
dihexanin + hexanoate
trihexanoin + H2O
hexanoic acid + ?
trilaurin + 3 H2O
glycerol + 3 laurate
trilaurin + H2O
?
-
-
-
?
trilaurin + H2O
dilaurin + laurate
trilaurin + H2O
dilaurin + lauric acid
-
-
-
?
trilaurin + H2O
lauric acid + ?
trilinolein + H2O
dilinolein + linoleate
trilinolein + H2O
linolic acid + ?
trilinolenein + H2O
linolenic acid + ?
-
-
-
-
?
trilinolenin + H2O
dilinolenin + linolenate
trilinolin + H2O
dilinolin + linolate
-
-
-
?
trimyristin + H2O
dimyristin + myristate
trimyristin + H2O
myristic acid + ?
trioctanin + H2O
dioctanin + octanoate
-
-
-
?
trioctanoate + H2O
dioctanoate + octanoate
-
-
-
-
?
trioctanoin + H2O
dioctanoin + octanoate
trioctanoin + H2O
octanoic acid + ?
trioctanoyl glycerol + H2O
?
-
-
-
-
?
triolein + 3 H2O
glycerol + 3 oleate
triolein + cinnamic acid
monocinnamoyl oleoyl glycerol + dicinnamoyl oleoyl glyerol + monocinnamoyl dioleoyl glycerol
-
transesterification
-
-
?
triolein + ferulic acid
monoferuloyl oleoyl glycerol + monoferuloyl dioleoyl glycerol
-
transesterification
-
-
?
triolein + H2O
1,2-diolein + oleate
triolein + H2O
diolein + oleate
triolein + H2O
diolein + oleic acid
trioleoylglycerol + H2O
oleic acid + ?
trioleoylglycerol + succinic acid
1,2-dioleoyl-3-succinoylglycerol + 2-oleoyl-1,3-succinoylglycerol
-
-
-
-
?
tripalmitin + 3 H2O
glycerol + 3 palmitate
-
42% activity compared to glyceryl tributyrate
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
tripalmitin + H2O
dipalmitin + palmitic acid
-
-
-
?
tripalmitin + H2O
palmitic acid + ?
tripalmitolein + H2O
?
-
highest activity
-
-
?
tripalmitolein + H2O
dipalmitolein + palmitate
-
-
-
?
tripalmitoylglycerol + succinic acid
1,2-dipalmitoyl-3-succinoylglycerol + 2-palmitoyl-1,3-disuccinoylglycerol
-
-
-
-
?
tripropionin + H2O
dipropionin + propanoate
-
-
-
-
?
tripropionin + H2O
dipropionin + propionate
tripropionin + H2O
propionic acid + ?
-
-
-
-
?
triricinolein + H2O
diricinolein + ricinolate
-
-
-
?
tristearin + 3 H2O
glycerol + 3 stearate
-
31% activity compared to glyceryl tributyrate
-
-
?
tristearin + H2O
distearin + stearate
tristearin + H2O
stearic acid + ?
trivaccinin + H2O
?
-
about 78% activity compared to olive oil
-
-
?
Tween 40 + H2O
?
-
i.e. poly(oxyethylene) sorbitan monopalmitate
-
?
Tween 60 + H2O
?
-
i.e. poly(oxyethylene) sorbitan monostearate
-
?
vinyl butyrate + H2O
ethenol + butyrate
-
-
-
-
?
vinyl propionate + H2O
?
-
-
-
?
vitamin A acetate + H2O
?
-
-
-
-
?
yeast hydrolysate + H2O
?
-
-
-
-
?
additional information
?
-
(R,S)-flurbiprofen ethyl ester + H2O
(S)-flurbiprofen + ethanol
-
enantioselective hydrolysis, kinetic resolution, overview
-
-
?
(R,S)-flurbiprofen ethyl ester + H2O
(S)-flurbiprofen + ethanol
high enantiomeric excess and conversion yield of 98% and 48%, respectively
-
-
?
(R,S)-flurbiprofen ethyl ester + H2O
(S)-flurbiprofen + ethanol
-
enantioselective hydrolysis, kinetic resolution, overview
-
-
?
(R,S)-flurbiprofen ethyl ester + H2O
(S)-flurbiprofen ethyl ester + (R)-flurbiprofen + ethanol
-
enantioselective reaction
-
-
?
(R,S)-flurbiprofen ethyl ester + H2O
(S)-flurbiprofen ethyl ester + (R)-flurbiprofen + ethanol
-
enantioselective reaction
-
-
?
(R,S)-ibuprofen + 1-propanol
(S)-ibuprofen n-propyl ester + (R)-ibuprofen
purified enzyme in a mixture of 1-propanol-isooctane in a ratio of 3:1, the conversion of racemic ibuprofen reaches 46% with very high enantioselectivity for production of the (S)-enantiomer
-
-
?
(R,S)-ibuprofen + 1-propanol
(S)-ibuprofen n-propyl ester + (R)-ibuprofen
purified enzyme in a mixture of 1-propanol-isooctane in a ratio of 3:1, the conversion of racemic ibuprofen reaches 46% with very high enantioselectivity for production of the (S)-enantiomer
-
-
?
(RS)-1-phenylethanol + vinyl acetate
(R)-1-phenylethyl acetate + acetaldehyde + (S)-1-phenylethanol
-
enantioselective esterification in vivo
-
-
ir
(RS)-1-phenylethanol + vinyl acetate
(R)-1-phenylethyl acetate + acetaldehyde + (S)-1-phenylethanol
-
enantioselective esterification
-
-
ir
1,2-didecanoyl-rac-glycerol + H2O
?
-
-
-
-
?
1,2-didecanoyl-rac-glycerol + H2O
?
-
-
-
-
?
1,2-dilauryl-rac-glycero-3-glutaric acid resorufinester + H2O
?
-
-
-
-
?
1,2-dilauryl-rac-glycero-3-glutaric acid resorufinester + H2O
?
-
-
-
-
?
1,2-dilauryl-rac-glycero-3-glutaric acid resorufinester + H2O
?
-
-
-
-
?
1,2-dilauryl-rac-glycero-3-glutaric acid resorufinester + H2O
?
-
-
-
-
?
1,2-dilauryl-rac-glycero-3-glutaric acid resorufinester + H2O
?
-
-
-
-
?
1,2-dilauryl-rac-glycero-3-glutaric acid resorufinester + H2O
?
-
-
-
-
?
1,2-dioctanoyl-sn-glycero-3-phosphocholine + H2O
?
-
-
-
?
1,2-dioctanoyl-sn-glycero-3-phosphocholine + H2O
?
-
-
-
?
1,2-dioleoylglycerol + H2O
oleic acid + ?
-
-
-
-
?
1,2-dioleoylglycerol + H2O
oleic acid + ?
-
-
-
-
?
1,2-dioleoylglycerol + H2O
oleic acid + ?
-
-
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
36.9% activity compared to rice bran oil
-
-
?
1-naphthyl acetate + H2O
1-naphthol + acetate
-
-
-
-
?
2,3-dimercapto-1-propanol tributyrate + H2O
?
-
regiospecificity study
-
?
2,3-dimercapto-1-propanol tributyrate + H2O
?
-
-
-
-
?
2,3-dimercaptopropan-1-ol tributyrate + H2O
?
-
-
-
?
2,3-dimercaptopropan-1-ol tributyrate + H2O
?
liberation of thiol groups by hydrolysis
-
-
?
2,3-dimercaptopropan-1-ol tributyrate + H2O
?
liberation of thiol groups by hydrolysis
-
-
?
2,3-dimercaptopropan-1-ol tributyrate + H2O
?
-
-
-
?
2-hexandecanoylthio-ethane-1-phosphocholine + H2O
?
-
-
-
?
2-hexandecanoylthio-ethane-1-phosphocholine + H2O
?
-
-
-
?
3-(4-methoxyphenyl)glycidic acid methyl ester + H2O
(2R,3S)-3-(4-methoxyphenyl)glycidic acid methyl ester + (2S,3R)-3-(4-methoxyphenyl)glycidic acid + methanol
-
-
-
-
?
3-(4-methoxyphenyl)glycidic acid methyl ester + H2O
(2R,3S)-3-(4-methoxyphenyl)glycidic acid methyl ester + (2S,3R)-3-(4-methoxyphenyl)glycidic acid + methanol
-
-
-
-
?
3-acetoxy beta-lactam + H2O
?
-
stereospecificity in hydrolysis of 3-acetoxy beta-lactam
-
-
?
3-acetoxy beta-lactam + H2O
?
-
stereospecificity in hydrolysis of 3-acetoxy beta-lactam
-
-
?
4-methylumbelliferyl butyrate + H2O
4-methylumbelliferol + butyrate
-
-
-
?
4-methylumbelliferyl butyrate + H2O
4-methylumbelliferol + butyrate
-
-
-
?
4-methylumbelliferyl butyrate + H2O
4-methylumbelliferone + butyrate
-
-
-
-
?
4-methylumbelliferyl butyrate + H2O
4-methylumbelliferone + butyrate
-
-
-
-
?
4-methylumbelliferyl butyrate + H2O
4-methylumbelliferone + butyrate
-
-
-
-
?
4-methylumbelliferyl oleate + H2O
4-methylumbelliferone + oleate
-
-
-
-
?
4-methylumbelliferyl oleate + H2O
4-methylumbelliferone + oleate
-
-
-
-
?
4-nitrophenol butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenol butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
about 30% activity compared to 4-nitrophenyl caprate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
low activity
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
highest activity with 4-nitrophenyl acetate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
highest activity with 4-nitrophenyl acetate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
low activity
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
about 88% activity compared to 4-nitrophenyl palmitate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
about 88% activity compared to 4-nitrophenyl palmitate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
low activity
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
100% activity
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
100% activity
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
about 45% activity compared to 4-nitrophenyl butyrate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
Cephaloleia presignis
-
low activity
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
12% of the activity with 4-nitrophenyl myristate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
12% of the activity with 4-nitrophenyl myristate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
0.2% activity compared to rice bran oil
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
worst substrate, less than 5% activity compared to 4-nitrophenyl laurate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
worst substrate, less than 5% activity compared to 4-nitrophenyl laurate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
about 34% activity compared to 4-nitrophenyl decanoate
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
about 34% activity compared to 4-nitrophenyl decanoate
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
20% of the activity with -nitrophenyl myristate
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
about 65% activity compared to 4-nitrophenyl caprate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
about 90% activity compared to 4-nitrophenyl palmitate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
about 90% activity compared to 4-nitrophenyl palmitate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
about 65% activity compared to 4-nitrophenyl acetate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
about 65% activity compared to 4-nitrophenyl acetate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
the enzyme shows a typical interfacial activation mechanism towards the substrate
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
the enzyme shows a typical interfacial activation mechanism towards the substrate
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
low activity
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
best substrate for wild type enzyme
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
low activity
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
Cephaloleia presignis
-
low activity
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
20% of the activity with 4-nitrophenyl myristate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
20% of the activity with 4-nitrophenyl myristate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
Penicillium candidum
-
low activity
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
high activity
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
high activity
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
low activity
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
low activity
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
low activity
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
high activity
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
about 10% activity compared to 4-nitrophenyl laurate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
about 10% activity compared to 4-nitrophenyl laurate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
about 42% activity compared to 4-nitrophenyl butyrate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
about 42% activity compared to 4-nitrophenyl butyrate
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
best substrate
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
best substrate
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
best substrate for isoforms FGL2 and FGL3
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
best 4-nitrophenyl ester substrate
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
-
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
best substrate
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
highest lipase activity is obtained with 0.25 mM of the substrate
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
best substrate
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
highest lipase activity is obtained with 0.25 mM of the substrate
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
best substrate
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
-
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
-
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
high activity
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
high activity
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
-
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
-
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
high activity
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
-
-
?
4-nitrophenyl caprate + H2O
4-nitrophenol + caprate
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
second-highest hydrolysis rate, about 95% activity compared to 4-nitrophenyl palmitate
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
second-highest hydrolysis rate, about 95% activity compared to 4-nitrophenyl palmitate
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
good substrate
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
best substrate
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
high activity
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
high activity
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
best substrate
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
high activity
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
high activity
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
low activity
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
low activity
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
about 85% activity compared to 4-nitrophenyl caprate
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
highest hydrolysis rate, about 90% activity compared to 4-nitrophenyl palmitate
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
best substrate
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
at 30°C, the enzyme prefers C8 synthetic substrate (4-nitrophenyl caprylate)to shorter or longer substrates
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
at 30°C, the enzyme prefers C8 synthetic substrate (4-nitrophenyl caprylate)to shorter or longer substrates
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
best substrate
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
highest activity of mutant enzyme S154L/S293L
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
highest activity of mutant enzyme S154L/S293L
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
preferred substrate of lipase A
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
best substrate for isoform FGL5
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
L1, best substrate
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
L1, best substrate
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
best substrate
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
high activity
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
high activity
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
preferred 4-nitrophenyl substrate of the recombinant enzyme
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
preferred 4-nitrophenyl substrate of the recombinant enzyme
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
best 4-nitrophenyl ester substrate
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
best 4-nitrophenyl ester substrate
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
about 70% activity compared to 4-nitrophenyl decanoate
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
about 10% activity compared to 4-nitrophenyl acetate
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
about 100% activity compared to 4-nitrophenyl butyrate
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
good substrate
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
preferred substrate of the native mature enzyme
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
preferred substrate of the native mature enzyme
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
85% of the activity with 4-nitrophenyl myristate
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
85% of the activity with 4-nitrophenyl myristate
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
81% of the activity with -nitrophenyl myristate
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
Penicillium candidum
-
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
-
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
about 30% activity compared to 4-nitrophenyl laurate
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
about 30% activity compared to 4-nitrophenyl laurate
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
about 25% activity compared to 4-nitrophenyl laurate
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
100% activity
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
100% activity
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
best substrate
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
best substrate
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
30% of the activity with 4-nitrophenyl myristate
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
30% of the activity with 4-nitrophenyl myristate
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
Penicillium candidum
-
low activity
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
low activity
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
about 40% activity compared to 4-nitrophenyl decanoate
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
about 40% activity compared to 4-nitrophenyl decanoate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
about 90% activity compared to 4-nitrophenyl caprate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
about 60% activity compared to 4-nitrophenyl palmitate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
enzyme shows a preference for lauric acid and a 1,3-position specificity
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
best substrate
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
about 80% activity compared to 4-nitrophenyl butyrate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
lowest activity of mutant enzyme S154L/S293L
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
lowest activity of mutant enzyme S154L/S293L
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
Cephaloleia presignis
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
best substrate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
preferred substrate of lipase B
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
best substrate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
best substrate for isoform FGL24
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
95% of the activity with 4-nitrophenyl myristate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
recombinant enzyme in Sf9 cells
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
Penicillium candidum
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
purified enzyme of strain F-111 shows preference for
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
high activity in a water-restricted environment containing a water content of 0.5-1% w/w
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
high activity in a water-restricted environment containing a water content of 0.5-1% w/w
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
maximum activity on 4-nitrophenyl laurate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
highest activity (100%)
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
about 65% activity compared to 4-nitrophenyl decanoate
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
about 50% activity compared to 4-nitrophenyl caprate
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
about 30% activity compared to 4-nitrophenyl palmitate
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
worst substrate, less than 5% activity compared to 4-nitrophenyl acetate
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
about 30% activity compared to 4-nitrophenyl butyrate
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
best substrate for isoform FGL1
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
-
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
maximal activity among the tested 4-nitrophenyl esters
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
-
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
purified enzyme of strain F-111 shows preference for
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
-
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
high activity
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
best 4-nitrophenyl ester substrate
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
preferred 4-nitrophenyl substrate of the wild-type enzyme
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
the enzyme shows maximum activity on 4-nitrophenyl myristate
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
about 90% activity compared to 4-nitrophenyl laurate
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
about 50% activity compared to 4-nitrophenyl laurate
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
about 10% activity compared to 4-nitrophenyl decanoate
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
-
best substrate
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
-
best substrate
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
-
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
preferred substrate of the recombinant mature lipase
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
preferred substrate of the recombinant mature lipase
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
-
70% of the activity with 4-nitrophenyl myristate
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
-
70% of the activity with 4-nitrophenyl myristate
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
Penicillium candidum
-
low activity
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
-
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
-
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
-
low activity
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
about 3% activity compared to 4-nitrophenyl laurate
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
-
-
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
-
-
-
-
?
4-nitrophenyl oleate + H2O
4-nitrophenol + oleate
Cephaloleia presignis
-
-
-
?
4-nitrophenyl oleate + H2O
4-nitrophenol + oleate
-
about 3% activity compared to 4-nitrophenyl decanoate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
about 40% activity compared to 4-nitrophenyl caprate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
the purified enzyme is most active toward 4-nitrophenyl palmitate (100% activity)
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
low activity
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
about 30% activity compared to 4-nitrophenyl butyrate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
low activity
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
in n-heptane
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
Cephaloleia presignis
-
high activity
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
lower activity
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
best substrate
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
best substrate
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
95% of the activity with 4-nitrophenyl myristate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
highest lipase activity is obtained with 0.25 mM of the substrate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
54% of the activity with -nitrophenyl myristate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
highest lipase activity is obtained with 0.25 mM of the substrate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
Penicillium candidum
-
best substrate
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
best substrate
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
high activity
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
best substrate
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
high activity
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
preferred substrate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
low activity
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
best substrate
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
best substrate
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
low activity
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
about 30% activity compared to 4-nitrophenyl laurate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
about 30% activity compared to 4-nitrophenyl laurate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
preferred substrate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
preferred substrate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
about 18% activity compared to 4-nitrophenyl laurate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
best substrate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
best substrate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
high activity
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
about 8% activity compared to 4-nitrophenyl decanoate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
high activity
-
-
?
4-nitrophenyl pentanoate + H2O
4-nitrophenol + pentanoate
-
-
-
?
4-nitrophenyl pentanoate + H2O
4-nitrophenol + pentanoate
-
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
-
about 60% activity compared to 4-nitrophenyl acetate
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
-
about 60% activity compared to 4-nitrophenyl acetate
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
Cephaloleia presignis
-
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
-
-
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
-
-
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
-
-
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
low activity
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
-
about 5% activity compared to 4-nitrophenyl laurate
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
-
about 5% activity compared to 4-nitrophenyl laurate
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
-
-
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
low activity
-
-
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
about 35% activity compared to 4-nitrophenyl caprate
-
-
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
-
-
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
low activity
-
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
-
-
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
-
-
-
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
about 15% activity compared to 4-nitrophenyl butyrate
-
-
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
-
-
-
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
-
-
-
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
90% of the activity with 4-nitrophenyl myristate
-
-
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
Penicillium candidum
-
-
-
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
-
-
-
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
-
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
-
-
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
-
-
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
-
-
-
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
-
-
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
-
-
-
?
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
about 6% activity compared to 4-nitrophenyl laurate
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
-
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
-
-
-
?
acylglycerol + H2O
glycerol + a carboxylate
-
-
-
-
?
acylglycerol + H2O
glycerol + a carboxylate
-
-
-
-
?
alpha-naphthyl butyrate + H2O
alpha-naphthol + butyrate
-
preferred substrate
-
?
alpha-naphthyl butyrate + H2O
alpha-naphthol + butyrate
-
preferred substrate
-
?
alpha-naphthyl caprylate + H2O
alpha-naphthol + caprylate
-
58% of the activity with the alpha-isomer
-
?
alpha-naphthyl caprylate + H2O
alpha-naphthol + caprylate
-
58% of the activity with the alpha-isomer
-
?
benzyl propionate + H2O
benzyl alcohol + propionate
-
950% activity compared to olive oil
-
-
?
benzyl propionate + H2O
benzyl alcohol + propionate
-
950% activity compared to olive oil
-
-
?
castor oil + H2O
?
-
-
-
?
castor oil + H2O
?
-
-
-
-
?
castor oil + H2O
?
-
-
-
-
?
castor oil + H2O
?
-
-
-
?
castor oil + H2O
?
-
major acyl group is ricinoleic acid
-
?
coconut oil + H2O
?
-
47.9% activity compared to rice bran oil
-
-
?
coconut oil + H2O
?
-
major acyl group is palmitic acid
-
?
corn oil + H2O
?
-
-
-
?
corn oil + H2O
?
-
-
-
-
?
corn oil + H2O
?
-
-
-
-
?
corn oil + H2O
?
-
major acyl groups are oleic acid and linoleic acid
-
?
cotton seed oil + H2O
?
-
-
-
?
cotton seed oil + H2O
?
-
-
-
?
cotton seed oil + H2O
?
-
-
-
?
diacylglycerol + H2O
acylglycerol + a carboxylate
-
-
-
-
?
diacylglycerol + H2O
acylglycerol + a carboxylate
-
-
-
-
?
dicaprin + H2O
caprin + caprate
-
hydrolyses more efficiently the 2,3-sn-dicaprin isomer than the 1,2-sn-dicaprin and the 1,3-sndicaprin monolayers
-
-
?
dicaprin + H2O
caprin + caprate
the three dicaprin isomers spread at the air-water interface, ROL29 prefers the distal ester groups of diglyceride isomer 1,3-sn-dicaprin, ROL32 is more stereoselective than ROL29 for the sn-3 position of the 2,3-sn-enantiomer of dicaprin
-
-
?
diolein + H2O
1-oleoyl-sn-glycerol + oleate
-
-
-
?
diolein + H2O
1-oleoyl-sn-glycerol + oleate
-
-
-
?
ethyl 2-arylpropanoate + H2O
ethanol + (R)-2-arylpropanoate
-
-
-
-
?
ethyl 2-arylpropanoate + H2O
ethanol + (R)-2-arylpropanoate
-
-
-
-
?
ethyl myristate + H2O
ethanol + myristic acid
-
-
-
-
?
ethyl myristate + H2O
ethanol + myristic acid
-
-
-
-
?
glyceryl trioctanoate + H2O
glycerol + octanoate
-
-
-
-
?
glyceryl trioctanoate + H2O
glycerol + octanoate
-
-
-
?
glyceryl trioleate + 3 H2O
glycerol + 3 oleate
-
14% activity compared to glyceryl tributyrate
-
-
?
glyceryl trioleate + 3 H2O
glycerol + 3 oleate
-
14% activity compared to glyceryl tributyrate
-
-
?
groundnut oil + H2O
?
-
major acyl group is oleic acid
-
?
groundnut oil + H2O
?
-
-
-
?
groundnut oil + H2O
?
-
-
-
?
hexadecyl butyrate + H2O
hexadecanol + butyric acid
-
-
-
-
?
hexadecyl butyrate + H2O
hexadecanol + butyric acid
-
-
-
-
?
hexadecyl formate + H2O
hexadecanol + formic acid
-
-
-
-
?
hexadecyl formate + H2O
hexadecanol + formic acid
-
-
-
-
?
hexadecyl propionate + H2O
hexadecanol + propionic acid
-
-
-
-
?
hexadecyl propionate + H2O
hexadecanol + propionic acid
-
-
-
-
?
high linoleic sunflower oil + H2O
?
-
-
-
-
?
high linoleic sunflower oil + H2O
?
-
-
-
-
?
high linoleic sunflower oil + H2O
?
-
-
-
-
?
high linoleic sunflower oil + H2O
?
-
-
-
-
?
high linoleic sunflower oil + H2O
?
-
-
-
-
?
high linoleic sunflower oil + H2O
?
-
-
-
-
?
high linoleic sunflower oil + H2O
?
-
-
-
-
?
high linoleic sunflower oil + H2O
?
-
-
-
-
?
high linoleic sunflower oil + H2O
?
-
-
-
-
?
high linoleic sunflower oil + H2O
?
-
-
-
-
?
high linoleic sunflower oil + H2O
?
-
-
-
-
?
high oleic sunflower oil + H2O
?
-
-
-
-
?
high oleic sunflower oil + H2O
?
-
-
-
-
?
high oleic sunflower oil + H2O
?
-
-
-
-
?
high oleic sunflower oil + H2O
?
-
-
-
-
?
high oleic sunflower oil + H2O
?
-
-
-
-
?
high oleic sunflower oil + H2O
?
-
-
-
-
?
high oleic sunflower oil + H2O
?
-
-
-
-
?
high oleic sunflower oil + H2O
?
-
-
-
-
?
high oleic sunflower oil + H2O
?
-
-
-
-
?
high oleic sunflower oil + H2O
?
-
-
-
-
?
high oleic sunflower oil + H2O
?
-
-
-
-
?
L-alpha-phosphatidylcholine + H2O
?
-
-
-
-
?
L-alpha-phosphatidylcholine + H2O
?
-
-
-
-
?
L-alpha-phosphatidylcholine + H2O
?
-
-
-
-
?
lard + H2O
?
-
-
-
-
?
long-chain triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
long-chain triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
methyl (R)-mandelate + H2O
(R)-mandelic acid + methanol
-
-
-
-
?
methyl (R)-mandelate + H2O
(R)-mandelic acid + methanol
-
-
-
-
?
methyl butyrate + H2O
methanol + butyrate
Cephaloleia presignis
-
-
-
?
methyl butyrate + H2O
methanol + butyrate
-
-
-
?
methyl butyrate + H2O
methanol + butyrate
-
-
-
?
methyl caprylate + H2O
methanol + caprylate
-
best substrate
-
-
?
methyl caprylate + H2O
methanol + caprylate
-
-
-
?
methyl laurate + H2O
methanol + laurate
Cephaloleia presignis
-
-
-
?
methyl laurate + H2O
methanol + laurate
-
-
-
-
?
methyl laurate + H2O
methanol + laurate
-
-
-
?
methyl linoleate + H2O
methanol + linolic acid
-
-
-
-
?
methyl linoleate + H2O
methanol + linolic acid
-
-
-
-
?
methyl linolenate + H2O
methanol + linoleic acid
-
-
-
-
?
methyl linolenate + H2O
methanol + linoleic acid
-
-
-
-
?
methyl myristate + H2O
methanol + myristate
-
-
-
?
methyl myristate + H2O
methanol + myristate
-
best fatty acid methyl ester substrate
-
-
?
methyl myristate + H2O
methanol + myristate
best fatty acid methyl ester substrate
-
-
?
methyl myristate + H2O
methanol + myristic acid
-
-
-
-
?
methyl myristate + H2O
methanol + myristic acid
-
-
-
-
?
methyl oleate + H2O
methanol + oleate
Cephaloleia presignis
-
high activity
-
?
methyl oleate + H2O
methanol + oleate
-
acylglycerol lipase activity, EC 3.1.1.23
-
-
?
methyl oleate + H2O
methanol + oleate
-
-
-
?
methyl oleate + H2O
methanol + oleic acid
-
-
-
-
?
methyl oleate + H2O
methanol + oleic acid
-
-
-
-
?
methyl oleate + H2O
methanol + oleic acid
-
-
-
-
?
methyl palmitate + H2O
methanol + palmitate
Cephaloleia presignis
-
high activity
-
?
methyl palmitate + H2O
methanol + palmitate
-
-
-
?
methyl propionate + H2O
methanol + propionate
Cephaloleia presignis
-
-
-
?
methyl propionate + H2O
methanol + propionate
-
-
-
?
methyl propionate + H2O
methanol + propionate
-
-
-
?
methyl stearate + H2O
methanol + stearate
Cephaloleia presignis
-
-
-
?
methyl stearate + H2O
methanol + stearate
-
-
-
?
monogalactosyldiacylglycerol + H2O
?
-
-
-
-
?
monogalactosyldiacylglycerol + H2O
?
-
-
-
-
?
mustard oil + H2O
?
-
-
-
-
?
mustard oil + H2O
?
-
-
-
-
?
mustard oil + H2O
?
-
major acyl groups are erucic and oleic acid
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
?
olive oil + H2O
?
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
the enzyme can tolerate the accumulation of long-chain free fatty acids at the interface when olive oil emulsion is used as substrate in the absence of bile salts and colipase
-
-
?
olive oil + H2O
?
-
emulsion
-
?
olive oil + H2O
?
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
95.3% activity compared to rice bran oil
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
?
olive oil + H2O
?
-
emulsion
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
best substrate, major acyl group is oleic acid
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
high activity
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
?
olive oil + H2O
?
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
?
olive oil + H2O
?
-
-
-
-
?
olive oil + H2O
?
-
-
-
?
olive oil + H2O
?
-
-
-
?
olive oil + H2O
?
-
-
-
?
olive oil + H2O
?
-
-
-
?
olive oil + H2O
?
-
purified emulsion
-
?
olive oil + H2O
?
-
-
-
?
olive oil + H2O
?
-
best substrate
-
-
?
p-nitrophenyl caprate + H2O
p-nitrophenol + caprate
-
highest activity with p-nitrophenyl caprate
-
-
?
p-nitrophenyl caprate + H2O
p-nitrophenol + caprate
-
highest activity with p-nitrophenyl caprate
-
-
?
p-nitrophenyl caprate + H2O
p-nitrophenol + caprate
-
highest activity with p-nitrophenyl caprate
-
-
?
palm olein + H2O
oleic acid + ?
-
-
-
-
?
palm olein + H2O
oleic acid + ?
-
-
-
-
?
peanut oil + H2O
?
-
-
-
?
peanut oil + H2O
?
-
highest hydrolytic activity towards peanut oil
-
-
?
peanut oil + H2O
?
-
-
-
?
peanut oil + H2O
?
-
highest hydrolytic activity towards peanut oil
-
-
?
phosphatidylcholine + H2O
?
-
-
-
-
?
phosphatidylcholine + H2O
?
from hen egg
-
-
?
phosphatidylcholine + H2O
?
from hen egg
-
-
?
phosphatidylethanolamine + H2O
?
-
-
-
-
?
phosphatidylethanolamine + H2O
?
-
-
-
-
?
phosphatidylethanolamine + H2O
?
-
-
-
?
phosphatidylethanolamine + H2O
?
-
-
-
-
?
phosphatidylglycerol + H2O
?
-
-
-
-
?
phosphatidylglycerol + H2O
?
-
-
-
-
?
polyethylene sorbitan monooleate + H2O
?
-
-
-
-
?
polyethylene sorbitan monooleate + H2O
?
-
i.e. Tween 80
-
-
?
retinyl palmitate + H2O
retinol + palmitate
-
-
-
?
retinyl palmitate + H2O
retinol + palmitate
-
-
-
?
sardine oil + H2O
?
-
the lipase is used for hydrolysis of triacylglycerol in sardine oil to enrich DELTA5-polyunsaturated fatty acids namely, arachidonic acid and eicosapentaenoic acid
-
-
?
sardine oil + H2O
?
-
the lipase is used for hydrolysis of triacylglycerol in sardine oil to enrich DELTA5-polyunsaturated fatty acids namely, arachidonic acid and eicosapentaenoic acid
-
-
?
soybean oil + H2O
?
-
-
-
-
?
soybean oil + H2O
?
-
-
-
-
?
soybean oil + H2O
?
-
-
-
-
?
soybean oil + H2O
?
-
-
-
?
soybean oil + H2O
?
-
-
-
?
soybean oil + H2O
?
-
-
-
-
?
soybean oil + H2O
?
-
-
-
-
?
soybean oil + H2O
?
-
-
-
?
soybean oil + H2O
?
-
-
-
-
?
soybean oil + H2O
?
-
-
-
-
?
soybean oil + H2O
?
-
concentrated soybean oil, high activity in a water-restricted environment containing a water content of 0.5-1% w/w
-
-
?
soybean oil + H2O
?
-
concentrated soybean oil, high activity in a water-restricted environment containing a water content of 0.5-1% w/w
-
-
?
soybean oil + H2O
?
-
major acyl groups are oleic acid and linoleic acid
-
?
soybean oil + H2O
?
-
-
-
?
soybean oil + H2O
?
substrate is stabilized with egg yolk lecithin
-
-
?
Span 85 + H2O
?
-
-
-
-
?
Span 85 + H2O
?
-
-
-
-
?
sunflower oil + H2O
?
-
91.7% activity compared to rice bran oil
-
-
?
sunflower oil + H2O
?
-
major acyl group is linoleic acid
-
?
tetradecyl butyrate + H2O
tetradecanol + butyric acid
-
-
-
-
?
tetradecyl butyrate + H2O
tetradecanol + butyric acid
-
-
-
-
?
trans-3-(4-methoxyphenyl) glycidic acid methyl ester + H2O
?
-
i.e. (+-)-methyl trans-3(4-methoxyphenyl) glycidate, the substrate is a key intermediate in the synthesis of cardiovascular drug, diltiazem
-
-
?
trans-3-(4-methoxyphenyl) glycidic acid methyl ester + H2O
?
-
i.e. (+-)-methyl trans-3(4-methoxyphenyl) glycidate, the substrate is a key intermediate in the synthesis of cardiovascular drug, diltiazem
-
-
?
triacetin + H2O
diacetin + acetate
-
-
-
?
triacetin + H2O
diacetin + acetate
-
-
-
?
triacetin + H2O
diacetin + acetate
-
poor substrate
-
?
triacetin + H2O
diacetin + acetate
-
-
-
-
?
triacetin + H2O
diacetin + acetate
-
-
-
-
ir
triacetin + H2O
diacetin + acetate
-
-
-
-
?
triacetin + H2O
diacetin + acetate
-
-
-
-
?
triacetin + H2O
diacetin + acetate
-
low activity
-
?
triacetin + H2O
diacetin + acetate
-
368% activity compared to olive oil
-
-
?
triacetin + H2O
diacetin + acetate
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
the strain HH-01 degrades 1.0% (v/v) edible oil in nutrient broth, almost completely within 10 days
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
the strain HH-01 degrades 1.0% (v/v) edible oil in nutrient broth, almost completely within 10 days
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
the seed enzyme shows a preference for triglyceride with natural monounsaturated fatty acids
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
ATGL plays a pivotal role for ATGL in intramuscular fatty acid handling, lipid storage and breakdown, overview, disturbances in skeletal muscle lipid turnover and lipolysis lead to accumulation of triacylglycerol and lipid intermediates in skeletal muscle, which plays an important role in the etiology of insulin resistance and type 2 diabetes mellitus
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
endothelial lipase plays a central role in plasma lipoprotein metabolism
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
the endothelial lipase is more active as a phospholipase than as a triacylglyceride lipase
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
the enzyme is involved in adipokinetic hormone-induced mobilization of fat body triglyceride stores in Manduca sexta, protein kinase A phosphorylates and activates the TG-lipase substrate, the lipid droplets, protein kinase A also phosphorylates the lipase, but does not directly activate it, overview
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
the enzyme specifically generates sn-1,3 and, in the presence of its co-activator CGI-58, sn-1,3 and sn-2,3 diacylglycerol
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
the enzyme specifically generates sn-1,3 and, in the presence of its co-activator CGI-58, sn-1,3 and sn-2,3 diacylglycerol
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
the enzyme acts on triacylglycerols with medium fatty acid chain length, substrate specificity, overview
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
of several natural oils, e.g. cottonseed oil, corn oil, palm oil, wheatgerm oil, soybean oil, rapeseed oil, coconut oil, linseed oil, peanut oil, and olive oil in descending activity, overview
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
of several natural oils, e.g. cottonseed oil, corn oil, palm oil, wheatgerm oil, soybean oil, rapeseed oil, coconut oil, linseed oil, peanut oil, and olive oil in descending activity, overview
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
triacylglycerol + H2O
diacylglycerol + a carboxylate
-
-
-
-
?
tributyrin + 3 H2O
glycerol + 3 butyrate
-
100% activity
-
-
?
tributyrin + 3 H2O
glycerol + 3 butyrate
-
100% activity
-
-
?
tributyrin + 3 H2O
glycerol + 3 butyrate
-
-
-
?
tributyrin + 3 H2O
glycerol + 3 butyrate
-
-
-
?
tributyrin + H2O
?
-
-
-
-
?
tributyrin + H2O
?
-
-
-
-
?
tributyrin + H2O
?
-
92.6% activity compared to rice bran oil
-
-
?
tributyrin + H2O
?
-
-
-
-
?
tributyrin + H2O
?
-
-
-
?
tributyrin + H2O
butyric acid + ?
-
-
-
-
?
tributyrin + H2O
butyric acid + ?
-
-
-
-
?
tributyrin + H2O
butyric acid + ?
-
-
-
-
?
tributyrin + H2O
butyric acid + ?
-
-
-
-
?
tributyrin + H2O
butyric acid + ?
-
-
-
-
?
tributyrin + H2O
butyric acid + ?
-
-
-
?
tributyrin + H2O
butyric acid + ?
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
Alcaligenes ssp.
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
preferred substrate
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
Cephaloleia presignis
-
best substrate
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
r
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
best substrate
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
best substrate
-
?
tributyrin + H2O
dibutyrin + butyrate
-
best substrate
-
?
tributyrin + H2O
dibutyrin + butyrate
-
best substrate
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
not BTID-A
-
?
tributyrin + H2O
dibutyrin + butyrate
-
not BTID-A
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
nonphysiologic substrate
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
best substrate, efficient hydrolysis in the absence of colipase and bile salts
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
best substrate
-
?
tributyrin + H2O
dibutyrin + butyrate
-
best substrate
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
Penicillium candidum
-
best substrate
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
Penicillium wortmanii
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
best substrate
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
best substrate
-
?
tributyrin + H2O
dibutyrin + butyrate
Q9EV86
preferred substrate
-
-
?
tributyrin + H2O
dibutyrin + butyrate
Q9EV86
preferred substrate
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
744% activity compared to olive oil
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
744% activity compared to olive oil
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
best triacylglyceride substrate for the wild-type enzyme
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
partially hydrolysed by isozyme SCO1725
-
-
?
tributyrin + H2O
dibutyrin + butyrate
partially hydrolysed by isozyme SCO1725
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
preferred substrate
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
?
tributyrin + H2O
dibutyrin + butyrate
-
-
-
-
?
tributyrin + H2O
dibutyrin + butyric acid
-
-
-
?
tributyrin + H2O
dibutyrin + butyric acid
-
-
-
?
tricaprin + H2O
?
-
-
-
-
?
tricaprin + H2O
?
-
-
-
-
?
tricaprin + H2O
dicaprin + caprate
-
-
-
-
?
tricaprin + H2O
dicaprin + caprate
-
high activity
-
-
?
tricaprin + H2O
dicaprin + caprate
-
best substrate
-
?
tricaprin + H2O
dicaprin + caprate
-
-
-
?
tricaprin + H2O
dicaprin + caprate
-
-
-
?
tricaprin + H2O
dicaprin + caprate
best triacylglyceride substrate
-
-
?
tricaprin + H2O
dicaprin + caprate
-
-
-
-
?
tricaprin + H2O
dicaprin + capriate
-
-
-
?
tricaprin + H2O
dicaprin + capriate
-
best substrate
-
?
tricaprin + H2O
dicaprin + decaprate
-
about 20% of the activity with tributyrin
-
?
tricaprin + H2O
dicaprin + decaprate
-
-
-
?
tricaprin + H2O
dicaprin + decaprate
-
-
-
?
tricaproin + H2O
dicaproin + caproate
-
-
-
?
tricaproin + H2O
dicaproin + caproate
-
-
-
-
?
tricaproin + H2O
dicaproin + caproate
-
about 20% of the activity with tributyrin
-
?
tricaproin + H2O
dicaproin + caproate
-
not BTID-A
-
?
tricaproin + H2O
dicaproin + caproate
-
high activity
-
-
?
tricaproin + H2O
dicaproin + caproate
-
best substrate
-
?
tricaproin + H2O
dicaproin + caproate
-
-
-
?
tricaproin + H2O
dicaproin + caproic acid
-
-
-
?
tricaproin + H2O
dicaproin + caproic acid
-
-
-
?
tricaprylin + H2O
?
-
-
-
?
tricaprylin + H2O
?
-
-
-
?
tricaprylin + H2O
?
-
-
-
-
?
tricaprylin + H2O
?
-
-
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
good substrate
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
best substrate
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
best substrate
-
?
tricaprylin + H2O
dicaprylin + caprylate
best substrate
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
-
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
-
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
-
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
-
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
best substrate
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
best substrate
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
best substrate, BTID-A and BTID-B
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
best triacylglyceride substrate
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
best substrate, BTID-A and BTID-B
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
-
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
preferred substrate
-
-
ir
tricaprylin + H2O
dicaprylin + caprylate
-
best substrate
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
best substrate
-
?
tricaprylin + H2O
dicaprylin + caprylate
Q9EV86
-
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
89% activity compared to olive oil
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
-
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
-
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
best substrate
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
-
-
-
?
tricaprylin + H2O
dicaprylin + caprylate
-
-
-
-
?
tridecanin + H2O
didecanin + decanoate
Penicillium candidum
-
-
-
?
tridecanin + H2O
didecanin + decanoate
-
-
-
?
trihexanin + H2O
dihexanin + hexanoate
Penicillium candidum
-
-
-
?
trihexanin + H2O
dihexanin + hexanoate
-
-
-
?
trihexanoin + H2O
hexanoic acid + ?
-
-
-
-
?
trihexanoin + H2O
hexanoic acid + ?
-
-
-
-
?
trihexanoin + H2O
hexanoic acid + ?
-
-
-
-
?
trihexanoin + H2O
hexanoic acid + ?
-
-
-
-
?
trilaurin + 3 H2O
glycerol + 3 laurate
-
66% activity compared to glyceryl tributyrate
-
-
?
trilaurin + 3 H2O
glycerol + 3 laurate
-
66% activity compared to glyceryl tributyrate
-
-
?
trilaurin + H2O
dilaurin + laurate
Cephaloleia presignis
-
high activity
-
?
trilaurin + H2O
dilaurin + laurate
-
-
-
-
?
trilaurin + H2O
dilaurin + laurate
-
-
-
-
?
trilaurin + H2O
dilaurin + laurate
-
-
-
?
trilaurin + H2O
dilaurin + laurate
-
about 10% of the activity with tributyrin
-
?
trilaurin + H2O
dilaurin + laurate
-
about 10% of the activity with tributyrin
-
?
trilaurin + H2O
dilaurin + laurate
-
-
-
?
trilaurin + H2O
dilaurin + laurate
-
-
-
?
trilaurin + H2O
dilaurin + laurate
-
-
-
?
trilaurin + H2O
dilaurin + laurate
-
-
-
?
trilaurin + H2O
dilaurin + laurate
-
-
-
?
trilaurin + H2O
dilaurin + laurate
Q9EV86
-
-
-
?
trilaurin + H2O
dilaurin + laurate
Q9EV86
-
-
-
?
trilaurin + H2O
dilaurin + laurate
-
-
-
?
trilaurin + H2O
dilaurin + laurate
high activity
-
-
?
trilaurin + H2O
dilaurin + laurate
-
low activity
-
-
?
trilaurin + H2O
lauric acid + ?
-
-
-
-
?
trilaurin + H2O
lauric acid + ?
-
-
-
-
?
trilaurin + H2O
lauric acid + ?
-
-
-
-
?
trilaurin + H2O
lauric acid + ?
-
-
-
-
?
trilaurin + H2O
lauric acid + ?
-
-
-
-
?
trilinolein + H2O
?
-
about 105% activity compared to olive oil
-
-
?
trilinolein + H2O
?
-
lowest activity
-
-
?
trilinolein + H2O
?
-
lowest activity
-
-
?
trilinolein + H2O
dilinolein + linoleate
-
trans C18:1(9)
-
?
trilinolein + H2O
dilinolein + linoleate
-
trans C18:1(9)
-
?
trilinolein + H2O
dilinolein + linoleate
-
the enzyme shows preferential hydrolysis of the 1(3)-position ester bond in trilinolein
-
-
?
trilinolein + H2O
dilinolein + linoleate
Geotrichum marinum
-
good substrate
-
-
?
trilinolein + H2O
dilinolein + linoleate
-
-
-
?
trilinolein + H2O
dilinolein + linoleate
-
-
-
-
?
trilinolein + H2O
dilinolein + linoleate
-
-
-
?
trilinolein + H2O
linolic acid + ?
-
-
-
-
?
trilinolein + H2O
linolic acid + ?
-
-
-
-
?
trilinolenin + H2O
?
-
about 100% activity compared to olive oil
-
-
?
trilinolenin + H2O
?
-
-
-
-
?
trilinolenin + H2O
?
-
-
-
-
?
trilinolenin + H2O
dilinolenin + linolenate
Geotrichum marinum
-
preferred substrate
-
-
?
trilinolenin + H2O
dilinolenin + linolenate
-
-
-
?
trimyristin + H2O
?
-
90.1% activity compared to rice bran oil
-
-
?
trimyristin + H2O
?
-
-
-
?
trimyristin + H2O
dimyristin + myristate
-
about 10% of the activity with tributyrin
-
?
trimyristin + H2O
dimyristin + myristate
-
-
-
?
trimyristin + H2O
dimyristin + myristate
-
-
-
-
?
trimyristin + H2O
dimyristin + myristate
Penicillium candidum
-
-
-
?
trimyristin + H2O
dimyristin + myristate
-
-
-
-
?
trimyristin + H2O
dimyristin + myristate
-
-
-
-
?
trimyristin + H2O
dimyristin + myristate
-
low activity
-
?
trimyristin + H2O
dimyristin + myristate
Q9EV86
-
-
-
?
trimyristin + H2O
dimyristin + myristate
best triacylglyceride substrate
-
-
?
trimyristin + H2O
dimyristin + myristate
-
-
-
-
?
trimyristin + H2O
dimyristin + myristate
-
-
-
-
?
trimyristin + H2O
dimyristin + myristate
-
-
-
?
trimyristin + H2O
myristic acid + ?
-
-
-
-
?
trimyristin + H2O
myristic acid + ?
-
-
-
-
?
trimyristin + H2O
myristic acid + ?
-
-
-
-
?
trioctanoin + H2O
?
-
about 59% activity compared to olive oil
-
-
?
trioctanoin + H2O
?
-
about 59% activity compared to olive oil
-
-
?
trioctanoin + H2O
?
-
-
-
?
trioctanoin + H2O
dioctanoin + octanoate
-
-
-
-
?
trioctanoin + H2O
dioctanoin + octanoate
-
-
-
-
?
trioctanoin + H2O
dioctanoin + octanoate
-
-
-
-
?
trioctanoin + H2O
dioctanoin + octanoate
-
-
-
?
trioctanoin + H2O
dioctanoin + octanoate
-
-
-
?
trioctanoin + H2O
dioctanoin + octanoate
-
-
-
?
trioctanoin + H2O
octanoic acid + ?
-
-
-
-
?
trioctanoin + H2O
octanoic acid + ?
-
-
-
-
?
triolein + 3 H2O
glycerol + 3 oleate
-
-
enzyme can hydrolyze all positions of the ester bonds in triolein
-
?
triolein + 3 H2O
glycerol + 3 oleate
-
-
enzyme can hydrolyze all positions of the ester bonds in triolein
-
?
triolein + H2O
1,2-diolein + oleate
-
-
-
-
?
triolein + H2O
1,2-diolein + oleate
-
-
-
-
?
triolein + H2O
1,2-diolein + oleate
-
-
-
-
?
triolein + H2O
1,2-diolein + oleate
-
-
-
-
?
triolein + H2O
1,2-diolein + oleate
-
-
-
?
triolein + H2O
1,2-diolein + oleate
the enzyme shows a preference for the hydrolysis of the sn-3 ester bond of triolein compared to the sn-1 position
higher amount of 1,2-diolein
-
?
triolein + H2O
?
-
cleavage occurs only at the Sn-1 and Sn-3 positions
-
-
?
triolein + H2O
?
-
cleavage occurs only at the Sn-1 and Sn-3 positions
-
-
?
triolein + H2O
?
-
-
-
-
?
triolein + H2O
?
-
-
-
-
?
triolein + H2O
?
-
-
-
-
?
triolein + H2O
?
-
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
?
triolein + H2O
diolein + oleate
low activity
-
-
?
triolein + H2O
diolein + oleate
-
cis-C18:1(9)
-
?
triolein + H2O
diolein + oleate
-
cis-C18:1(9)
-
?
triolein + H2O
diolein + oleate
-
preferred substrate of enzyme form L1
-
?
triolein + H2O
diolein + oleate
-
low activity
-
?
triolein + H2O
diolein + oleate
-
low activity
-
?
triolein + H2O
diolein + oleate
-
-
-
?
triolein + H2O
diolein + oleate
-
hydrolysis at all positions, strain J33
-
?
triolein + H2O
diolein + oleate
-
hydrolysis at all positions, strain J33
-
?
triolein + H2O
diolein + oleate
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
olive oil in aqueous solution, enantioselective hydrolysis
-
-
?
triolein + H2O
diolein + oleate
Cephaloleia presignis
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
r
triolein + H2O
diolein + oleate
-
good substrate
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
?
triolein + H2O
diolein + oleate
-
olive oil
-
-
?
triolein + H2O
diolein + oleate
-
olive oil
-
-
?
triolein + H2O
diolein + oleate
Geotrichum marinum
-
good substrate
-
-
?
triolein + H2O
diolein + oleate
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
substrate is an olive oil/gum arabic emulsion containing radiolabeled triolein in presence of bile acids and lecithin at rate-limiting concentrations, rapid exchange of the enzyme between two different triacylglycerol droplets measured by a non-exchanging enzyme inhibitor orlistat in one of the droplets
-
-
?
triolein + H2O
diolein + oleate
-
olive oil
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
enzyme shows no positional specificity towards the triacylglycerol
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
Penicillium candidum
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
olive oil with predominantly triolein, regiospecificity for the 1- and 3-oleoyl residues
-
-
?
triolein + H2O
diolein + oleate
-
olive oil with predominantly triolein, regiospecificity for the 1- and 3-oleoyl residues
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
cleaves mainly 1,3-ester bonds, and to a lesser extent the 2-position ester bond
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
cleaves mainly 1,3-ester bonds, and to a lesser extent the 2-position ester bond
-
?
triolein + H2O
diolein + oleate
Q9EV86
low activity
-
-
?
triolein + H2O
diolein + oleate
Q9EV86
low activity
-
-
?
triolein + H2O
diolein + oleate
-
-
-
?
triolein + H2O
diolein + oleate
-
110% activity compared to olive oil
-
-
?
triolein + H2O
diolein + oleate
-
110% activity compared to olive oil
-
-
?
triolein + H2O
diolein + oleate
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
?
triolein + H2O
diolein + oleate
-
olive oil
-
-
?
triolein + H2O
diolein + oleate
-
olive oil
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
olive oil
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
-
?
triolein + H2O
diolein + oleate
-
low activity
-
?
triolein + H2O
diolein + oleate
-
low activity
-
?
triolein + H2O
diolein + oleate
-
cis C18:1
main product is oleic acid, further products are 1,3-dioleylglycerol, 1,2-dioleylglycerol, 2,3-dioleylglycerol, and minor product is 1-monooleylglycerol
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
substrate is an olive oil/gum arabic emulsion containing radiolabeled triolein in presence of bile acids and lecithin at rate-limiting concentrations, rapid exchange of the enzyme between two different triacylglycerol droplets measured by a non-exchanging enzyme inhibitor in one of the droplets
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
?
triolein + H2O
diolein + oleate
-
-
-
-
?
triolein + H2O
diolein + oleic acid
-
-
-
?
triolein + H2O
diolein + oleic acid
-
-
-
?
triolein + H2O
diolein + oleic acid
-
-
-
?
triolein + H2O
diolein + oleic acid
-
-
-
?
trioleoylglycerol + H2O
oleic acid + ?
-
-
-
-
?
trioleoylglycerol + H2O
oleic acid + ?
-
-
-
-
?
trioleoylglycerol + H2O
oleic acid + ?
-
-
-
-
?
trioleoylglycerol + H2O
oleic acid + ?
-
-
-
-
?
trioleoylglycerol + H2O
oleic acid + ?
-
-
-
-
?
trioleoylglycerol + H2O
oleic acid + ?
-
-
-
-
?
trioleoylglycerol + H2O
oleic acid + ?
-
-
-
-
?
trioleoylglycerol + H2O
oleic acid + ?
-
-
-
-
?
trioleoylglycerol + H2O
oleic acid + ?
-
-
-
-
?
trioleoylglycerol + H2O
oleic acid + ?
-
-
-
?
trioleoylglycerol + H2O
oleic acid + ?
-
-
-
-
?
trioleoylglycerol + H2O
oleic acid + ?
-
-
-
-
?
trioleoylglycerol + H2O
oleic acid + ?
-
-
-
-
?
trioleoylglycerol + H2O
oleic acid + ?
-
-
-
-
?
trioleoylglycerol + H2O
oleic acid + ?
-
-
-
-
?
tripalmitin + H2O
?
-
about 45% activity compared to olive oil
-
-
?
tripalmitin + H2O
?
-
82.1% activity compared to rice bran oil
-
-
?
tripalmitin + H2O
?
-
-
-
-
?
tripalmitin + H2O
?
-
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
Cephaloleia presignis
-
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
-
-
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
-
-
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
-
low activity with isozyme LIP II, residual activity with isozyme LIP I
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
-
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
-
about 20% of the activity with tributyrin
-
?
tripalmitin + H2O
dipalmitin + palmitate
-
about 20% of the activity with tributyrin
-
?
tripalmitin + H2O
dipalmitin + palmitate
-
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
-
high activity
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
-
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
Penicillium candidum
-
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
-
low activity
-
?
tripalmitin + H2O
dipalmitin + palmitate
Q9EV86
-
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
Q9EV86
-
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
-
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
-
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
high activity
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
-
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
-
-
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
-
-
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
low activity
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
-
low activity
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
-
-
-
?
tripalmitin + H2O
dipalmitin + palmitate
-
low activity
-
-
?
tripalmitin + H2O
palmitic acid + ?
-
-
-
-
?
tripalmitin + H2O
palmitic acid + ?
-
-
-
-
?
tripalmitin + H2O
palmitic acid + ?
-
-
-
-
?
tripalmitin + H2O
palmitic acid + ?
-
-
-
-
?
tripalmitin + H2O
palmitic acid + ?
-
-
-
-
?
tripalmitin + H2O
palmitic acid + ?
-
-
-
-
?
tripalmitin + H2O
palmitic acid + ?
-
-
-
-
?
tripalmitin + H2O
palmitic acid + ?
-
-
-
-
?
tripalmitin + H2O
palmitic acid + ?
-
-
-
-
?
tripropionin + H2O
dipropionin + propionate
-
the enzyme shows a typical interfacial activation mechanism towarsd the substrate
-
?
tripropionin + H2O
dipropionin + propionate
-
the enzyme shows a typical interfacial activation mechanism towarsd the substrate
-
?
tripropionin + H2O
dipropionin + propionate
Cephaloleia presignis
-
-
-
?
tripropionin + H2O
dipropionin + propionate
-
-
-
?
tripropionin + H2O
dipropionin + propionate
-
-
-
-
?
tripropionin + H2O
dipropionin + propionate
-
-
-
-
?
tripropionin + H2O
dipropionin + propionate
-
-
-
?
tripropionin + H2O
dipropionin + propionate
-
-
-
-
?
tripropionin + H2O
dipropionin + propionate
-
-
?
tristearin + H2O
?
-
about 38% activity compared to olive oil
-
-
?
tristearin + H2O
?
-
72.9% activity compared to rice bran oil
-
-
?
tristearin + H2O
?
-
-
-
-
?
tristearin + H2O
?
-
-
-
?
tristearin + H2O
distearin + stearate
-
-
-
?
tristearin + H2O
distearin + stearate
-
about 10% of the activity with tributyrin
-
?
tristearin + H2O
distearin + stearate
-
-
-
?
tristearin + H2O
distearin + stearate
Penicillium candidum
-
-
-
?
tristearin + H2O
distearin + stearate
-
-
-
?
tristearin + H2O
distearin + stearate
Q9EV86
low activity
-
-
?
tristearin + H2O
distearin + stearate
-
-
-
?
tristearin + H2O
distearin + stearate
-
-
-
-
?
tristearin + H2O
distearin + stearate
-
low activity
-
-
?
tristearin + H2O
distearin + stearate
-
-
-
?
tristearin + H2O
distearin + stearate
-
low activity
-
-
?
tristearin + H2O
stearic acid + ?
-
-
-
-
?
tristearin + H2O
stearic acid + ?
-
-
-
-
?
tristearin + H2O
stearic acid + ?
-
-
-
-
?
tristearin + H2O
stearic acid + ?
-
-
-
-
?
tristearin + H2O
stearic acid + ?
-
-
-
-
?
tristearin + H2O
stearic acid + ?
-
-
-
-
?
Tween 20 + H2O
?
-
-
-
?
Tween 20 + H2O
?
-
i.e. poly(oxyethylene) sorbitan monolaurate
-
?
Tween 80 + H2O
?
-
-
-
-
?
Tween 80 + H2O
?
-
i.e. poly(oxyethylene) sorbitan monooleate
-
?
Tween 80 + H2O
?
-
i.e. poly(oxyethylene) sorbitan monooleate
-
?
vinyl butyrate + H2O
?
-
-
-
?
vinyl butyrate + H2O
?
-
-
-
?
additional information
?
-
-
the enzyme 11folds favorably catalyzes the hydrolysis of rice bran oil, sesame oil, and coconut oil in comparison to palm oil. The transesterification activity of palm oil to fatty acid methyl esters reveals 31.64% after 48h. Wasting palm oil shows the highest activity among all oil substrates tested (about 1300% activity compared to palm oil). COmpared to palm oil, the enzyme shows about 150% activity with sunflower oil, about 150% activity with safflower oil, about 300% activity with canola oil, about 300% activity with olive oil, about 100% activity with soybean oil, and about 600% activity with camellia tea oil
-
-
?
additional information
?
-
-
maximal activity with fatty acid chain length of 14 carbon atoms, similarly active with the diacylglycerols and triacylglycerols and more active with oleic acid than with stearic acid
-
-
?
additional information
?
-
-
substrates are long acyl chain 4-nitrophenol esters
-
?
additional information
?
-
-
maximal activity with fatty acid chain length of 14 carbon atoms, similarly active with the diacylglycerols and triacylglycerols and more active with oleic acid than with stearic acid
-
-
?
additional information
?
-
-
substrates are long acyl chain 4-nitrophenol esters
-
?
additional information
?
-
-
substrate specificity, enzyme prefers substrates of medium- and long-chain fatty acids
-
?
additional information
?
-
-
broad specificity towards the acyl group (C8-C16) of ethyl esters
-
-
?
additional information
?
-
-
substrate specificity, enzyme prefers substrates of medium- and long-chain fatty acids
-
?
additional information
?
-
-
medium chain acyl group p-nitrophenyl esters are good substrate, increased activity with detergents
-
-
?
additional information
?
-
-
medium chain acyl group p-nitrophenyl esters are good substrate, increased activity with detergents
-
-
?
additional information
?
-
Alcaligenes ssp.
-
enzyme does not possess protease activity and does not hydrolyze peptide bonds, no activity with N-benzoyl-L-tyrosine 4-nitroanilide
-
?
additional information
?
-
-
the enzyme also uses olive oil (100% activity), corn oil (about 85% activity), castor oil (about 80% activity), sunflower oil (about 95% activity), rape seed oil (about 85% activity), linseed oil (about 75% activity), cotton seed (about 90% activity), and jojoba oil (about 83% activity) as substrates
-
-
?
additional information
?
-
-
the enzyme also uses olive oil (100% activity), corn oil (about 85% activity), castor oil (about 80% activity), sunflower oil (about 95% activity), rape seed oil (about 85% activity), linseed oil (about 75% activity), cotton seed (about 90% activity), and jojoba oil (about 83% activity) as substrates
-
-
?
additional information
?
-
the enzyme is involved in but not essential for breakdoen of stored triacylglycerides during germination
-
-
?
additional information
?
-
no activity with olein, digalactosyldiacylglycerol, galactosyldiacylglycerol, phosphatidylcholine, and cholesterol oleate
-
-
?
additional information
?
-
-
the enzyme utilizes olive oil as a substrate, no activity with 2-nitrophenyl palmitate
-
?
additional information
?
-
-
AFL1-1 has potential enantioselectivity for the ability to catalyze methyl 3-(4-methoxyphenyl) glycidate and methyl 3-phenylglycidate
-
-
?
additional information
?
-
-
almost no activity on long-chained acyl esters such as 4-nitrophenyl palmitate
-
-
?
additional information
?
-
-
AFL1-1 has potential enantioselectivity for the ability to catalyze methyl 3-(4-methoxyphenyl) glycidate and methyl 3-phenylglycidate
-
-
?
additional information
?
-
-
almost no activity on long-chained acyl esters such as 4-nitrophenyl palmitate
-
-
?
additional information
?
-
-
substrate specificity
-
?
additional information
?
-
-
preference toward esters of short- and middle-chain fatty acids
-
-
?
additional information
?
-
-
preference toward esters of short- and middle-chain fatty acids
-
-
?
additional information
?
-
-
substrate specificity
-
?
additional information
?
-
-
no activity with trielaidin, an olive oil emulsion containing 10% v/v olive oil and 1% m/v gum arabic is used as substrate, the enzyme shows a sn-1 selectivity using diacylglycerols, and R-isomer hydrolytic preference with pseudolipids representing triacylglycerols in which 2 of the ester bonds are replaced with ether and amide linkages
-
?
additional information
?
-
-
substrate is olive oil, the enzyme is 1,3-specific
-
?
additional information
?
-
-
the enzyme also shows transesterification activity with 4-nitrophenyl palmitate ester substrates, overview
-
-
?
additional information
?
-
-
no activity with trielaidin, an olive oil emulsion containing 10% v/v olive oil and 1% m/v gum arabic is used as substrate, the enzyme shows a sn-1 selectivity using diacylglycerols, and R-isomer hydrolytic preference with pseudolipids representing triacylglycerols in which 2 of the ester bonds are replaced with ether and amide linkages
-
?
additional information
?
-
-
substrate specificity, the enantioselective lipase hydrolyzes 4-nitrophenyl esters with acyl chain lengths between C4 and C12, and shows high enantioselectivity toward the R-isomer of ethyl 2-arylpropanoate, overview
-
-
?
additional information
?
-
-
substrate specificity, the enantioselective lipase hydrolyzes 4-nitrophenyl esters with acyl chain lengths between C4 and C12, and shows high enantioselectivity toward the R-isomer of ethyl 2-arylpropanoate, overview
-
-
?
additional information
?
-
-
an emulsion containing olive oil and gum arabic is used as substrate, enzyme shows a preference for short-chain triacylglycerides
-
?
additional information
?
-
-
an emulsion containing olive oil and gum arabic is used as substrate, enzyme shows a preference for short-chain triacylglycerides
-
?
additional information
?
-
-
fatty acid substrate specificity is broad with little preference for C12 and C4
-
?
additional information
?
-
-
LipA has a preference for 4-nitrophenyl esters with longer fatty acid chains
-
?
additional information
?
-
-
strain A30-1, active with triglycerides of C16:0 to C22:0fatty acids and on natural fats and oils
-
?
additional information
?
-
-
strain A30-1, active with triglycerides of C16:0 to C22:0fatty acids and on natural fats and oils
-
?
additional information
?
-
-
fatty acid substrate specificity is broad with little preference for C12 and C4
-
?
additional information
?
-
-
LipA has a preference for 4-nitrophenyl esters with longer fatty acid chains
-
?
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
?
-
-
substrate specificity of the extracellular enzyme, the enzyme shows low activity
-
-
?
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
?
-
the enzyme prefers substrates containing middle-size fatty acids
-
-
?
additional information
?
-
-
the enzyme prefers substrates containing middle-size fatty acids
-
-
?
additional information
?
-
-
the enzyme is involved in basal lipolysis of storage triacylglycerides, and hormonally as well as developmentally regulated, physiological functions, role in apoB-containing lipoprotein assembly in the endoplasmic reticulum, overview
-
-
?
additional information
?
-
diacylglycerol lipase may regulate protein kinase C activity and 2-arachidonoyl-sn-glycerol levels by rapidly altering the intracellular concentration of diacylglycerols
-
-
?
additional information
?
-
1,2-diacyl-sn-glycerols are the preferred substrates over 1,3-diacyl-sn-glycerols. The enzyme hydrolyzes stearate in preference to palmitate from the sn-1-position of 1,2-diacyl-sn-glycerols. 1-O-alkyl-2-acyl-sn-glycerols are not a substrate for the enzyme
-
-
?
additional information
?
-
-
the enzyme hydrolyzes triacylglycerols to fatty acids and glycerol, the fatty acids from the sn-1 or 3-positions are hydrolyzed first to yield 1,2(2,3)-diacylglycerols
-
-
?
additional information
?
-
-
substrate specificity of the extracellular enzyme
-
-
?
additional information
?
-
substrate specificity for saturated fatty acids from C6 to C12 and unsaturated long-chain fatty acids. Monoglycerides are hydrolyzed very slowly
-
-
?
additional information
?
-
-
substrate specificity for saturated fatty acids from C6 to C12 and unsaturated long-chain fatty acids. Monoglycerides are hydrolyzed very slowly
-
-
?
additional information
?
-
substrate specificity for saturated fatty acids from C6 to C12 and unsaturated long-chain fatty acids. Monoglycerides are hydrolyzed very slowly
-
-
?
additional information
?
-
Q05489
catalytic triad of the active center consists of the residues Ser87, Asp263 and His285. These residues are not exposed to the solvent, but a narrow channel connects them with the molecular surface
-
-
?
additional information
?
-
-
catalytic triad of the active center consists of the residues Ser87, Asp263 and His285. These residues are not exposed to the solvent, but a narrow channel connects them with the molecular surface
-
-
?
additional information
?
-
-
the enzyme also uses olive oil and safflower oil as substrates
-
-
?
additional information
?
-
-
the enzyme also uses olive oil and safflower oil as substrates
-
-
?
additional information
?
-
the enzyme preferentially performs transfer reactions such as alcoholysis in presence of suitable nucleophiles other than water, and catalyzes the hydrolysis of water insoluble medium-chain triacylglyceride substrates
-
?
additional information
?
-
-
the enzyme preferentially performs transfer reactions such as alcoholysis in presence of suitable nucleophiles other than water, and catalyzes the hydrolysis of water insoluble medium-chain triacylglyceride substrates
-
?
additional information
?
-
-
temperature-dependent substrate specificity of isozymes with (R,S)-profen 2,2,2-trifluoroethyl thioesters, overview
-
-
?
additional information
?
-
Cephaloleia presignis
-
olive oil is utilized as substrate with high activity, the enzyme hydrolyzes long-chain fatty acids rather than short-chain fatty acids of 4-nitrophenyl esters and methyl esters, and it hydrolyzes short-chain fatty acids rather than short-shain fatty acids of triglycerides
-
?
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
?
-
-
with p-nitrophenyl esters of different fatty acids as substrates enzyme activity is highest when the acyl chain is short e.g. C2
-
-
?
additional information
?
-
-
with p-nitrophenyl esters of different fatty acids as substrates enzyme activity is highest when the acyl chain is short e.g. C2
-
-
?
additional information
?
-
-
LipA is a non-specific lipase able to act at random for the complete breakdown of triacylglycerols
-
-
?
additional information
?
-
-
LipA is a non-specific lipase able to act at random for the complete breakdown of triacylglycerols
-
-
?
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
-
-
?
additional information
?
-
-
PLRP and pancreatic lipase differ in enzymatic properties such as substrate specificity, sensitivity to inhibition by bile salts and colipase dependence
-
-
?
additional information
?
-
-
enzyme also utilizes water-soluble substrates, enzyme does not possess protease activity and does not hydrolyze peptide bonds, no activity with N-benzoyl-L-tyrosine 4-nitroanilide
-
?
additional information
?
-
catalyzes the initial step in triglyceride hydrolysis
-
-
?
additional information
?
-
-
catalyzes the initial step in triglyceride hydrolysis
-
-
?
additional information
?
-
-
the lipase hydrolyzes triacylglycerol to produce 1,2-diacylglycerol (with yield of 50.2%) and 2-monoacylglycerol (with yield of 14.0%) as main products and free fatty acids
-
-
?
additional information
?
-
-
the lipase hydrolyzes triacylglycerol to produce 1,2-diacylglycerol (with yield of 50.2%) and 2-monoacylglycerol (with yield of 14.0%) as main products and free fatty acids
-
-
?
additional information
?
-
substrate specificity, overview
-
?
additional information
?
-
-
substrate specificity, overview
-
?
additional information
?
-
-
substrate is olive oil emulsion
-
?
additional information
?
-
-
the enzyme also possesses esterase activity
-
?
additional information
?
-
-
substrate is olive oil emulsion
-
?
additional information
?
-
-
the enzyme also possesses esterase activity
-
?
additional information
?
-
substrate specificity, overview
-
?
additional information
?
-
-
enzyme hydrolyzes triacylglycerides of plant oils such as olive oil, soybean oil, palm oil, and lard as carbon sources
-
?
additional information
?
-
-
substrate specificity, methyl eicosanoate and methyl decosanoate are poor substrates, overview
-
-
?
additional information
?
-
-
enzyme hydrolyzes triacylglycerides of plant oils such as olive oil, soybean oil, palm oil, and lard as carbon sources
-
?
additional information
?
-
-
substrate specificity, methyl eicosanoate and methyl decosanoate are poor substrates, overview
-
-
?
additional information
?
-
-
substrate specificity with natural oils and triacylglycerol substrates, overview, the enzyme catalyzes the hydrolysis of triacylglycerols into fatty acids and glycerol at the water-lipid interface and its reverse reaction in non-aqueous solvents
-
-
?
additional information
?
-
substrate specificity with natural oils and triacylglycerol substrates, overview, the enzyme catalyzes the hydrolysis of triacylglycerols into fatty acids and glycerol at the water-lipid interface and its reverse reaction in non-aqueous solvents
-
-
?
additional information
?
-
-
the enzyme catalyzes the hydrolysis of triacylglycerols into fatty acids and glycerol at the water-lipid interface and its reverse reaction in non-aqueous solvents
-
-
?
additional information
?
-
the enzyme catalyzes the hydrolysis of triacylglycerols into fatty acids and glycerol at the water-lipid interface and its reverse reaction in non-aqueous solvents
-
-
?
additional information
?
-
-
linolenic acid and behenic acid are not hydrolysed
-
-
?
additional information
?
-
-
linolenic acid and behenic acid are not hydrolysed
-
-
?
additional information
?
-
-
substrate specificity with natural oils and triacylglycerol substrates, overview, the enzyme catalyzes the hydrolysis of triacylglycerols into fatty acids and glycerol at the water-lipid interface and its reverse reaction in non-aqueous solvents
-
-
?
additional information
?
-
Geotrichum marinum
-
substrate specificity, the extracellular enzyme prefers triacylglyceride substrates with cis double bonds in the fatty acid side chains, activity increases with number of double bonds, no activity with tristearin
-
-
?
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
?
-
-
regulation of gene expression
-
-
?
additional information
?
-
-
measurement of in vivo enzyme activities by use of a liquid lipid containing test meal, determination of free fatty acids
-
?
additional information
?
-
-
the enzyme mobilizes stored triacylglycerols some of which is used for very-low-density lipoprotein assembly in the liver
-
?
additional information
?
-
-
the enzyme catalyzes the hydrolysis of triacylglycries into IDL and HDl, no co-linearitiy between insulin sensitivity and adiponectin as well as insulin sensitivity and enzyme activity, overview
-
-
?
additional information
?
-
-
the enzyme is involved in basal lipolysis of storage triacylglycerides, and hormonally as well as developmentally regulated, physiological functions, role in apoB-containing lipoprotein assembly in the endoplasmic reticulum, overview
-
-
?
additional information
?
-
-
the enzyme participates in VLDL assembly in endoplasmic reticulum without utilizing VLDL lipids as substrates
-
-
?
additional information
?
-
-
substrate specificity of recombinant wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
the inactive enzyme mutant S152G binds to tricaprylin in a water emulsion interface competiting with the active enzyme hydrolyzing the substrate, overview
-
-
?
additional information
?
-
-
the phospholipase A2 isozymes also show triacylglycerol lipase activity and acylglycerol transacylase activity
-
-
?
additional information
?
-
-
Val407 and Ile408 in the beta5'-loop are required for interaction of the enzyme with the colipase in presence of bile salt micelles, overview
-
-
?
additional information
?
-
-
the enzyme also shows phospholipase A1 activity, EC 3.1.1.32, galactolipase activity, EC 3.1.1.26, and acylglycerol lipase activity, EC 3.1.1.23, overview
-
-
?
additional information
?
-
-
adipose TG lipase, ATGL, and hormone sensitive lipase, HSL, regulate lipolysis in a serial manner, with ATGL cleaving the first fatty acid and HSL the second fatty acid of triacylglycerol, lipolysis control, detailed overview
-
-
?
additional information
?
-
-
ATGL selectively performs the first step in triacylglyceride hydrolysis resulting in the formation of diacylglyceride and free fatty acid. The specific activity against triacylglycerided is more than 10fold higher than against diacylglyceride, and the enzyme shows essentially no hydrolytic activity when other lipid substrates are used such as cholesteryl esters or retinyl esters. Molecular mechanisms that regulate ATGL activity, detailed overview
-
-
?
additional information
?
-
-
structure, function, and regulation of ATGL and HSL, overview
-
-
?
additional information
?
-
-
ATGL binds to the pigment epithelium derived factor
-
-
?
additional information
?
-
-
ATGLalso possesses phospholipase and transacylase activity
-
-
?
additional information
?
-
-
enzymatic activity chain fatty acid esters longer than C12 is below 10% of maximum activity
-
-
?
additional information
?
-
enzyme is active toward 4-nitrophenyl esters of various carbon chain lengths with peak activity on long-chain fatty acid (C14). It displays high sn-1,3-regioselectivity on hydrolyzing triolein
-
-
?
additional information
?
-
-
enzyme is active toward 4-nitrophenyl esters of various carbon chain lengths with peak activity on long-chain fatty acid (C14). It displays high sn-1,3-regioselectivity on hydrolyzing triolein
-
-
?
additional information
?
-
-
the enzyme exhibits efficient hydrolysis of oilive oil in the absence of colipase and bile salts
-
-
?
additional information
?
-
-
the enzyme hydrolyzes alpha-naphthyl esters of fatty acid with chain lengths from C4 to C18
-
?
additional information
?
-
-
the enzyme hydrolyzes alpha-naphthyl esters of fatty acid with chain lengths from C4 to C18
-
?
additional information
?
-
-
lipases A and B display no interfacial activation due to absence of the lid structure which regulates the access to the active site. The enzyme performs estrification of lactic acid and alcohols in hexane
-
?
additional information
?
-
-
CalA shows preference for short-chain triglycerides, low activity with hydrophilic esters
-
-
?
additional information
?
-
-
the enzyme performs a reversible monoglyceride isomerization, the rate of iso-propanolysis reactions is higher than propanolysis, mechanism of 1,3-specific alcoholysis, overview
-
-
?
additional information
?
-
-
The conversion of the lauric acid is at 80% after 4 h whereas the residual amount of polyglycerol is at 50% at this time. The conversion of polyglycerol remains lower than the conversion of lauric acid, because of the multiple hydroxy functions within the mixture of different glycerol oligomers. The equilibrium of the reaction can be shifted to total conversion by removal of water applying vacuum to the stirred tank reactor.
-
-
?
additional information
?
-
-
The synthesis of myristyl myristate by Sepabeads EC-EP/CALB is an example for a biocatalytic surfactant production.
-
-
?
additional information
?
-
-
lipase B can only convert straight chain fatty acids of different length with a preference toward C5 and C12
-
-
?
additional information
?
-
-
the enzyme catalyzes the alcoholysis of soybean oil with ethanol in propane medium
-
-
?
additional information
?
-
lipolysis is regulated by the opposing functions of the enzyme ATGL and adiponutrin, overview
-
-
?
additional information
?
-
-
lipolysis is regulated by the opposing functions of the enzyme ATGL and adiponutrin, overview
-
-
?
additional information
?
-
-
the enzyme is involved in basal lipolysis of storage triacylglycerides, and hormonally as well as developmentally regulated, the hormone-sensitive lipase is negatively regulated by perilipin in adipose tissue, physiological functions, role in apoB-containing lipoprotein assembly in the endoplasmic reticulum, overview
-
-
?
additional information
?
-
-
ATGL and diacylglycerol acyltransferase-1, DGAT-1, may be cooperatively involved in rosiglitazone-stimulated triglyceride hydrolysis and fatty acid re-esterification in 3T3-L1 adipocytes, overview
-
-
?
additional information
?
-
-
ATGL and hormone sensitive lipase, HSL, regulate lipolysis in a serial manner, with ATGL cleaving the first fatty acid and HSL the second fatty acid of triacylglycerol, lipolysis control, detailed overview
-
-
?
additional information
?
-
-
ATGL selectively performs the first step in triacylglyceride hydrolysis resulting in the formation of diacylglyceride and free fatty acid. The specific activity against triacylglycerides is more than 10fold higher than against diacylglyceride, and the enzyme shows essentially no hydrolytic activity when other lipid substrates are used such as cholesteryl esters or retinyl esters. Molecular mechanisms that regulate ATGL activity, detailed overview
-
-
?
additional information
?
-
-
HSL translocates from the cytoplasm to the lipid droplet surface and interacts with Peri A in stimulated lipolysis
-
-
?
additional information
?
-
-
structure, function, and regulation of ATGL and HSL, overview
-
-
?
additional information
?
-
-
ATGL binds to the pigment epithelium derived factor
-
-
?
additional information
?
-
-
ATGLalso possesses phospholipase and transacylase activity
-
-
?
additional information
?
-
-
the enzyme hydrolyzes long-chain fatty acid esters in vivo with a modest substrate preference for C16:1
-
-
?
additional information
?
-
-
the enzyme lacks the ability to hydrolyze diacylglycerols, monoacylglycerols, cholesteryl esters, or retinyl esters
-
-
?
additional information
?
-
-
the enzyme lacks the ability to hydrolyze monoacylglycerol, CEs, or retinyl esters
-
-
?
additional information
?
-
-
the enzyme hydrolyzes long-chain fatty acid esters in vivo with a modest substrate preference for C16:1
-
-
?
additional information
?
-
-
the enzyme prefers triglycerides with C16-fatty acyl chains and C18-fatty acyl chains, it cleaves only the primary groups of triglycerides, marked preference for substrates containing endogenously occuring fatty acids
-
-
?
additional information
?
-
-
the enzyme is involved in the hydrolysis of both acylglycerols and cholesterol esters in lysosomes
-
-
?
additional information
?
-
-
enzyme also provides phospholipase A2 activity, it preferentially hydrolyzes the sn-2-position of the substrate
-
?
additional information
?
-
-
no activity with 4-nitrophenyl acetate
-
-
?
additional information
?
-
Penicillium candidum
-
substrate specificity
-
?
additional information
?
-
-
highly active against all triacylglycerols and very low activity against partial acylglycerols or monoesters
-
-
?
additional information
?
-
-
highly specific for short-chain fatty acids esters
-
?
additional information
?
-
-
highly specific for short-chain fatty acids esters
-
?
additional information
?
-
the recombinant enzyme displays high activity on short to medium chain length substrates, and poor activity on C18 substrates, overview, poor activity with 4-nitrophenyl palmitate, 4-nitrophenyl stearate, and 4-methylumbelliferyl oleate
-
-
?
additional information
?
-
-
the recombinant enzyme displays high activity on short to medium chain length substrates, and poor activity on C18 substrates, overview, poor activity with 4-nitrophenyl palmitate, 4-nitrophenyl stearate, and 4-methylumbelliferyl oleate
-
-
?
additional information
?
-
the recombinant enzyme displays high activity on short to medium chain length substrates, and poor activity on C18 substrates, overview, poor activity with 4-nitrophenyl palmitate, 4-nitrophenyl stearate, and 4-methylumbelliferyl oleate
-
-
?
additional information
?
-
-
the extracellular enzyme inhibits the chemotaxis and chemiluminescence of monocytes, but has little effect on neutrophils, in human peripheral blood contributing to pathogenesis, overview
-
-
?
additional information
?
-
-
substrate specificity of the extracellular enzyme, the enzyme shows high activity
-
-
?
additional information
?
-
-
the enzyme also shows 8fold lower esterase activity with 4-nitrophenyl acetate and Tween 80 as substrates
-
-
?
additional information
?
-
-
the enzyme is unspecific, but prefers substrates with shorter side chains, exo-enzyme
-
-
?
additional information
?
-
-
the extracellular enzyme form is an exo-enzyme
-
-
?
additional information
?
-
double-lid structure movements are involved in the enzyme function, Phe214 and Ala217 play important roles in lid movement, lid closure is driven by hydrophobic interactions, overview
-
-
?
additional information
?
-
-
double-lid structure movements are involved in the enzyme function, Phe214 and Ala217 play important roles in lid movement, lid closure is driven by hydrophobic interactions, overview
-
-
?
additional information
?
-
-
lipases catalyze the hydrolysis of neutral lipids in biological systems performing three reactions: hydrolysis of ester in aqueous solutions, esterification in organic solvents, and transesterification between ester and acyl group donor with a wide substrate specificiy, e.g. lipids, sugars, alcohols, acids, and esters
-
-
?
additional information
?
-
-
the enzyme is unspecific, but prefers substrates with shorter side chains, exo-enzyme
-
-
?
additional information
?
-
-
the enzyme also shows 8fold lower esterase activity with 4-nitrophenyl acetate and Tween 80 as substrates
-
-
?
additional information
?
-
-
lipases catalyze the hydrolysis of neutral lipids in biological systems performing three reactions: hydrolysis of ester in aqueous solutions, esterification in organic solvents, and transesterification between ester and acyl group donor with a wide substrate specificiy, e.g. lipids, sugars, alcohols, acids, and esters
-
-
?
additional information
?
-
-
the extracellular enzyme inhibits the chemotaxis and chemiluminescence of monocytes, but has little effect on neutrophils, in human peripheral blood contributing to pathogenesis, overview
-
-
?
additional information
?
-
-
the extracellular enzyme form is an exo-enzyme
-
-
?
additional information
?
-
-
substrate specificity of the extracellular enzyme
-
-
?
additional information
?
-
-
substrate specificity overview, enzyme splits polyunsaturated fatty acid ester bonds, the enzyme preferably acts on short- to middle-chain length fatty acid simple methyl esters and triglycerides
-
?
additional information
?
-
-
the enzyme is responsible for the spoilage of milk
-
-
?
additional information
?
-
-
substrate specificity of the recombinant extracellular enzyme overexpressed in Escherichia coli
-
-
?
additional information
?
-
LipB68 performs the enantioselective acylation of racemic alcohols, e.g. toluene, and effectively catalyzes the transesterification of both alpha-phenylethanol and alpha-phenylpropanol at 20°C with high enantioselectivity, overview
-
-
?
additional information
?
-
-
LipB68 performs the enantioselective acylation of racemic alcohols, e.g. toluene, and effectively catalyzes the transesterification of both alpha-phenylethanol and alpha-phenylpropanol at 20°C with high enantioselectivity, overview
-
-
?
additional information
?
-
LipB68 performs the enantioselective acylation of racemic alcohols, e.g. toluene, and effectively catalyzes the transesterification of both alpha-phenylethanol and alpha-phenylpropanol at 20°C with high enantioselectivity, overview
-
-
?
additional information
?
-
-
substrate specificity of the recombinant extracellular enzyme overexpressed in Escherichia coli
-
-
?
additional information
?
-
-
substrate specificity overview, enzyme splits polyunsaturated fatty acid ester bonds, the enzyme preferably acts on short- to middle-chain length fatty acid simple methyl esters and triglycerides
-
?
additional information
?
-
-
the enzyme is responsible for the spoilage of milk
-
-
?
additional information
?
-
Q9EV86
substrate specificity, the enzyme prefers triacylglycerides with short fatty acid chains
-
-
?
additional information
?
-
-
substrate specificity, the enzyme prefers triacylglycerides with short fatty acid chains
-
-
?
additional information
?
-
Q9EV86
substrate specificity, the enzyme prefers triacylglycerides with short fatty acid chains
-
-
?
additional information
?
-
-
enzyme shows a preference for long-chain fatty acid triacylglyceride substrates and natural oils like olive oil, soybean oil, mustard oil, coconut oil, and best almond oil, substrate specificty overview
-
?
additional information
?
-
-
Pseudomonas mendocina PK-12CS is able to grow on olive oil, soybean oil, tributyrin and triolein as sole carbon and energysource
-
?
additional information
?
-
-
the enzyme also uses olive oil (100% activity), mustard oil (96% activity), soybean oil (88.8% activity), palm oil (73% activity), and groundnut oil (92% activity) as substrates
-
-
?
additional information
?
-
-
the lipase possesses 1,3-positional specificity
-
-
?
additional information
?
-
-
the enzyme also uses olive oil (100% activity), mustard oil (96% activity), soybean oil (88.8% activity), palm oil (73% activity), and groundnut oil (92% activity) as substrates
-
-
?
additional information
?
-
-
the lipase possesses 1,3-positional specificity
-
-
?
additional information
?
-
-
enzyme shows a preference for long-chain fatty acid triacylglyceride substrates and natural oils like olive oil, soybean oil, mustard oil, coconut oil, and best almond oil, substrate specificty overview
-
?
additional information
?
-
-
Pseudomonas mendocina PK-12CS is able to grow on olive oil, soybean oil, tributyrin and triolein as sole carbon and energysource
-
?
additional information
?
-
-
enantioselective transesterification of 2-phenoxy-1-propanol
-
?
additional information
?
-
enzyme shows a preference for long-chain fatty acid triacylglyceride substrates
-
?
additional information
?
-
olive oil is utilized as substrate with high activity
-
?
additional information
?
-
-
olive oil is utilized as substrate with high activity
-
?
additional information
?
-
-
enantioselective transesterification of 2-phenoxy-1-propanol
-
?
additional information
?
-
olive oil is utilized as substrate with high activity
-
?
additional information
?
-
enzyme shows a preference for long-chain fatty acid triacylglyceride substrates
-
?
additional information
?
-
substrate specificity, LipA1 shows a preference for trimyristin and 4-nitrophenyl myristate, overview
-
-
?
additional information
?
-
-
substrate specificity of the recombinant and the wild-type enzyme, preference for triacylglycerides with short length fatty acids
-
-
?
additional information
?
-
-
substrate specificity of the recombinant and the wild-type enzyme, preference for triacylglycerides with short length fatty acids
-
-
?
additional information
?
-
-
the enzyme is involved in basal lipolysis of storage triacylglycerides, and hormonally as well as developmentally regulated, physiological functions, role in apoB-containing lipoprotein assembly in the endoplasmic reticulum, overview
-
-
?
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
-
-
?
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
?
-
substrate specificity, regioselectivity, and stereoselectivity of ROL29 and ROL32, the N-terminal peptide of the enzymes plays a role, overview, interaction of ROL29 and ROL32 with egg-yolk phosphocholine layer and penetration velocity
-
-
?
additional information
?
-
ROLw is unable to hydrolyse triacylglycerols in the presence of high concentration of bile salts, it is a serine enzyme
-
-
?
additional information
?
-
ROLw is unable to hydrolyse triacylglycerols in the presence of high concentration of bile salts, it is a serine 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
?
-
-
specific for the primary position of the glycerides. Triglycerides with C18 are hydrolyzed in this order: C18:3, C18:2, C18:1, C18:0
-
-
?
additional information
?
-
the enzyme is involved in regulation of lipolysis
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of lipolysis
-
-
?
additional information
?
-
substrate specificity, no activity with oleoyl-CoA and 1,2-dioleoyl-3-phosphatidylcholine
-
-
?
additional information
?
-
-
substrate specificity, no activity with oleoyl-CoA and 1,2-dioleoyl-3-phosphatidylcholine
-
-
?
additional information
?
-
-
enzyme shows broad substrate specificity, exhibiting carboxylesterase activity towards short-chain acyl esters and lipase activity toward long-chain acyl esters including triacylglycerols regardless of saturated and unsaturated fatty acids
-
-
?
additional information
?
-
-
enzyme shows broad substrate specificity, exhibiting carboxylesterase activity towards short-chain acyl esters and lipase activity toward long-chain acyl esters including triacylglycerols regardless of saturated and unsaturated fatty acids
-
-
?
additional information
?
-
-
substrate specificity of isozymes, overview
-
-
?
additional information
?
-
-
the enzyme is required for mobilization of triacylglycerides stored in lipid particles, overview
-
-
?
additional information
?
-
-
substrate specificity of isozymes, overview
-
-
?
additional information
?
-
-
the enzyme is required for mobilization of triacylglycerides stored in lipid particles, overview
-
-
?
additional information
?
-
-
the enzyme is more active on short-chain triacylglycerols than on long-chain ones
-
-
?
additional information
?
-
-
substrate specificity, lipase penetration into the egg-phosphocholine monolayer, overview
-
-
?
additional information
?
-
substrate specificity, no or poor activity with tributyrin, triacetin, tripropionin, tristearin, 4-nitrophenyl stearate, and 4-nitrophenyl acetate, the lipase shows preferential substrate specificity toward the medium-chain-length fatty acids, overview
-
-
?
additional information
?
-
-
substrate specificity, no or poor activity with tributyrin, triacetin, tripropionin, tristearin, 4-nitrophenyl stearate, and 4-nitrophenyl acetate, the lipase shows preferential substrate specificity toward the medium-chain-length fatty acids, overview
-
-
?
additional information
?
-
-
does not hydolyze propylene carbonate
-
-
?
additional information
?
-
-
does not hydolyze propylene carbonate
-
-
?
additional information
?
-
substrate specificity, no or poor activity with tributyrin, triacetin, tripropionin, tristearin, 4-nitrophenyl stearate, and 4-nitrophenyl acetate, the lipase shows preferential substrate specificity toward the medium-chain-length fatty acids, overview
-
-
?
additional information
?
-
-
substrate specificity, no or poor activity with tributyrin, triacetin, tripropionin, tristearin, 4-nitrophenyl stearate, and 4-nitrophenyl acetate, the lipase shows preferential substrate specificity toward the medium-chain-length fatty acids, overview
-
-
?
additional information
?
-
-
the enzyme probably is involved in fat mobilization during seed germination
-
-
?
additional information
?
-
-
substrate specificity, the enzyme catalyzes hydrolysis of triacylglycerides with long fatty acid chains, low activity with tripalmitin and tristearin, no activity with tributyrin and triacetate, phosphatidylcholine and monogalactosyldiacylglycerol are poor substrates
-
-
?
additional information
?
-
Ssp is not responsible for binding to collagen type I by the cell
-
-
?
additional information
?
-
-
Ssp is not responsible for binding to collagen type I by the cell
-
-
?
additional information
?
-
enzyme hydrolyzes triacylglycerols without chain length specificity
-
?
additional information
?
-
-
enzyme hydrolyzes triacylglycerols without chain length specificity
-
?
additional information
?
-
-
substrate specificity, the enzyme strongly prefers short-chain substrates, the enzyme SWL2 also shows phospholipase activity
-
?
additional information
?
-
-
substrate specificity, the enzyme strongly prefers short-chain substrates, the enzyme SWL2 also shows phospholipase activity
-
?
additional information
?
-
-
residue Asp290 is important for the chain length specificity and catalytic efficiency of the enzyme
-
-
?
additional information
?
-
-
the enyzyme also uses olive oil as substrate
-
-
?
additional information
?
-
isozyme SCO1725 shows no activity on tricaprin, tricaproin, and olive oil, 4-nitrophenyl stearate is hardly hydrolysed, 4-nitrophenyl stearate is no substrate for isozyme SCO1725
-
-
?
additional information
?
-
isozyme SCO1725 shows no activity on tricaprin, tricaproin, and olive oil, 4-nitrophenyl stearate is hardly hydrolysed, 4-nitrophenyl stearate is no substrate for isozyme SCO1725
-
-
?
additional information
?
-
isozyme SCO1725 shows no activity on tricaprin, tricaproin, and olive oil, 4-nitrophenyl stearate is hardly hydrolysed, 4-nitrophenyl stearate is no substrate for isozyme SCO1725
-
-
?
additional information
?
-
isozyme SCO1725 shows no activity on tricaprin, tricaproin, and olive oil, 4-nitrophenyl stearate is hardly hydrolysed, 4-nitrophenyl stearate is no substrate for isozyme SCO1725
-
-
?
additional information
?
-
-
enzyme also performs transesterification reactions, regio- and enantioselctivity, overview, substrate specificity: enzyme hydrolyzes most efficiently medium chain length fatty acid glycerol esters, C8-C12, and shows a preference for esters of C16 and C18 unsaturated fatty acids over C16 and C18 saturated fatty acid esters, as well as for triacylglycerol substrates with cis double bond, e.g. triolein, versus trans double bonds, e.g. trielaidin, enzyme also utilizes different natural plant oils as substrates, overview
-
?
additional information
?
-
-
the pancreatic enzyme shows a wide substrate spectrum but prefers triacylglyceride substrates with short fatty acid chains
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
methyl esters are cleaved by lipase 5 times faster than ethyl esters. The relative hydrolysis rates are rather low for esters of C3 and C4 alcohols, they increase abruptly for esters of n-hexyl alcohol, which are cleaved faster than methyl esters
-
-
?
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
?
-
-
the enzyme is involved in basal lipolysis of storage triacylglycerides, and hormonally as well as developmentally regulated, physiological functions, role in apoB-containing lipoprotein assembly in the endoplasmic reticulum, overview
-
-
?
additional information
?
-
-
pancreatic lipase-catalyzed esterification of n-butanoic acid in solvent-free system and in isooctane carried out with three alcohols: n-pentanol, n-heptanol and geraniol, 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
-
-
?
additional information
?
-
Talaromyces thermophilus lipase (TTL) also hydrolyzes monogalactosyl diacylglycerol (MGDG) and digalactosyl diacylglycerol (DGDG) substrates (EC 3.1.1.26) presented in various forms to the enzyme. The enzyme has galactolipase activity on galactolipid micelles, monomolecular films, and UV-absorbing surface-coated substrate, overview. TTL possesses broad substrate specificity and is active on triglycerides with various acyl chain lengths, phospholipids, and galactolipids
-
-
?
additional information
?
-
-
Talaromyces thermophilus lipase (TTL) also hydrolyzes monogalactosyl diacylglycerol (MGDG) and digalactosyl diacylglycerol (DGDG) substrates (EC 3.1.1.26) presented in various forms to the enzyme. The enzyme has galactolipase activity on galactolipid micelles, monomolecular films, and UV-absorbing surface-coated substrate, overview. TTL possesses broad substrate specificity and is active on triglycerides with various acyl chain lengths, phospholipids, and galactolipids
-
-
?
additional information
?
-
Talaromyces thermophilus lipase (TTL) also hydrolyzes monogalactosyl diacylglycerol (MGDG) and digalactosyl diacylglycerol (DGDG) substrates (EC 3.1.1.26) presented in various forms to the enzyme. The enzyme has galactolipase activity on galactolipid micelles, monomolecular films, and UV-absorbing surface-coated substrate, overview. TTL possesses broad substrate specificity and is active on triglycerides with various acyl chain lengths, phospholipids, and galactolipids
-
-
?
additional information
?
-
-
1,3-positional specific lipase
-
-
?
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
?
-
-
1,3-positional specific lipase
-
-
?
additional information
?
-
-
LipA and LipB exhibit high activity with long-chain fatty acid glycerides, yielding maximum activity with trioleate and, among the 4-nitrophenyl esters, with 4-nitrophenyl laurate, hydrolysis of glycerol ester bonds occurs at positions 1 and 3, tributyrin and tricaproin are poor substrates, overview
-
-
?
additional information
?
-
the enzyme is a hemolytic factor and involved in pathogenicity and as alternative source of iron from erythrocytes
-
-
?
additional information
?
-
-
the enzyme is a hemolytic factor and involved in pathogenicity and as alternative source of iron from erythrocytes
-
-
?
additional information
?
-
-
the enzyme reveals mid- to long- chain specificity for 4-nitrophenyl esters and triacylglycerols, with highest specificity on C-12 followed by C-14, C-16, and C-18. The enzyme shows (S)-selectivity in 1,4-dioxane and 2-propanol and (R)-selectivity in hexane during chiral separation of (+/-)1-phenylethanol by esterification
-
-
?
additional information
?
-
-
the enzyme reveals mid- to long- chain specificity for 4-nitrophenyl esters and triacylglycerols, with highest specificity on C-12 followed by C-14, C-16, and C-18. The enzyme shows (S)-selectivity in 1,4-dioxane and 2-propanol and (R)-selectivity in hexane during chiral separation of (+/-)1-phenylethanol by esterification
-
-
?
additional information
?
-
the lipase hydrolyses 4-nitrophenyl esters of fatty acids with chain lengths up to C14
-
-
?
additional information
?
-
no activity with 4-nitrophenyl butyrate and 4-nitrophenyl propionate
-
-
?
additional information
?
-
-
substrate specificity, the enzyme shows preference for triacylglyceride substrates with long fatty acid chains
-
-
?
additional information
?
-
-
substrate specificity, the enzyme shows preference for triacylglyceride substrates with long fatty acid chains
-
-
?
additional information
?
-
substrate specificity of LipY8p, overview
-
-
?
additional information
?
-
substrate specificity of LipY8p, overview
-
-
?
additional information
?
-
-
substrate specificity of LipY8p, overview
-
-
?
additional information
?
-
the lipase showed a preference for long chain fatty acid methyl esters of C12-C16, substrate specificity, overview
-
-
?
additional information
?
-
-
the lipase showed high activity toward long-chain fatty acid methyl esters with C12C16, overview
-
-
?
additional information
?
-
-
no phospholipid-hydrolyzing activity is detected with Lip9
-
-
?
additional information
?
-
substrate specificity of LipY8p, overview
-
-
?
additional information
?
-
substrate specificity of LipY8p, overview
-
-
?
additional information
?
-
-
substrate specificity of LipY8p, overview
-
-
?
additional information
?
-
-
no phospholipid-hydrolyzing activity is detected with Lip9
-
-
?
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1,6-di[O-(carbamoyl)cyclohexaneoxim]hexane
-
i.e. RG 80267
1-(2-chlorophenyl)-3-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]urea
-
-
1-(4-chlorophenyl)-1-methyl-3-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]urea
-
-
1-(4-chlorophenyl)-3-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]urea
-
-
1-(4-methoxyphenyl)-3-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]urea
-
-
1-(diphenylmethyl)-3-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]urea
-
-
1-benzyl-3-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]urea
-
-
1-ethyl-3-(3-dimethylaminopropyl) carbodiimide
1-hexandecanesulfonyl chloride
complete inhibition at 10 mM
1-methyl-1-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]-3-phenylurea
-
-
1-methyl-3-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]-1-phenylurea
-
-
1-phenyl-3-[5-(piperidin-1-ylsulfonyl)furan-3-yl]urea
-
-
1-propanol
-
about 99% inhibition at 1% (v/v)
1-[1,2-dimethyl-5-(piperidin-1-ylsulfonyl)-1H-pyrrol-3-yl]-3-phenylurea
-
-
1-[1-methyl-3-(piperidin-1-ylsulfonyl)-1H-pyrazol-5-yl]-3-phenylurea
-
-
1-[2,4-dimethyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]-3-phenylurea
-
-
1-[2-methyl-4-(morpholin-4-ylsulfonyl)phenyl]-3-phenylurea
-
-
1-[2-methyl-5-(morpholin-4-ylsulfonyl)furan-3-yl]-3-phenylurea
-
-
1-[2-methyl-5-(piperidin-1-ylsulfonyl)-1H-pyrrol-3-yl]-3-phenylurea
-
-
1-[2-methyl-5-(piperidin-1-ylsulfonyl)furan-3-yl]-3-[(1S)-1-phenylethyl]urea
-
-
1-[2-methyl-5-[(4-methylpiperazin-1-yl)sulfonyl]furan-3-yl]-3-phenylurea
-
-
1-[2-methyl-6-(piperidin-1-ylsulfonyl)pyridin-3-yl]-3-phenylurea
-
-
2,4,6-Trinitrobenzenesulfonic acid
-
55% residual activity at 2 mM
2-methyl-N-phenyl-5-(piperidin-1-ylsulfonyl)furan-3-carboxamide
-
-
3,4-dichloroisocoumarin
-
weak inhibition
3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate
Geotrichum marinum
-
i.e. CHAPS, 33% inhibition at 1 mM
4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride
4-Dimethylaminobenzaldehyde
-
-
4-hydroxymercuribenzoate
-
competitive inhibition of LIII, 60% inhibition at 5 mM
5-methyl-N-phenyl-4-[(phenylcarbamoyl)amino]furan-2-sulfonamide
-
-
alginate
-
alginate inhibits pancreatic lipase by a maximum of 72.2% with synthetic substrate and 58% with natural substrate. High-guluronic acid alginates from Laminaria hyperborea seaweed inhibit pancreatic lipase to a significantly higher degree than high-mannuronic acid alginates from Lessonia nigrescens
Alkaline phosphatase
-
-
-
BaCl2
-
30% inhibition at 1 mM
benzaldehyde
-
greatly inhibits the enzyme activity
benzalkonium chloride
-
little inhibitory effect
benzoic acid
-
greatly inhibits the enzyme activity
benzyl alcohol
-
complete inhibition at 1% (v/v)
beta-mercaptoethanol
-
about 75% inhibition at 1 mM, about 99% inhibition at 5 mM
bis-p-nitrophenyl methylphosphonate
-
complete and irreversible inhibition
boronic acid
-
alkane boronic acid and arene boronic acid, competitive
bovine serum albumin
amphipathic protein, the inhibition is fully reversible by addition of bile salts and colipase
-
Brij
slight inhibition of wild-type enzyme, and slight activation of the mutant N-fused enzyme at 1 mM
-
Brij 35
-
little inhibitory effect
butanol
-
70%, 30°C, complete immediate inactivation
C11Y4 phosphonate
in the absence of surfactant, the rate of cutinase inhibition is very low. The addition of beta-octylglucoside is required to trigger the inhibition of cutinase, which is completely inactivated after 60 min
CaCl2
-
21% inhibition at 1 mM
capric acid
-
89.7% residual activity at 1 mM
cetyl trimethylammonium bromide
-
-
cetyltriethylammonium bromide
Geotrichum marinum
-
complete inhibition at 1 mM
cetyltrimethylammonium bromide
chloroform
-
inhibitory at 3% (v/v)
cholate
-
1% w/v, 20% decrease in activity
Colipase
-
at high concentrations relative to lipase
-
CuSO4
-
31% inhibition at 1 mM
diethyl 4-nitrophenyl phosphate
Diethyl p-nitrophenyl phosphate
Digitonin
-
inhibitory at 0.5 mM
diisopropyl fluorophosphate
diisopropylfluorophosphate
-
82% residual activity after 30 min at 8 mM
dimethylformamide
-
57% inhibition of recombinant refolded enzyme at 30% v/v, 28% activation of recombinant refolded enzyme at 10% v/v
DMSO
-
BTID-A, 54% inhibition at 1% w/v
dodecanesulfonyl chloride
-
dodecyltrimethylammonium chloride
-
-
E-600
nearly complete inhibition of recombinant LipY at 0.0005 mM
endoprotease Glu-C
-
proteolytic cleavage only of the heat-denatured enzyme, not of the native enzyme
-
ethyl acetate
-
inhibitory at 8% (v/v)
eugenol
-
substrate inhibition
formaldehyde
-
complete inhibition at 10% (v/v)
hydrogen peroxide
-
62% residual activity after 5 h at 25% (v/v)
ionic detergents
Penicillium candidum
-
-
-
iso-amyl alcohol
-
about 80% inhibition at 1% (v/v)
iso-butanol
-
about 95% inhibition at 1% (v/v)
isopropyl fluorophosphate
-
-
KCN
-
62% inhibition at 1 mM
lysophosphatidylcholine
-
increases Km and reduces Vmax of the enzyme with triaclyglyrol substrates, not with monoacylglycerols, the activity is completely restored by addition of taurodeoxycholine or phospholipid
methylbenzethonium bromide
Geotrichum marinum
-
98% inhibition at 1 mM
N,N,5-trimethyl-4-[(phenylcarbamoyl)amino]furan-2-sulfonamide
-
-
N-(2-methoxyethyl)-N,5-dimethyl-4-[(phenylcarbamoyl)amino]furan-2-sulfonamide
-
-
n-dodecyltrimethylammonium bromide
-
-
N-ethyl-5-phenylisoxazolium-3'-sulfonate
-
-
N-lauroyl sarcosine
-
strong inhibition
Na-molybdate
-
inhibits slightly at 1 mM
oleic acid
-
inhibits enzyme production, product inhibition
p-bromophenacyl bromide
-
-
p-chloromercuribenzoate
-
5 mM, 30 min, 70°C, pH 8.5, 70% inhibition
p-chloromercuric benzoate
-
20% residual activity after 30 min at 8 mM
p-chloromercuriphenyl sulfonic acid
-
-
papain
-
proteolytic cleavage only of the heat-denatured enzyme, not of the native enzyme
-
Pectin
-
pectin freshly isolated from citrus segment membranes is a strong inhibitor of lipase activity, commercial citrus pectin shows a weak inhibitory effect (activity is reduced by 20%)
Pg250de
-
78% residual activity at 1% (v/v)
-
Pg400de
-
96% residual activity at 1% (v/v)
-
phenylmethanesulfonyl fluoride
-
67.2% residual activity at 5 mM
phenylmethanosulfonyl fluorate
-
-
phenylmethylsulfonyl fluoride
phytic acid
strong inhibition
poly-alpha-olefin
-
10 mM, 81% inhibition
-
Polyethylene glycol
-
little inhibitory effect
polyoxyethylene oleyl ether
-
-
-
protamine
-
50% inhibition at 2 mg/ml
Rc-(Rp,Sp)-1,2-dioctylcarbamoyl-glycero-3-O-(4-nitrophenyl) octylphosphonate
binding site structure, binding arrests the enzyme in the open conformation
sodium dioctyl sulfosuccinate
Geotrichum marinum
-
47% inhibition at 1 mM
Sodium dodecyl sulfate
-
-
sodium hypochlorite
-
85% residual activity after 5 h at 25% (v/v)
sodium lauryl sulfate
-
-
Span 40
-
little inhibitory effect
-
Sr2+
-
about 45% inhibition at 5 mM
sulfonylfuran urea
-
potent and non-selective inhibitor of endothelial lipase
-
tannin
-
70% reduction in activity at 10%
-
tetradecyl trimethylammonium bromide
-
inactive in the presence of micellar concentrations of tetradecyl trimethylammonium bromide
tetrahydrolipstatine
-
40% residual activity in the absence of sodium deoxycholate, complete inhibition in the presence of 4 mM sodium deoxycholate
thrombin
-
proteolytic cleavage only of the heat-denatured enzyme, not of the native enzyme
-
trinitrobenzene sulfonic acid
-
-
Triton B-1956
-
about 55% inhibition at 1% (w/v) Triton B-1956
-
Trypsin
-
proteolytic cleavage only of the heat-denatured enzyme, not of the native enzyme
-
Tween 60
-
10% residual activity at 0.001% (v/v)
Tween 85
-
about 85% inhibition at 1% (w/v) Tween 85
-
1,10-phenanthroline
-
inhibition at 10-30 mM
1-butanol
-
complete inhibition at 1% (v/v)
1-butanol
-
47% inhibition of recombinant refolded enzyme at 10% v/v
1-ethyl-3-(3-dimethylaminopropyl) carbodiimide
-
complete inhibition at 5 mM
1-ethyl-3-(3-dimethylaminopropyl) carbodiimide
-
complete inhibition at 50 mM
2-mercaptoethanol
-
-
2-mercaptoethanol
slight inhibition
2-mercaptoethanol
-
BTID-A, 26% inhibition at 1% w/v
2-mercaptoethanol
-
10 mM, 7.7% inhibition
2-mercaptoethanol
-
strong inhibition
2-mercaptoethanol
43% residual activity at 10 mM, with 4-nitrophenyl caproate as substrate, at 25°C
2-mercaptoethanol
-
reduces the enzyme activity to 48% after 1 h
2-mercaptoethanol
-
maximal inhibition of 32% at 1 mM of recombinant refolded enzyme
2-propanol
-
about 95% inhibition at 1% (v/v)
4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride
-
the presence of detergents, e.g. SDS, CTAB, Triton X-100, or Triton X-45, permitts the inhibition of lipase by irreversible covalent inhibitors, e.g. 4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride, AEBSF, while the enzyme, in the absence of detergent, is not inhibited by these irreversible inhibitors
4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride
-
the presence of detergents, e.g. SDS, CTAB, Triton X-100, or Triton X-45, permits the inhibition of lipase by irreversible covalent inhibitors, e.g. 4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride, AEBSF, while the enzyme, in the absence of detergent, is not inhibited by these irreversible inhibitors
4-chloromercuribenzoate
-
4-chloromercuribenzoate
-
5 mM, 51% residual activity
acetone
-
inhibitory effect of organic solvents, overview
acetone
-
54% relative activity at 10% (v/v) acetone
acetone
-
about 98% inhibition at 1% (v/v)
acetone
-
45% inhibition of recombinant refolded enzyme at 30% v/v
acetone
-
98.3% inhibition at 50% (v/v)
acetonitrile
-
inhibitory at 5% (v/v)
acetonitrile
-
about 99% inhibition at 1% (v/v)
acetonitrile
-
60% inhibition of recombinant refolded enzyme at 30% v/v
Ag+
-
56% residual activity at 1 mM
Ag+
-
80% residual activity at 5 mM
Ag+
Cephaloleia presignis
-
complete inhibition, 1 mM
Ag+
-
about 85% inhibition at 1 mM
Ag+
-
7.57% relative activity at 1 mM
Ag+
48% inhibition at 1 mM
Ag+
isoyzme SCO1725 shows 11% residual activity in the presence of 1 mM Ag+; isozyme SCO7513 shows 10% residual activity in the presence of 1 mM Ag+
Al3+
-
SSL shows 67% residual activity in the presence of 10 mM Al3+
Ba2+
-
69% residual activity at 1 mM
Ba2+
-
74.3% residual activity at 5 mM
Ba2+
-
77.22% residual activity at 5 mM
Ba2+
-
28% inhibition at 1 mM
Ba2+
-
62.5% residual activity at 1 mM
Ca2+
-
-
Ca2+
-
73% residual activity at 5 mM
Ca2+
-
72.04% residual activity at 5 mM
Ca2+
-
BTID-A, slight inhibition
Ca2+
-
50% inhibition at 1 mM
Ca2+
-
isozyme Lip-1 shows 84% relative activity in the presence of 1 mM Ca2+; isozyme Lip-2 shows 75% relative activity in the presence of 1 mM Ca2+
Ca2+
52% residual activity at 10 mM, with 4-nitrophenyl caproate as substrate, at 25°C
Ca2+
-
50% inhibition at 2.5 mM
Ca2+
-
50% inhibition at 5 mM
Ca2+
-
14% activation of recombinant refolded enzyme at 0.1 mM, 17% inhibition at 10 mM
Ca2+
-
SSL and SML show 80% and 60% residual activity, respectively, in the presence of 10 mM Ca2+
Ca2+
-
95.0% residual activity at 10 mM
Ca2+
isoyzme SCO1725 shows 91% residual activity at 10 mM Ca2+; isozyme SCO7513 shows 86% residual activity in the presence of 1 mM Ca2+
Ca2+
-
the enzyme activity is not affected by Ca2+ at 1-10 mM, 15% inhibition at 25 mM at pH 9.4-9.6
Ca2+
-
90% residual activity at 1 mM
Ca2+
49% residual activity at 1 mM
Cd2+
50% inhibition
Cd2+
-
isozyme Lip-1 shows 38% relative activity in the presence of 5 mM Cd2+; isozyme Lip-2 shows 28% relative activity in the presence of 5 mM Cd2+
Cd2+
-
about 70% inhibition at 2 mM
Cd2+
-
strain KKA-5, slight inhibition
Cd2+
-
49.1% residual activity at 1 mM
cetyltrimethylammonium bromide
-
-
cetyltrimethylammonium bromide
-
45% residual activity after 5 h at 25% (v/v)
CHAPS
complete inhibition of both wild-type and mutant N-fused enzymes at 1 mM
CHAPS
-
inhibitory at 0.5 mM
CHAPS
-
86% residual activity after 5 h at 25% (v/v)
cholic acid
-
-
cholic acid
-
90% residual activity at 0.5% (w/v)
chymotrypsin
-
proteolytic cleavage only of the heat-denatured enzyme, not of the native enzyme
-
chymotrypsin
partial proteolytic digestion of the recombinant enzyme
-
Co2+
-
68% residual activity at 5 mM
Co2+
-
38.83% residual activity at 5 mM
Co2+
-
82.7% inhibition at 50 mM
Co2+
-
74% relative activity at 5 mM
Co2+
-
about 75% inhibition at 5 mM
Co2+
-
5 mM, 30 min, 70°C, pH 8.5, 65% inhibition
Co2+
-
88% residual activity at 2 mM
Co2+
36% residual activity at 10 mM, with 4-nitrophenyl caproate as substrate, at 25°C
Co2+
-
1 mM, 13% inhibition
Co2+
-
46.0% residual activity at 10 mM
Co2+
isoyzme SCO1725 shows 93% residual activity in the presence of 10 mM Co2+; isozyme SCO7513 shows 72% residual activity in the presence of 10 mM Co2+
Co2+
-
36.2% residual activity at 1 mM
Co2+
-
complete inhibition
Co2+
-
inhibition at 1 mM
Cs+
-
-
Cu2+
-
strong inhibition
Cu2+
-
47.5% residual activity at 2 mM
Cu2+
-
strong inhibition, 40% residual activity at 50 mM
Cu2+
-
62% residual activity at 5 mM
Cu2+
-
31% inhibition at 10 mM
Cu2+
-
complete inhibition at 10 mM
Cu2+
-
complete inhibition at 5 mM
Cu2+
-
78.35% residual activity at 5 mM
Cu2+
Cephaloleia presignis
-
complete inhibition, 1 mM
Cu2+
-
11% residual activity at 1 mM
Cu2+
-
about 46% inhibition at 5 mM
Cu2+
-
5 mM, 30 min, 70°C, pH 8.5, complete inhibition
Cu2+
-
1 mM, 19% inhibition
Cu2+
-
isozyme Lip-1 shows 75% relative activity in the presence of 5 mM Cu2+; isozyme Lip-2 shows 65% relative activity in the presence of 5 mM Cu2+
Cu2+
-
78.41% relative activity at 1 mM
Cu2+
-
in the presence of 2 mM copper the activity is reduced by 76%
Cu2+
-
about 70% inhibition at 2 mM
Cu2+
Penicillium candidum
-
about 75% inhibition at 1 mM
Cu2+
57% residual activity at 10 mM, with 4-nitrophenyl caproate as substrate, at 25°C
Cu2+
-
strain KKA-5, slight inhibition
Cu2+
-
92% inhibition at 5 mM
Cu2+
-
70% residual activity after 30 min at 8 mM
Cu2+
-
52% inhibition at 1 mM
Cu2+
-
37.5% residual activity at 1 mM
Cu2+
-
SSL and SML show 5% and 30% residual activity, respectively, in the presence of 10 mM Cu2+
Cu2+
-
strong inhibition with substrate tributyrin
Cu2+
-
37.0% residual activity at 10 mM
Cu2+
isoyzme SCO1725 shows 88% residual activity at 1 mM Cu2+; isozyme SCO7513 shows 51% residual activity in the presence of 10 mM Cu2+
Cu2+
-
4.4% residual activity at 1 mM
Cu2+
complete inhibition at 0.1 mM
Cu2+
-
about 25% inhibition at 1 mM
deoxycholate
-
-
deoxycholate
-
no carboxyl esterase activity in presence of 2-hydroxy bile salts, such as deoxycholate and taurodeoxycholate
deoxycholate
-
no carboxyl esterase activity in presence of 2-hydroxy bile salts, such as deoxycholate and taurodeoxycholate
diethyl 4-nitrophenyl phosphate
-
strong inhibition
diethyl 4-nitrophenyl phosphate
-
10% residual activity at 10 mM
diethyl 4-nitrophenyl phosphate
-
rapid and complete inhibition
diethyl 4-nitrophenyl phosphate
-
i.e. E600, 80% and 60% inhibition of SSF lipase and SmF lipase, respectively, pH 7.5, 25°C
diethyl 4-nitrophenyl phosphate
-
diethyl 4-nitrophenyl phosphate
-
diethyl 4-nitrophenyl phosphate is only ìnhibitory in the presence of deoxycholic acid sodium salt (2 mM)
diethyl dicarbonate
-
-
diethyl dicarbonate
-
0.5 mM, 15% residual activity
diethyl dicarbonate
complete inhibition at 0.1 mM
Diethyl p-nitrophenyl phosphate
-
-
Diethyl p-nitrophenyl phosphate
-
-
Diethyl p-nitrophenyl phosphate
-
i.e. E600, inhibition in presence of bile salts
diethyldicarbonate
-
complete inhibition at 5 mM
diethyldicarbonate
-
complete inhibition at 2 mM
diethyldicarbonate
-
10 mM, 17% inhibition
diethyldicarbonate
-
65% inhibition at 0.1 mM, complete inhibition at 1 mM
diethyldicarbonate
-
15% inhibition of recombinant refolded enzyme at 10 mM
diisopropyl fluorophosphate
Cephaloleia presignis
-
complete inhibition, 1 mM
diisopropyl fluorophosphate
-
weak
diisopropyl fluorophosphate
-
inhibits both lipase and phospholipase activities of the enzyme
diisopropyl fluorophosphate
-
30% inhibition at 5 mM, 60% inhibition at 25 mM
diisopropyl fluorophosphate
-
-
dithiothreitol
-
86% residual activity at 1 mM
dithiothreitol
-
5 mM, 30 min, 70°C, pH 8.5, 25% inhibition
dithiothreitol
-
BTID-A, 48% inhibition at 1% w/v
dithiothreitol
-
strong inhibition
dithiothreitol
isoyzme SCO1725 shows 36% residual activity in the presence of 10 mM dithiothreitol; isozyme SCO7513 shows 86% residual activity in the presence of 10 mM dithiothreitol
dithiothreitol
-
inhibition at 1 mM
DTNB
-
competitive inhibition of LIII, 30% inhibition at 5 mM
E600
-
different inhibition levels of recombinant wild-type enzymes and chimeric mutant enzymes, influenced by bile salt, overview
E600
in the absence of surfactant, no inhibition is observed with E600. The addition of beta-octylglucoside is required to trigger the inhibition of cutinase, which is completely inactivated after 12 min
EDTA
-
complete inhibition at 1 mM
EDTA
-
strong, about 90% inhibition at 1 mM
EDTA
-
significant inhibition at 70 mM
EDTA
-
about 22% inhibition at 1 mM
EDTA
-
65.41% residual activity at 5 mM
EDTA
-
15% residual activity at 1 mM
EDTA
-
BTID-B, 45% inhibition at 1% w/v, BTID-A, 68% inhibition at 1% w/v
EDTA
-
10 mM, 92% inhibition
EDTA
-
isozyme Lip-1 shows 25% relative activity in the presence of 5 mM EDTA; isozyme Lip-2 shows 35% relative activity in the presence of 5 mM EDTA
EDTA
-
82% residual activity at 10 mM
EDTA
60% inhibition at 20 mM, poor inhibition at 1 mM
EDTA
47% residual activity at 10 mM, with 4-nitrophenyl caproate as substrate, at 25°C
EDTA
-
60% inhibition at 1 mM, completely reversible by 5 mM MgSO4
EDTA
-
no inhibition of extracellular isozyme 1 by EDTA up to 10 mM, but 80% inhibition of extracellular isozyme 2 by 10 mM EDTA
EDTA
-
38% inhibition at 1 mM
EDTA
-
92% residual activity at 1 mM
EDTA
removal of bound Ca2+ ions inactivates the enzyme
EDTA
-
27-29% inhibition of recombinant refolded enzyme at 0.1-10 mM
EDTA
-
complete inhibition
EDTA
-
16.0% residual activity at 10 mM
EDTA
-
25.3% residual activity at 2 mM
EDTA
-
3% remaining activity at 5 mM
EDTA
-
1 mM, 11% inhibition
EDTA
-
complete inhibition at 10 mM
EDTA
-
almost complete inhibition at 10 mM
EDTA
-
reversible by Hg2+ and Al3+
EDTA
-
inhibition at 1 mM
EGTA
-
15% residual activity at 1 mM
eserine
-
27% inhibition at 5 mM
eserine
-
5 mM, 8% residual activity
ethanol
-
inhibitory effect of organic solvents, overview
ethanol
-
56.2% relative activity at 10% (v/v) ethanol
ethanol
-
BTID-A, 42% inhibition at 1% w/v
ethanol
-
43% activation of recombinant refolded enzyme at 10% v/v, and 44% inhibition at 30% v/v
ethanol
-
98.8% inhibition at 50% (v/v)
Fe2+
-
complete inhibition at 1 mM
Fe2+
-
57.2% residual activity at 2 mM
Fe2+
-
strong inhibition, 30% residual activity at 50 mM
Fe2+
-
30% residual activity at 5 mM
Fe2+
-
33% inhibition at 10 mM
Fe2+
-
36.9% relative activity at 5 mM
Fe2+
-
strong inhibition with residual activity of 20.27% at 5 mM
Fe2+
Cephaloleia presignis
-
complete inhibition, 1 mM
Fe2+
-
18% residual activity at 1 mM
Fe2+
-
about 60% inhibition at 5 mM
Fe2+
-
5 mM, 30 min, 70°C, pH 8.5, 90% inhibition
Fe2+
47% inhibition at 1 mM, 99.2% inhibition at 10 mM
Fe2+
Geotrichum marinum
-
inhibits at 6 mM
Fe2+
-
25.54% relative activity at 1 mM
Fe2+
-
7% residual activity at 10 mM
Fe2+
-
14% residual activity at 10 mM
Fe2+
Penicillium candidum
-
complete inhibition at 1 mM
Fe2+
-
strain KKA-5, strong inhibition
Fe2+
-
1 mM, 63% inhibition
Fe2+
-
71.37% residual activity at 1 mM
Fe2+
-
SSL and SML show 73% and 18% residual activity, respectively, in the presence of 10 mM Fe2+
Fe2+
-
14.0% residual activity at 10 mM
Fe2+
-
inhibition at 1 mM
Fe3+
-
strong inhibition, 25% residual activity at 50 mM
Fe3+
-
77% residual activity at 5 mM
Fe3+
-
complete inhibition at 5 mM
Fe3+
-
12.8% relative activity at 5 mM
Fe3+
-
strong inhibition with residual activity of 35.11% at 5 mM
Fe3+
Cephaloleia presignis
-
complete inhibition, 1 mM
Fe3+
-
68% inhibition at 1 mM
Fe3+
-
58.56% relative activity at 1 mM
Fe3+
complete inhibition at 10 mM, with 4-nitrophenyl caproate as substrate, at 25°C
Fe3+
-
strain KKA-5, strong inhibition
Fe3+
-
1 mM, 67% inhibition
Fe3+
-
97% inhibition at 1 mM
Fe3+
-
60% inhibition at 1 mM
Fe3+
-
14% inhibition of recombinant refolded enzyme at 10 mM, 23% at 1 mM, 18% at 0.1 mM
Fe3+
-
SSL and SML show 28% and 9% residual activity, respectively, in the presence of 10 mM Fe3+
Fe3+
-
12% residual activity at 10 mM
Hg2+
-
77% residual activity at 1 mM
Hg2+
-
Hg2+ shows the highest reduction in enzyme activity by 83.3% at 1 mM
Hg2+
-
32.3% residual activity at 5 mM
Hg2+
-
72% inhibition at 70 mM
Hg2+
-
strong inhibition with residual activity of 13.19% at 5 mM
Hg2+
-
5 mM, 30 min, 70°C, pH 8.5, 55% inhibition
Hg2+
-
1 mM, 89% inhibition
Hg2+
-
75% inhibition at 1 mM
Hg2+
-
isozyme Lip-1 shows 20% relative activity in the presence of 5 mM Hg2+; isozyme Lip-2 shows 25% relative activity in the presence of 5 mM Hg2+
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
76% residual activity at 2 mM
Hg2+
-
complete inhibition at 1 mM
Hg2+
complete inhibition at 1 mM
Hg2+
11% residual activity at 10 mM, with 4-nitrophenyl caproate as substrate, at 25°C
Hg2+
-
strain KKA-5, strong inhibition
Hg2+
-
94% inhibition at 5 mM
Hg2+
-
1 mM, 16% inhibition
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
43.75% residual activity at 1 mM
Hg2+
-
SSL and SML show 7% and 9% residual activity, respectively, in the presence of 10 mM Hg2+
Hg2+
-
activity is completely inhibited at 1 mM
Hg2+
complete inhibition at 0.1 mM
Hg2+
-
almost complete inhibition at 1 mM
HgCl2
-
complete inhibition at 1 mM
iodoacetic acid
-
88% residual activity at 5 mM
Isopropanol
-
inhibitory effect of organic solvents, overview
Isopropanol
-
40.2% relative activity at 10% (v/v) isopropanol
Isopropanol
-
slight inhibition at 1%
Isopropanol
-
39% activation of recombinant refolded enzyme at 10% v/v, and 44% inhibition at 30% v/v
Isopropanol
-
98.9% inhibition at 50% (v/v)
K+
-
39% residual activity at 1 mM
K+
-
about 48% inhibition at 5 mM
K+
-
82% residual activity at 2 mM
K+
-
75% residual activity at 1 mM
K+
-
SML shows 85% residual activity in the presence of 10 mM Ki+
K+
-
89.0% residual activity at 10 mM
Li+
-
76.4% residual activity at 1 mM
Li+
-
82% residual activity at 5 mM
Li+
-
92.24% residual activity at 5 mM
Li+
-
about 10% inhibition at 5 mM
Li+
-
5 mM, 30 min, 70°C, pH 8.5, 15% inhibition
Li+
-
56% inhibition at 1 mM
Li+
-
SSL and SML show 80% and 60% residual activity, respectively, in the presence of 10 mM Li+
Li+
-
98.2% residual activity at 1 mM
Li+
88% residual activity at 1 mM
methanol
-
54.3% relative activity at 10% (v/v) methanol
methanol
-
99% inhibition at 50% (v/v)
Mg2+
-
85% residual activity at 2 mM
Mg2+
-
78% residual activity at 5 mM
Mg2+
-
96.6% relative activity at 5 mM
Mg2+
-
94.49% residual activity at 1 mM
Mg2+
-
about 30% inhibition at 1 mM
Mg2+
-
5 mM, 30 min, 70°C, pH 8.5, 25% inhibition
Mg2+
-
86% residual activity at 1 mM
Mg2+
-
86% residual activity at 2 mM
Mg2+
-
80% residual activity at 1 mM
Mg2+
-
about 70% inhibition at 2 mM
Mg2+
54% residual activity at 10 mM, with 4-nitrophenyl caproate as substrate, at 25°C
Mg2+
-
32% inhibition at 5 mM
Mg2+
-
10% activation of recombinant refolded enzyme at 1 mM, 15% inhibition at 10 mM
Mg2+
-
SSL and SML show 54% and 71% residual activity, respectively, in the presence of 10 mM Mg2+
Mg2+
-
slightly inhibits the reaction activity but enhances the enantioselectivity of the hydrolysis of (R,S)-flurbiprofen ethyl ester
Mg2+
-
88.0% residual activity at 10 mM
Mg2+
isoyzme SCO1725 shows 92% residual activity in the presence of 10 mM Mg2+; isozyme SCO7513 shows 83% residual activity in the presence of 10 mM Mg2+
Mg2+
-
1 mM, 17% inhibition
Mg2+
-
64.2% residual activity at 1 mM
Mg2+
62% residual activity at 0.1 mM
Mg2+
-
inhibition at 1 mM
Mn2+
-
complete inhibition at 1 mM
Mn2+
-
71% residual activity at 5 mM
Mn2+
-
complete inhibition at 5 mM
Mn2+
-
58.6% relative activity at 5 mM
Mn2+
-
90.66% residual activity at 5 mM
Mn2+
-
about 75% inhibition at 1 mM
Mn2+
-
5 mM, 30 min, 70°C, pH 8.5, 25% inhibition
Mn2+
Geotrichum marinum
-
inhibits at 6 mM
Mn2+
-
81% inhibition at 1 mM
Mn2+
-
92% residual activity at 2 mM
Mn2+
55% residual activity at 10 mM, with 4-nitrophenyl caproate as substrate, at 25°C
Mn2+
-
strain KKA-5, slight inhibition
Mn2+
-
47% inhibition at 5 mM
Mn2+
-
1 mM, 18% inhibition
Mn2+
-
17% inhibition at 1 mM
Mn2+
-
75% residual activity at 1 mM
Mn2+
-
SSL and SML show 80% and 60% residual activity, respectively, in the presence of 10 mM Mn2+
Mn2+
-
60.0% residual activity at 10 mM
Mn2+
92% residual activity at 1 mM
Mn2+
-
complete inhibition
N-bromosuccinimide
-
34.4% residual activity at 5 mM
N-bromosuccinimide
-
complete inhibition at 0.001 mM
N-bromosuccinimide
-
5 mM, 30 min, 70°C, pH 8.5, 55% inhibition
Na+
-
-
Na+
-
about 75% inhibition at 5 mM
Na+
-
89% residual activity at 2 mM
Na+
-
90.0% residual activity at 10 mM
NaCl
-
loss of 50% activity at 7.5%
NaN3
-
78% residual activity at 10 mM
NaN3
-
75% residual activity at 1 mM
NEM
-
10% inhibition at 5 mM
Ni2+
-
60% residual activity at 1 mM
Ni2+
-
78% inhibition at 10 mM
Ni2+
-
92.24% residual activity at 5 mM
Ni2+
-
7% residual activity at 1 mM
Ni2+
-
about 45% inhibition at 5 mM
Ni2+
-
86% inhibition at 1 mM
Ni2+
-
40.0% residual activity at 10 mM
Ni2+
-
almost complete inhibition at 1 mM
orlistat
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
paraoxon
inhibition of the lipase activities toward emulsified triolein and dissolved p-nitrophenyl acetate by a 1000fold molar excess of paraoxon, 1 h, 99% inhibition
Pb2+
-
6.22% relative activity at 1 mM
Pb2+
-
1 mM, 22% inhibition
Pb2+
-
24.4% residual activity at 1 mM
phenylmethylsulfonyl fluoride
-
-
phenylmethylsulfonyl fluoride
-
11.6% residual activity at 5 mM
phenylmethylsulfonyl fluoride
-
18% residual activity at 5 mM
phenylmethylsulfonyl fluoride
-
completely inactivates the original lipase at 70 mM
phenylmethylsulfonyl fluoride
-
complete inhibition at 10 mM
phenylmethylsulfonyl fluoride
-
38.54% residual activity 5 mM
phenylmethylsulfonyl fluoride
-
about 99% inhibition at 5 mM
phenylmethylsulfonyl fluoride
-
9.1% relative activity at 1 mM
phenylmethylsulfonyl fluoride
-
54% residual activity at 5 mM
phenylmethylsulfonyl fluoride
-
36% residual activity at 5 mM
phenylmethylsulfonyl fluoride
-
weak
phenylmethylsulfonyl fluoride
complete inhibition at 10 mM, with 4-nitrophenyl caproate as substrate, at 25°C
phenylmethylsulfonyl fluoride
remarkable reduction in activity at 1 mM
phenylmethylsulfonyl fluoride
-
SML shows 32% residual activity in the presence of 10 mM phenylmethylsulfonyl fluoride
phenylmethylsulfonyl fluoride
-
0.5 mM, 46% residual activity
phenylmethylsulfonyl fluoride
-
-
phenylmethylsulfonyl fluoride
-
complete inhibition at 1 mM
phenylmethylsulfonyl fluoride
-
PMSF
-
slight inhibition
PMSF
-
about 15% inhibition at 1 mM
PMSF
about 40% inhibition at 10 mM, 20% at 1 mM
PMSF
-
5 mM, 30 min, 70°C, pH 8.5, complete inhibition
PMSF
strong inhibition at 10 mM
PMSF
-
BTID-A, 92% inhibition at 1% w/v
PMSF
-
10 mM, 89% inhibition
PMSF
75% inhibition of recombinant LipY at 5 mM
PMSF
-
19% inhibition at 5 mM
PMSF
-
inhibition of both extracellular isozymes
PMSF
-
43% inhibition of recombinant refolded enzyme at 10 mM, 15% at 1 mM
PMSF
-
complete inhibition at 10 mM
PMSF
-
98% nhibition at 15 mM
Pyridine
-
rapid deactivation
Pyridine
25-30% inhibition at about 30% v/v
Rb+
-
about 10% inhibition at 5 mM
SDS
-
complete inhibition at 1% (w/v)
SDS
-
0.201% residual activity at 0.1% (w/v)
SDS
-
21.3% residual activity at 5 mM
SDS
-
20% inhibition at 1 mM
SDS
-
31.2% relative activity at 0.05% (w/v) SDS
SDS
-
SDS sharply decreases the lipase activity by 85% at 0.1% (w/v)
SDS
-
inactive in the presence of micellar concentrations of SDS
SDS
-
10% residual activity at 0.001% (v/v)
SDS
98% inhibition at 0.1% w/v
SDS
complete inhibition of both wild-type and mutant N-fused enzymes at 0.1 mM
SDS
-
about 90% inhibition at 1% (w/v) SDS
SDS
-
1% w/v, 95% decrease in activity
SDS
-
BTID-B, complete inhibition at 1% w/v, no inhibition of BTID-A
SDS
Geotrichum marinum
-
complete inhibition at 1 mM
SDS
the complete inhibition is partially reversible by Triton X-100, 20% of maximal activity can be recovered
SDS
-
50% inhibition at 2mM
SDS
-
42% inhibition at 0.1% w/v
SDS
0.9% residual activity at 10 mM, with 4-nitrophenyl caproate as substrate, at 25°C
SDS
-
93% inhibition at 5 mM
SDS
-
95% inhibition at 0.4%
SDS
-
44% residual activity at 0.1% (w/v) after 15 min incubation, 24.3% residual activity at 0.1% (w/v) after 30 min incubation, 5.3% residual activity at 0.1% (w/v) after 45 min incubation
SDS
-
52% activation of the recombinant refolded enzyme at 1% w/v, 83% inhibition of the recombinant refolded enzyme at 5% w/v
SDS
-
SDS shows strong inhibitory effect on SSL and SML, leaving residual activity of 43% and 28%, respectively
SDS
-
20.1% residual activity at 0.1% (w/v)
Sn2+
-
complete inhibition at 5 mM
Sn2+
-
1 mM, 20% inhibition
sodium cholate
Penicillium candidum
-
-
sodium deoxycholate
-
isozymes Lip3 and Lip1, inhibition kinetics
sodium deoxycholate
inhibits at 1%
sodium deoxycholate
-
the enzyme is inhibited by bile salts
sodium deoxycholate
-
recombinant and native enzymes are partially inhibited by the sodium deoxycholate and retain respectively 30 and 25% of their activities at 8 mM
sodium deoxycholate
-
90% residual activity after 5 h at 25% (v/v)
sodium deoxycholate
-
40% loss of activity in presence of 8 mM sodium deoxycholate
sodium deoxycholate
-
completely inhibited at 4 mM sodium deoxycholate
sodium taurocholate
55% inhibition of wild-type enzyme and slight activation of the mutant N-fused enzyme at 1 mM
sodium taurocholate
-
67% inhibition at 5 mM
sodium taurodeoxycholate
-
bile salts are required by the pancreatic lipase, optimal activation at 0.1 mM, inhibits the recombinant chimeric protein NcC2 at concentration above 2 mM
sodium taurodeoxycholate
-
-
sodium taurodeoxycholate
-
the inhibition is reversed by the addition of colipase
taurodeoxycholate
-
no carboxyl esterase activity in presence of 2-hydroxy bile salts, such as deoxycholate and taurodeoxycholate
taurodeoxycholate
-
no carboxyl esterase activity in presence of 2-hydroxy bile salts, such as deoxycholate and taurodeoxycholate
tetrahydrolipstatin
-
complete inhibition at 1 mM
tetrahydrolipstatin
inhibition of ROLw
Triton X-100
-
complete inhibition at 1% (w/v)
Triton X-100
-
48.55% residual activity at 0.1% (v/v)
Triton X-100
-
inactive in the presence of micellar concentrations of Triton X-100
Triton X-100
strong inhibition of both wild-type and mutant N-fused enzymes at 1 mM
Triton X-100
the inhibition is fully reversible by addition of bile salts and colipase
Triton X-100
inhibits at 1%
Triton X-100
-
1% w/v, 30% decrease in activity
Triton X-100
Geotrichum marinum
-
complete inhibition at 1 mM
Triton X-100
-
complete inhibition at 10% (v/v)
Triton X-100
activates at 0.1%, inhibits at higher concentrations
Triton X-100
-
complete inhibition at 10% (v/v)
Triton X-100
-
48% inhibition at 0.01%
Triton X-100
inhibition at concentrations above 1%
Triton X-100
-
91% residual activity at 1 mM
Triton X-100
-
19-39% activation of the recombinant refolded enzyme at 0.2-1% w/v, 89% inhibition of the recombinant refolded enzyme at 5% w/v
Triton X-100
-
inhibits the activity seriously
Triton X-100
-
2.3% residual activity at 0.1% (w/v)
Triton X-100
-
the activity of the enzyme dereases rapidly with a concentration of Triton X-100 greater than 0.3 mM
Triton X-100
the protein retains about 70% activity with Triton X-100
Triton X-45
-
42-45% activation of the recombinant refolded enzyme at 0.2-1% w/v, 31% inhibition of the recombinant refolded enzyme at 5% w/v
-
Triton X-45
-
inhibits the activity seriously
-
Tween 20
-
little inhibitory effect
Tween 20
-
82.52% residual activity at 0.1% (v/v)
Tween 20
18-19% inhibition at 0.1-1.0% w/v
Tween 20
over 90% inhibition of both wild-type and mutant N-fused enzymes at 1 mM
Tween 20
-
about 90% inhibition at 1% (w/v) Tween 20
Tween 20
-
1% w/v, 7% decrease in activity
Tween 20
Geotrichum marinum
-
complete inhibition at 1 mM
Tween 20
-
74% residual activity after 5 h at 25% (v/v)
Tween 20
-
40% residual activity at 1 mM
Tween 20
-
80.1% residual activity at 0.1% (w/v)
Tween 40
-
10% residual activity at 0.001% (v/v)
Tween 40
-
about 40% inhibition at 1% (w/v) Tween 40
Tween 80
-
4% residual activity at 1% (v/v)
Tween 80
-
little inhibitory effect
Tween 80
-
57.24% residual activity at 0.1% (v/v)
Tween 80
-
10% residual activity at 0.001% (v/v)
Tween 80
about 30% inhibition of both wild-type and mutant N-fused enzymes at 1 mM
Tween 80
-
about 50% inhibition at 1% (w/v) Tween 80
Tween 80
-
1% w/v, 6% decrease in activity
Tween 80
-
20% residual activity at 10% (v/v)
Tween 80
-
33% residual activity at 10% (v/v)
Tween 80
Penicillium candidum
-
-
Tween 80
-
60% residual activity at 1 mM
Tween 80
-
72% residual activity at 1% (v/v)
Zn2+
-
67% residual activity at 1 mM
Zn2+
-
32.2% residual activity at 2 mM
Zn2+
-
59.1% residual activity at 5 mM
Zn2+
-
72.41% residual activity at 5 mM
Zn2+
-
69.1% inhibition at 50 mM
Zn2+
-
86% inhibition at 10 mM
Zn2+
-
28.9% relative activity at 5 mM
Zn2+
Cephaloleia presignis
-
complete inhibition, 1 mM
Zn2+
-
3% residual activity at 1 mM
Zn2+
-
about 57% inhibition at 5 mM
Zn2+
-
5 mM, 30 min, 70°C, pH 8.5, 85% inhibition
Zn2+
65% inhibition at 1 mM, 98.4% inhibition at 10 mM
Zn2+
-
86% inhibition at 1 mM
Zn2+
-
98% inhibition at 1 mM
Zn2+
-
isozyme Lip-1 shows 20% relative activity in the presence of 5 mM Zn2+; isozyme Lip-2 shows 18% relative activity in the presence of 5 mM Zn2+
Zn2+
-
49% residual activity at 10 mM
Zn2+
1 mM, 40% residual activity
Zn2+
-
90% residual activity at 2 mM
Zn2+
-
51% residual activity at 10 mM
Zn2+
-
about 70% inhibition at 2 mM
Zn2+
-
strain KKA-5, strong inhibition, strain MB5001: 94% inhibition at 1 mM
Zn2+
-
85% inhibition at 5 mM
Zn2+
-
activates extracellular isozyme 1 slightly, inhibits extracellular isozyme 2
Zn2+
-
51% residual activity after 30 min at 1 mM
Zn2+
-
1 mM, 65% inhibition
Zn2+
-
50% residual activity at 1 mM
Zn2+
-
70% inhibition of recombinant refolded enzyme at 10 mM, 66% at 1 mM, 35% at 0.1 mM
Zn2+
-
SSL and SML show 76% and 55% residual activity, respectively, in the presence of 10 mM Zn2+
Zn2+
-
strong inhibition with substrate tribuyrin
Zn2+
-
16.2% residual activity at 10 mM
Zn2+
-
80% residual activity at 2 mM
Zn2+
-
1 mM, 17% inhibition
Zn2+
58% residual activity at 1 mM
Zn2+
-
complete inhibition
Zn2+
-
slight inhibition at 1 mM
additional information
-
no inhibition by 2-mercaptoethanol, dithiothreitol, and Zn2+
-
additional information
-
not affected by EDTA, sodium citrate, SDS, myristic acid, palmitic acid, and urea (6.0 M). The enzyme is not inhibited by iodoacetate, citraconic anhydride, phenylglyoxal, and N-acetylimidazole
-
additional information
-
no effect by metal chelators, no inhibition by trinitrobenzene sulfonic acid, N-ethylmaleimide, p-chloromercuribenzoate, o-phenanthroline, and 4,4'-dipyridyl-disulfide
-
additional information
-
not inhibited by Ca2+, Mn2+, Ni2+, Ba2+, and EDTA
-
additional information
-
no inhibition by EDTA 50 mM
-
additional information
-
not inhibited by citraconic anhydride (5 mM), N-ethylmaleimide (10 mM), iodoacetate (10 mM), N-acetylimidazole (10 mM), and phenylglyoxal (10 mM)
-
additional information
-
not inhibited by EDTA
-
additional information
-
Na+ has no significant effect on the enzyme activity; the activity is strongly affected by the thiol inhibitor N-bromosuccinimide
-
additional information
-
enzyme from strain A30-1 is stable to alkaline protease treatment
-
additional information
-
not affected by EDTA
-
additional information
no inhibition with PMSF
-
additional information
-
no inhibition with PMSF
-
additional information
-
not inhibited by sodium taurodeoxycholate and CHAPS
-
additional information
Cephaloleia presignis
-
not affected by Ca2+, Mn2+, Mg2+, Na+, K+, PMSF, EDTA, all at 1 mM
-
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
-
additional information
-
pancreatic lipase NcCc is probably irreversibly inactivated at the surface of tributyrin droplets which is prevented by colipase
-
additional information
-
Span 20 does not affect the activity
-
additional information
-
no inhibition by iodoacetamide, K+, Na+ at 5 mM
-
additional information
no inhibition by EDTA, PMSF, 2-mercaptoethanol, PMSF, DTT, Tween 20, 3-[(3-cholamidopropyl)dimethylammonio]-1-propane sulfonic acid, or Triton X-100
-
additional information
-
poor inhibition by Mg2+ at 1 mM, and by 2-mercaptoethanol, DTT, SDS, and EDTA at 1%
-
additional information
-
changes in HDL cholesteryl ester and fatty acid content have no effect on hepatic lipase displacement, increases in HDL phospholipid and TG content significantly inhibit hepatic lipase displacement
-
additional information
-
no inhibition by 2-mercaptoethanol, PMSF, and iodoacetamide
-
additional information
-
not significantly affected by Na+, K+, Mg2+, Mn2+, Cd2+, Ca2+, and EDTA
-
additional information
not inhibitory: Na+, K+, Ca2+, Mg2+, Cu2+, Co2+, Fe2+ at 1 mM
-
additional information
-
not inhibitory: Na+, K+, Ca2+, Mg2+, Cu2+, Co2+, Fe2+ at 1 mM
-
additional information
-
no inhibition by PMSF, E-64, 1,10-phenanthroline, and tosyllysylchloromethyl ketone
-
additional information
-
competitive substrate inhibition
-
additional information
insulin suppresses expression of the enzyme
-
additional information
-
insulin suppresses expression of the enzyme
-
additional information
-
no inhibition by Ca2+, Triton X-100 and NP-40 decreased the activity marginally at lower concentrations and then restorde the activity at 4 mM
-
additional information
-
no inhibition by Ca2+, Mg2+, Mn2+, Na+, K+, Cu2+, EDTA, p-chloromercuribenzoate, and iodoacetate
-
additional information
-
strain KKA-5, no inhibition by Ca2+ and Mg2+
-
additional information
-
alcohols and glycols up to 20% activates the enzyme, high concentrations inhibit
-
additional information
-
no inhibition of extracellular enzyme by 1 M NaCl, 0.1 mg/ml heparin, and SH-reagents 4-hydroymercuribenzoate, 2-mercaptoethanol, iodoacetate, sodium diphosphate, and NaF
-
additional information
-
the enzyme is repressed by long-chain fatty acids including oleic acid
-
additional information
-
no inhibition by EDTA at 1 mM
-
additional information
-
no inhibition by EDTA, DTT, iodoacetic acid, and o-phenanthroline
-
additional information
-
the enzyme is not affected by EDTA and Tween 80
-
additional information
-
the enzyme activity is not affected significantly by Hg2+, Ca2+, Mg2+, Fe3+, EDTA and phenylmethylsulfonyl fluoride (1 mM each)
-
additional information
-
the lipase of strain F-111 is unaffected by various detergents
-
additional information
-
no inhibition by PMSF, no inhibition by Tween 20, Tween 80, and Triton X-100, negligible inhibition by Zn2+
-
additional information
-
no inhibition by Ca2+, Hg2+, Zn2+, Mn2+, Cu2+, Mg2+, Co2+, Cd2+, Pb2+, EDTA, and o-phenanthrolin
-
additional information
effects of detergents on LipA1 activity, overview
-
additional information
-
enzyme is not affected by benzamidine and PMSF
-
additional information
-
not affected by 2-mercaptoethanol and EDTA
-
additional information
-
denaturation of the pure SDL at the tributyrin/water interface due to the high interfacial energy
-
additional information
-
effects of surfactants on the enantioselective hydrolysis of (R,S)-flurbiprofen ethyl ester into (S)-flurbiprofen, PMSF are poor inhibitors
-
additional information
no inhibition by bile salts or amphiphilic proteins
-
additional information
-
no inhibition by bile salts or amphiphilic proteins
-
additional information
Ca2+ and Mg2+ do not significantly reduce the lipolytic activity, resistant to inhibition by phenylmethylsulfonyl fluoride; Ca2+ and Mg2+ do not significantly reduce the lipolytic activity, resistant to inhibition by phenylmethylsulfonyl fluoride
-
additional information
Ca2+ and Mg2+ do not significantly reduce the lipolytic activity, resistant to inhibition by phenylmethylsulfonyl fluoride; Ca2+ and Mg2+ do not significantly reduce the lipolytic activity, resistant to inhibition by phenylmethylsulfonyl fluoride
-
additional information
-
plant extracts from bearberry (Arctostaphylos uva-ursi), garden pea (Pisum sativum), Norway spruce (Picea abies) and large leaved lime (Tilia platyphyllos) show inhibition of pancreatic lipase (over 40%)
-
additional information
-
not affected by EDTA and Ca2+
-
additional information
-
palm olein water content above 3.6% (v/v) inhibits the activity of lipase
-
additional information
-
effect of buffer conditions on the enzyme activity
-
additional information
not inhibited by phenylmethylsulfonyl fluoride, eserine, and SDS
-
additional information
no inhibition of YLLIP2 by bile salts at micellar concentrations
-
additional information
the LIP2 is not affected by Mg2+, Mn2+, EDTA, SDS, Tween 80, Span 65, Span 85, Triton X-100, DTT, and 2-mercaptoethanol
-
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1,1,1-trichloroethane
-
enzyme catalyzes the regioselective hydrolysis of preacetylated monosaccharide derivatives in
1,4-butanediol
half-life is 7.4 days
1,4-dioxane
-
18 h at 50% v/v, 100% stable
1,5-pentanediol
half-life is 0.19 days
1-dodecanol
-
149.6% activity at 1% (v/v)
1-undecanol
-
the enzyme retains its activity of 74% in the presence of 1% (v/v) 1-undecanol
amyl alcohol
48 h, 92.5% remaining activity, purified recombinant LipAB, incubation in 50% alcohol/water solution at room temperature
cetyltrimethylammonium bromidecetyltrimethylammonium bromide
diethyl ether
-
50%, 30 min, 70°C, pH 8.5, complete loss of activity
ethyl methyl ketone
-
75% remaining activity after 10 min at 50°C
ethylbenzene
-
the enzyme retains its activity of 77% in the presence of 1% (v/v) ethylbenzene
Ethylene glycol
half-life is 84.6 days
isoamyl alcohol
-
the enzyme is highly resistant to 50% (v/v) isoamylalcohol (108% activity)
n-heptadecane
-
142.5% activity at 1% (v/v)
n-hexacedane
-
the enzyme retains its activity of 78% in the presence of 1% (v/v) n-hexadecane
n-hexadecane
-
81% activity at 50% (v/v)
n-octane
half-life is 9.2 days
n-pentadecane
-
128.5% activity at 1% (v/v)
n-propanol
48 h, 93.5% remaining activity, purified recombinant LipAB, incubation in 50% alcohol/water solution at room temperature
n-tetradecane
-
115.8% activity at 1% (v/v)
o-xylene
-
136.1% activity at 1% (v/v)
propan-2-ol
-
97% loss of activity after 30 min in 60% propan-2-ol, loss of only 3% activity after 30 min in 30% propan-2-ol
propanol
-
100% activity at 20% (v/v)
sorbitol
-
50%, 30 min, 70°C, pH 8.5, 10% activation
toluol
-
50%, 30 min, 70°C, pH 8.5, complete loss of activity
Tween
stable in the presence of the detergent Tween 20
1-butanol
-
0.917% residual activity at 50% (v/v), 4.28% residual activity at 10% (v/v)
1-butanol
-
0.917% residual activity at 50% (v/v), 4.28% residual activity at 10% (v/v)
-
1-decanol
-
the enzyme retains its activity of 86% in the presence of 1% (v/v) 1-decanol
1-decanol
-
30% (v/v), half-life: more than 5 days, the half-life of the enzyme in absence of organic solvents is 3 days
1-octanol
-
137.3% activity at 1% (v/v)
1-octanol
-
215% activity at 20% (v/v)
2,3-butanediol
-
100.4% activity at 1% (v/v)
2,3-butanediol
-
100.4% activity at 1% (v/v)
-
2-propanol
22°C, stable to
2-propanol
-
22°C, stable to
-
2-propanol
-
30% v/v, 1 h, 30°C, 0.1 M Tris buffer, pH 8.0, 47% reduced activity
2-propanol
-
for the concentrated lipase, the availability of 5% 2-propanol is sufficient to hold the lipase in monomeric form
2-propanol
-
30% v/v, 1 h, 30°C, 0.1 M Tris buffer, pH 8.0, 47% reduced activity
-
2-propanol
-
70%, 30°C, completely stable for 1 h, loss of 18% activity after 2h
2-propanol
-
70%, 30°C, completely stable for 1 h, loss of 18% activity after 2h
-
Acetone
-
0.917% residual activity at 50% (v/v), 113% activity at 10% (v/v)
Acetone
-
0.917% residual activity at 50% (v/v), 113% activity at 10% (v/v)
-
Acetone
-
the residual activities of Lip5 double mutant remains at 44.76% after incubation for 1 h in 30% (v/v) acetone
Acetone
-
the residual activities of Lip5 double mutant remains at 44.76% after incubation for 1 h in 30% (v/v) acetone
-
Acetone
-
50%, 30 min, 70°C, pH 8.5, loss of 60% activity
Acetone
-
50%, 30 min, 70°C, pH 8.5, loss of 60% activity
-
Acetone
-
30% v/v, 1 h, 30°C, 0.1 M Tris buffer, pH 8.0, 16% reduced activity
Acetone
-
30% v/v, 1 h, 30°C, 0.1 M Tris buffer, pH 8.0, 16% reduced activity
-
Acetone
-
70%, 30°C, completely stable for 1 h, loss of 60% activity after 2h
Acetone
-
70%, 30°C, completely stable for 1 h, loss of 60% activity after 2h
-
Acetone
-
30% (v/v), half-life: 1 day, the half-life of the enzyme in absence of organic solvents is 3 days
Acetone
-
complete inhibition at 50% (v/v)
Acetone
-
complete inhibition at 50% (v/v)
Acetone
-
complete inactivation at pH 8.0
Acetone
-
at 25% v/v, 30°C, 95% remaining activity after 24 h, 33% after 48 h
Acetone
-
150% activity at 20% (v/v)
Acetone
-
150% activity at 20% (v/v)
-
Acetone
-
18 h at 50% v/v, 80% remaining activity
Acetone
the enzyme displays 100% activity in presence of 30% (v/v) acetone
Acetone
30°C, 30 min, about 90% remaining activity at 10%, inactivation at 20%
acetonitrile
-
66% activity at 50% (v/v)
acetonitrile
-
loss of about 25% activity at 30% v/v after 1 h at 30°C
acetonitrile
-
loss of about 25% activity at 30% v/v after 1 h at 30°C
-
acetonitrile
-
30% (v/v), half-life: less than 1 day, the half-life of the enzyme in absence of organic solvents is 3 days
acetonitrile
-
30% (v/v), half-life: less than 1 day, the half-life of the enzyme in absence of organic solvents is 3 days
-
acetonitrile
over 50% activity is retained at 70°C in the presence of 25% (v/v) acetonitrile
acetonitrile
-
18 h at 50% v/v, 92% remaining activity
benzene
-
the enzyme is highly resistant to 50% (v/v) benzene
benzene
-
142.0% activity at 1% (v/v)
benzene
-
30% (v/v), half-life: 2 days, the half-life of the enzyme in absence of organic solvents is 3 days
Brij 35
-
121% relative activity after 5 h at 25% (v/v)
Brij 35
-
121% relative activity after 5 h at 25% (v/v)
-
Butanol
-
60% activity at 50% (v/v)
Butanol
-
80% loss of activity after 30 min, complete loss of activity after 24 h
Butanol
-
50%, 30 min, 70°C, pH 8.5, complete loss of activity
Butanol
-
50%, 30 min, 70°C, pH 8.5, complete loss of activity
-
Butanol
-
70%, 30°C, complete immediate inactivation
Butanol
-
70%, 30°C, complete immediate inactivation
-
Butanol
-
93.6% inactivation at pH 8.0
Butanol
-
at 25% v/v, 30°C, 10% remaining activity after 48 h
cetyltrimethylammonium bromidecetyltrimethylammonium bromide
-
stimulated in the presence of 0.1% cetyltrimethylammonium bromidecetyltrimethylammonium bromide (145.3% relative activity)
cetyltrimethylammonium bromidecetyltrimethylammonium bromide
-
stimulated in the presence of 0.1% cetyltrimethylammonium bromidecetyltrimethylammonium bromide (145.3% relative activity)
-
chloroform
-
50%, 30 min, 70°C, pH 8.5, complete loss of activity
chloroform
-
30% (v/v), half-life: 2 days, the half-life of the enzyme in absence of organic solvents is 3 days
chloroform
-
at 25% v/v, 30°C, 130% activity after 24 h, 140% after 48 h
chloroform
-
400% activity at 20% (v/v)
chloroform
-
400% activity at 20% (v/v)
-
cyclohexane
-
30% (v/v), half-life: more than 5 days, the half-life of the enzyme in absence of organic solvents is 3 days
cyclohexane
half-life is 0.48 days
dimethyl formamide
-
the purified enzyme is stable for over 30 days at 20-55°C in presence of water-miscible organic solvents such as alcohols, glycols, pyridine, acetonitrile, dimethyl formamide, or dimethyl sulfoxide
dimethyl formamide
-
the purified enzyme is stable for over 30 days at 20-55°C in presence of water-miscible organic solvents such as alcohols, glycols, pyridine, acetonitrile, dimethyl formamide, or dimethyl sulfoxide
-
dimethyl sulfoxide
half-life is 3.4 days
dimethyl sulfoxide
-
the purified enzyme is stable for over 30 days at 20-55°C in presence of water-miscible organic solvents such as alcohols, glycols, pyridine, acetonitrile, dimethyl formamide, or dimethyl sulfoxide
dimethyl sulfoxide
-
the purified enzyme is stable for over 30 days at 20-55°C in presence of water-miscible organic solvents such as alcohols, glycols, pyridine, acetonitrile, dimethyl formamide, or dimethyl sulfoxide
-
dimethyl sulfoxide
-
18 h at 50% v/v, 63% remaining activity
dimethylformamide
-
loss of about 10% activity at 30% v/v after 1 h at 30°C
dimethylformamide
-
loss of about 10% activity at 30% v/v after 1 h at 30°C
-
dimethylformamide
-
30% (v/v), half-life: 2 days, the half-life of the enzyme in absence of organic solvents is 3 days
dimethylformamide
-
at 25% v/v, 30°C, 120% activity after 24 h, 110% after 48 h, 100% remaining activity after 30 min at 50°C
dimethylsulfoxide
-
stimulated in the presence of 10% dimethylsulfoxide (105.1% relative activity)
dimethylsulfoxide
-
stimulated in the presence of 10% dimethylsulfoxide (105.1% relative activity)
-
DMSO
-
92% activity at 50% (v/v)
DMSO
-
57.2% residual activity at 50% (v/v), 99.1% activity at 10% (v/v)
DMSO
-
the enzyme retains its activity of 62.5% in the presence of 1% (v/v) DMSO
DMSO
-
30% (v/v), half-life: 2 days, the half-life of the enzyme in absence of organic solvents is 3 days
DMSO
30°C, 30 min, about 90% remaining activity at 10%, 95% activity at 20%
DMSO
at 50%, 3 h, room temperature, purified recombinant LipY7p, over 60% remaining activity
DMSO
at 50%, 3 h, room temperature, purified recombinant LipY8p, over 60% remaining activity
DMSO
-
at 50%, 3 h, room temperature, purified recombinant LipY8p, over 60% remaining activity
-
DMSO
-
at 50%, 3 h, room temperature, purified recombinant LipY7p, over 60% remaining activity
-
Ethanol
-
60% activity at 50% (v/v)
Ethanol
-
complete loss of activity after 30 min in 90% ethanol, loss of 41% activity after 30 min in 40% ethanol
Ethanol
-
2.14% residual activity at 50% (v/v), 100% activity at 10% (v/v)
Ethanol
-
2.14% residual activity at 50% (v/v), 100% activity at 10% (v/v)
-
Ethanol
-
1 h, pH 7.0, 37°C, the mycelium-bound and constitutive enzymes are very stable in presence of ethanol
Ethanol
48 h, stable, purified recombinant LipAB, incubation in 50% alcohol/water solution at room temperature
Ethanol
22°C, crude enzyme is significantly more resistant to higher concentrations of ethanol (above 40%) than to lower concentrations (20%), whereas purified lipase is inactivated by concentrations of above 40%
Ethanol
-
22°C, crude enzyme is significantly more resistant to higher concentrations of ethanol (above 40%) than to lower concentrations (20%), whereas purified lipase is inactivated by concentrations of above 40%
-
Ethanol
-
the residual activities of Lip5 double mutant remains at 24.32% after incubation for 1 h in 30% (v/v) ethanol
Ethanol
-
the residual activities of Lip5 double mutant remains at 24.32% after incubation for 1 h in 30% (v/v) ethanol
-
Ethanol
-
116.4% activity at 1% (v/v)
Ethanol
-
116.4% activity at 1% (v/v)
-
Ethanol
-
50%, 30 min, 70°C, pH 8.5, loss of 70% activity
Ethanol
-
50%, 30 min, 70°C, pH 8.5, loss of 70% activity
-
Ethanol
-
70%, 30°C, completely stable for 1 h, loss of 30% activity after 2h
Ethanol
-
70%, 30°C, completely stable for 1 h, loss of 30% activity after 2h
-
Ethanol
-
30% (v/v), half-life: less than 1 day, the half-life of the enzyme in absence of organic solvents is 3 days
Ethanol
-
30% (v/v), half-life: less than 1 day, the half-life of the enzyme in absence of organic solvents is 3 days
-
Ethanol
-
complete inactivation at pH 8.0
Ethanol
half-life is 0.20 days
Ethanol
-
at 25% v/v, 30°C, 90% remaining activity after 24 h, 17% after 48 h, 55% remaining activity after 10 min at 50°C
Ethanol
-
half-life is 0.20 days
-
Ethanol
-
inactivates at 45°C
Ethanol
-
inactivates at 45°C
-
Ethanol
-
100% activity at 20% (v/v)
Ethanol
-
100% activity at 20% (v/v)
-
Ethanol
-
18 h at 50% v/v, 91% remaining activity
Ethanol
30°C, 30 min, about 90% remaining activity at 10%, inactivation at 20%
Glycerol
48 h, stable, purified recombinant LipAB, incubation in 50% alcohol/water solution at room temperature
Glycerol
-
50%, 30 min, 70°C, pH 8.5, loss of 60% activity
Glycerol
-
50%, 30 min, 70°C, pH 8.5, loss of 60% activity
-
Glycerol
-
30% (v/v), half-life: 4 days, the half-life of the enzyme in absence of organic solvents is 3 days
Glycerol
-
30% (v/v), half-life: 4 days, the half-life of the enzyme in absence of organic solvents is 3 days
-
Glycerol
half-life is 37 days
Glycerol
-
half-life is 37 days
-
heptane
-
149.6% activity at 1% (v/v)
heptane
-
149.6% activity at 1% (v/v)
-
heptane
-
the recombinant lipase shows stability in the presence of heptane
heptane
-
the recombinant lipase shows stability in the presence of heptane
-
hexane
-
72% activity at 50% (v/v)
hexane
-
139.3% activity at 1% (v/v)
hexane
-
90% residual activity at 100% (v/v)
hexane
-
estrification of lactic acid and alcohols in hexane
hexane
-
82% residual activity at 100% (v/v)
hexane
-
8% inactivation at pH 8.0
hexane
-
at 25% v/v, 30°C, 100% remaining activity after 24 h, 64% after 48 h, 100% reaming activity after 15 min at 60°C, 50% reamining activity after 30 min at 60°C
hexane
the enzyme displays 100% activity in presence of 30% (v/v) n-hexane
hydrogen peroxide
-
the enzyme shows stability in the presence of 30% (w/v) hydrogen peroxide
hydrogen peroxide
-
the enzyme shows stability in the presence of 30% (w/v) hydrogen peroxide
-
isooctane
-
128.6% activity at 1% (v/v)
isooctane
-
30% (v/v), half-life: more than 5 days, the half-life of the enzyme in absence of organic solvents is 3 days
isooctane
-
71% residual activity at 100% (v/v)
isooctane
-
58% residual activity at 100% (v/v)
isooctane
-
9% inactivation at pH 8.0
isopropanol
-
59% activity at 50% (v/v)
isopropanol
-
no activity at 50% (v/v), 83.8% activity at 10% (v/v)
isopropanol
-
no activity at 50% (v/v), 83.8% activity at 10% (v/v)
-
isopropanol
-
relative activity of 62% is apparent in the presence of 1% (v/v) isopropanol
isopropanol
-
relative activity of 62% is apparent in the presence of 1% (v/v) isopropanol
-
isopropanol
48 h, 91.7% remaining activity, purified recombinant LipAB, incubation in 50% alcohol/water solution at room temperature
isopropanol
-
lipase activity is almost lost (4.59% residual activity) in the presence of 30% (v/v) isopropanol
isopropanol
-
lipase activity is almost lost (4.59% residual activity) in the presence of 30% (v/v) isopropanol
-
isopropanol
-
50%, 30 min, 70°C, pH 8.5, loss of 60% activity
isopropanol
-
36% residual activity at 50% (v/v)
isopropanol
-
23% residual activity at 50% (v/v)
isopropanol
-
98% inactivation at pH 8.0
isopropanol
-
at 25% v/v, 30°C, 65% remaining activity after 24 h, 16% after 48 h
isopropanol
-
4 h, completely stable in 80% at 30°C
isopropanol
-
4 h, completely stable in 80% at 30°C
-
isopropanol
30°C, 30 min, about 90% remaining activity at 10%, inactivation at 20%
Methanol
-
64% activity at 50% (v/v)
Methanol
-
0.613% residual activity at 50% (v/v), 108% activity at 10% (v/v)
Methanol
-
0.613% residual activity at 50% (v/v), 108% activity at 10% (v/v)
-
Methanol
-
1 h, pH 7.0, 37°C, the mycelium-bound and constitutive enzymes are very stable in presence of methanol
Methanol
-
relative activity of 71% is apparent in the presence of 1% (v/v) methanol
Methanol
-
relative activity of 71% is apparent in the presence of 1% (v/v) methanol
-
Methanol
48 h, 98.34% remaining activity, purified recombinant LipAB, incubation in 50% alcohol/water solution at room temperature
Methanol
-
the residual activities of Lip5 double mutant remains at 48.23% after incubation for 1 h in 30% (v/v) methanol
Methanol
-
the residual activities of Lip5 double mutant remains at 48.23% after incubation for 1 h in 30% (v/v) methanol
-
Methanol
-
107.3% activity at 1% (v/v)
Methanol
-
107.3% activity at 1% (v/v)
-
Methanol
-
50%, 30 min, 70°C, pH 8.5, loss of 20% activity
Methanol
-
50%, 30 min, 70°C, pH 8.5, loss of 20% activity
-
Methanol
-
30% v/v, 1 h, 30°C, 0.1 M Tris buffer, pH 8.0, 16% reduced activity
Methanol
-
30% v/v, 1 h, 30°C, 0.1 M Tris buffer, pH 8.0, 16% reduced activity
-
Methanol
-
70%, 30°C, loss of 35% activity after 2h
Methanol
-
70%, 30°C, loss of 35% activity after 2h
-
Methanol
-
30% (v/v), half-life: 2 days, the half-life of the enzyme in absence of organic solvents is 3 days
Methanol
-
30% (v/v), half-life: 2 days, the half-life of the enzyme in absence of organic solvents is 3 days
-
Methanol
-
complete inhibition at 50% (v/v)
Methanol
not inhibitory at 10% v/v. At 20% v/v, not inhibitory up to 30°C and 57% residual activity at 40°C
Methanol
-
complete inhibition at 50% (v/v)
Methanol
-
complete inactivation at pH 8.0
Methanol
half-life is 0.29 days
Methanol
-
at 25% v/v, 30°C, 80% remaining activity after 24 h, 42% after 48 h, 100% remaining activity after 10 min at 50°C
Methanol
-
half-life is 0.29 days
-
Methanol
-
inactivates at 45°C
Methanol
-
inactivates at 45°C
-
Methanol
-
150% activity at 20% (v/v)
Methanol
-
150% activity at 20% (v/v)
-
Methanol
30°C, 30 min, about 90% remaining activity at 10%, 60% activity at 20%
N,N-dimethylformamide
half-life is 7.9 days
N,N-dimethylformamide
-
18 h at 50% v/v, 4% remaining activity
n-decane
-
75% activity at 50% (v/v)
n-decane
half-life is 0.40 days
n-heptane
-
92% activity at 50% (v/v)
n-heptane
-
enzyme performs the hydrolysis of 4-nitrophenyl palmitate in n-heptane
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
n-heptane
-
103% activity at 100% (v/v)
n-heptane
-
95% residual activity at 100% (v/v)
n-heptane
-
13.6% activation at pH 8.0
n-heptane
half-life is 7.9 days
n-hexane
-
50%, 30 min, 70°C, pH 8.5, loss of 85% activity
n-hexane
-
30% (v/v), half-life: more than 5 days, the half-life of the enzyme in absence of organic solvents is 3 days
n-hexane
half-life is 7.7 days
n-hexane
-
150% activity at 60% (v/v)
Pyridine
-
rapid complete deactivation
Pyridine
-
rapid complete deactivation
-
Pyridine
-
the purified enzyme is stable for over 30 days at 20-55°C in presence of water-miscible organic solvents such as alcohols, glycols, pyridine, acetonitrile, dimethyl formamide, or dimethylsulfoxide
Pyridine
-
the purified enzyme is stable for over 30 days at 20-55°C in presence of water-miscible organic solvents such as alcohols, glycols, pyridine, acetonitrile, dimethyl formamide, or dimethylsulfoxide
-
SDS
-
SDS has little stimulatory effect
SDS
-
SDS has little stimulatory effect
-
SDS
activity is completely lost with SDS
SDS
-
activity is completely lost with SDS
-
tert-Butanol
-
30% (v/v), half-life: 1 day, the half-life of the enzyme in absence of organic solvents is 3 days
tert-Butanol
-
30% (v/v), half-life: 1 day, the half-life of the enzyme in absence of organic solvents is 3 days
-
tert-Butanol
half-life is 0.17 days
tert-Butanol
-
half-life is 0.17 days
-
tetrahydrofuran
-
loss of about 90% activity at 30% v/v after 1 h at 30°C
tetrahydrofuran
-
loss of about 90% activity at 30% v/v after 1 h at 30°C
-
tetrahydrofuran
-
18 h at 50% v/v, no remaining activity, complete inactivation
toluene
-
catalyzes the esterification of sulcatol and fatty acids in toluene
toluene
-
164.9% activity at 1% (v/v)
toluene
-
164.9% activity at 1% (v/v)
-
toluene
-
30% (v/v), half-life: more than 5 days, the half-life of the enzyme in absence of organic solvents is 3 days
toluene
-
17.7% inactivation at pH 8.0
toluene
half-life is 0.37 days
toluene
-
250% activity at 20% (v/v)
toluene
-
250% activity at 20% (v/v)
-
Triton X-100
stable in the presence of the detergent Triton X-100
Triton X-100
-
stimulated in the presence of 0.1% Triton X-100 (110.2% relative activity)
Triton X-100
-
stimulated in the presence of 0.1% Triton X-100 (110.2% relative activity)
-
Triton X-100
free enzyme shows less than 50% loss of activity with 0.1% (v/v) Triton X-100, lipase immobilized in the presence of Triton X-100 shows a total loss of activity after 9 cycles of reuse, retaining 53% of its initial activity after seven cycles, while the immobilized lipase without Triton X-100 loses all of its activity after 12 cycles, retaining 69% of its initial activity after 7 cycles
Triton X-100
-
free enzyme shows less than 50% loss of activity with 0.1% (v/v) Triton X-100, lipase immobilized in the presence of Triton X-100 shows a total loss of activity after 9 cycles of reuse, retaining 53% of its initial activity after seven cycles, while the immobilized lipase without Triton X-100 loses all of its activity after 12 cycles, retaining 69% of its initial activity after 7 cycles
-
Tween 80
less than 50% loss of activity with 0.1% (v/v) Tween 80
Tween 80
-
less than 50% loss of activity with 0.1% (v/v) Tween 80
-
Tween 80
-
124% relative activity after 5 h at 25% (v/v)
Tween 80
-
124% relative activity after 5 h at 25% (v/v)
-
additional information
-
the enzyme is only very slightly affected by isopropanol and acetone
additional information
-
slight decrease in activity in the presence of commercial detergents
additional information
-
slight decrease in activity in the presence of commercial detergents
-
additional information
-
the enzyme is only very slightly affected by isopropanol and acetone
-
additional information
-
the enzyme is highly active in presence of many different organic solvents, overview
additional information
-
commercial detergents enhance the enzyme activity, the enzyme retains 60% or more activity in presence of commercial detergents
additional information
-
commercial detergents enhance the enzyme activity, the enzyme retains 60% or more activity in presence of commercial detergents
-
additional information
the purified enzyme is stable to organic solvents with the exception of pyridine, which inhibits 25-30% of the activity, overview
additional information
-
the purified enzyme is stable to organic solvents with the exception of pyridine, which inhibits 25-30% of the activity, overview
additional information
-
BTID-B is strongly resistant to organic solvents
additional information
-
BTID-B is strongly resistant to organic solvents
-
additional information
strain LST-03 is organic solvent-tolerant, overview
additional information
-
strain LST-03 is organic solvent-tolerant, overview
additional information
-
the purified enzyme is stable for over 30 days at 20-55°C in presence of water-miscible organic solvents such as alcohols, glycols, pyridine, acetonitrile, dimethyl formamide, or dimethylsulfoxide
additional information
-
lipases maintain activity and selectivity in organic solvents
additional information
-
the enzyme activity is not significantly affected by dimethylsulfonyloxide, isopropanol, ethanol, methanol, benzene, toluene, xylene, cyclohexane, hexane, n-heptane, isooctane, decane, and tetradecane
additional information
-
strain LST-03 is organic solvent-tolerant, overview
-
additional information
-
lipases maintain activity and selectivity in organic solvents
-
additional information
-
the enzyme activity is not significantly affected by dimethylsulfonyloxide, isopropanol, ethanol, methanol, benzene, toluene, xylene, cyclohexane, hexane, n-heptane, isooctane, decane, and tetradecane
-
additional information
-
the purified enzyme is stable for over 30 days at 20-55°C in presence of water-miscible organic solvents such as alcohols, glycols, pyridine, acetonitrile, dimethyl formamide, or dimethylsulfoxide
-
additional information
-
the enzyme shows good stability in water-miscible and immiscible solvents, overview
additional information
-
the enzyme shows good stability in water-miscible and immiscible solvents, overview
-
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medicine
the enzyme can be used in enzyme replacement therapy treating pancreatic exocrine insufficiency
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
biofuel production
-
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel
biofuel production
-
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel
biofuel production
-
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel
biofuel production
-
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel
biofuel production
-
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel
biofuel production
-
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel
biofuel production
-
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel
biofuel production
-
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel
biofuel production
-
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel
biofuel production
-
Candida rugosa lipase immobilized on hydrous niobium oxide to be used in the biodiesel synthesis
biofuel production
-
lipase catalyzes biodiesel production using soybean oil and ethanol as substrates and pressurized n-propane as solvent
biofuel production
-
LP326 catalyzes biodiesel production using methanol and various oils
biofuel production
-
biodiesel production
biofuel production
-
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel
-
biofuel production
-
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel
-
biofuel production
-
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel
-
biofuel production
-
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel
-
biofuel production
-
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel
-
biofuel production
-
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel
-
biofuel production
-
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel
-
biofuel production
-
LP326 catalyzes biodiesel production using methanol and various oils
-
biofuel production
-
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel
-
biofuel production
-
conversion of degummed soybean oil to biodiesel fuel, synthesis of lipase-catalyzed biodiesel
-
biofuel production
-
biodiesel production
-
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
biotechnology
-
the alkaline lipase is stable and active in organic solvents and a water-restricted environment and has a great potential as a biotechnological tool e.g. in organosynthetic reactions in water-restricted medium or in control and prevention of metalworking fluid putrification in the metal industry
biotechnology
-
biocatalytic surfactant production, for example the synthesis of myristyl myristate.
detergent
-
strain M1, enzyme is used for removal of fatty stains under conditions of a modern machine wash and in alkaline environment
detergent
-
the enzyme is usable with laundry detergents
detergent
-
detergents and cold water washing, production of alpha-butylglucoside lactate by transesterification for cosmetics
detergent
-
detergents and cold water washing, production of alpha-butylglucoside lactate by transesterification for cosmetics
detergent
-
detergents and cold water washing, production of alpha-butylglucoside lactate by transesterification for cosmetics
detergent
-
detergents and cold water washing, production of alpha-butylglucoside lactate by transesterification for cosmetics
detergent
-
detergents and cold water washing, production of alpha-butylglucoside lactate by transesterification for cosmetics
detergent
-
detergents and cold water washing, production of alpha-butylglucoside lactate by transesterification for cosmetics
detergent
-
detergents and cold water washing, production of alpha-butylglucoside lactate by transesterification for cosmetics
detergent
-
detergents and cold water washing, production of alpha-butylglucoside lactate by transesterification for cosmetics
detergent
-
detergents and cold water washing, production of alpha-butylglucoside lactate by transesterification for cosmetics
detergent
-
the enzyme is usable with laundry detergents
-
detergent
-
detergents and cold water washing, production of alpha-butylglucoside lactate by transesterification for cosmetics
-
detergent
-
detergents and cold water washing, production of alpha-butylglucoside lactate by transesterification for cosmetics
-
detergent
-
detergents and cold water washing, production of alpha-butylglucoside lactate by transesterification for cosmetics
-
detergent
-
detergents and cold water washing, production of alpha-butylglucoside lactate by transesterification for cosmetics
-
detergent
-
detergents and cold water washing, production of alpha-butylglucoside lactate by transesterification for cosmetics
-
detergent
-
detergents and cold water washing, production of alpha-butylglucoside lactate by transesterification for cosmetics
-
detergent
-
detergents and cold water washing, production of alpha-butylglucoside lactate by transesterification for cosmetics
-
detergent
-
detergents and cold water washing, production of alpha-butylglucoside lactate by transesterification for cosmetics
-
detergent
-
detergents and cold water washing, production of alpha-butylglucoside lactate by transesterification for cosmetics
-
environmental protection
-
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids
environmental protection
-
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids
environmental protection
-
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids
environmental protection
-
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids
environmental protection
-
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids
environmental protection
-
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids
environmental protection
-
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids
environmental protection
-
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids
environmental protection
-
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids
environmental protection
-
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids
-
environmental protection
-
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids
-
environmental protection
-
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids
-
environmental protection
-
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids
-
environmental protection
-
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids
-
environmental protection
-
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids
-
environmental protection
-
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids
-
environmental protection
-
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids
-
environmental protection
-
degradation of lipid wastes, bioremediation and bioaugumentation, removal of solid and water pollution by hydrocarbons, oils and lipids
-
food industry
-
protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats
food industry
-
protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats
food industry
-
protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats
food industry
-
protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats
food industry
-
protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats
food industry
-
protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats
food industry
-
protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats
food industry
-
protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats
food industry
-
protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats
food industry
-
protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats
-
food industry
-
protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats
-
food industry
-
protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats
-
food industry
-
protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats
-
food industry
-
protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats
-
food industry
-
protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats
-
food industry
-
protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats
-
food industry
-
protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats
-
food industry
-
protein polymerization and gelling in fish, improvement in food texture, flavor modification, production of fatty acids and interestrification of fats
-
synthesis
-
immobilized enzyme catalyzes the esterification of oleic acid with butanol dissolved in hexane
synthesis
-
enantioselective hydrolysis of chiral esters
synthesis
-
immobilized enzyme is used for the transesterification reaction that replaces pamitic acid in palm oil with stearic acid
synthesis
-
possible industrial application of the enzyme in continuous processes due to effective immobilization on diverse materials, overview
synthesis
-
synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
synthesis
-
synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
synthesis
-
synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
synthesis
-
synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
synthesis
-
synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
synthesis
-
synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
synthesis
-
synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
synthesis
-
synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
synthesis
-
synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
synthesis
-
synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
synthesis
-
synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
synthesis
-
synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
synthesis
-
synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
synthesis
-
synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
synthesis
-
synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
synthesis
-
synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
synthesis
Penicillium wortmanii
-
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 performs chemically selective hydrolysis, synthesis of optically active substances from achiral or racemic compounds
synthesis
-
useful in application to the processing of industrial fats and oils containing eicosapentanoic acid and docosahexaenoic acid, such as fish oil splitting
synthesis
-
production of (-)-4-endo-hydroxy-2-oxabicyclo[3.3.0]oct-7-en-3-one, which is an intermediate for the anti-HIV agent carbovir
synthesis
-
production of (2R,3S)-3-(4-methoxyphenyl)glycidic acid methyl ester, which is an intermediate in the synthesis of diltiazem. diltiazem hydrochloride is a coronary vasodilator and a calcium channel blocker
synthesis
-
production of (3R,4S)-cis-azetidinone acetate, which is an intermediate for the synthesis of paclitaxel
synthesis
-
production of (S)-1-phenylethylamine and (R)-phenylethylmethoxyamide, which are intermediates for pharmaceuticals and pesticides and can also be used as chiral synthons in asymmetric synthesis
synthesis
-
production of (S)-acetic acid 2-methyl-4-oxo-3-prop-2-ynyl-cyclopent-2-enyl ester, which is used as an intermediate in the synthesis of pyrethroids, which are used as insecticides. They show excellent insecticidal activities and a low toxicity in mammals.
synthesis
-
production of (S)-acetic acid 4-(2,4-difluoro-phenyl)-2-hydroxymethyl-pent-4-enyl ester, which is used as an improved azole antifungal. It shows activity against systemic Candida and pulmonary Aspergillus infections
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
Candida cyclindraceae
-
production of Ibuprofen, which is an important nonsteroidal antiinflammatory drug
synthesis
-
production of isopropyl palmitate, which is used in the preparation of soaps, skin creams, lubricants and grease
synthesis
-
production of [4-[4a,6b(E)]]-6-[4,4-bis(4-fluorophenyl)-3-(1-methyl-1H-tetrazol-5-yl)-1,3-butadienyl]-tetrahydro-4-hydroxy-2H-pyran-2-one acetate, which is a hydroxymethyl glutaryl coenzyme A (HMG-CoA) reductase inhibitor and a potential anticholesterol drug candidate
synthesis
-
construction of an overexpressing Aspergillus oryzae strain immobilized on supporting particles for enantioselective transesterification reaction
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
synthesis
application of the immobilized lipase in non-conventional biocatalysis for the synthesis of surfactants and biodiesel, overview
synthesis
-
the enantioselective lipase shows potential to be used as a catalyst to prepare optically pure pharmaceuticals
synthesis
the enzyme shows potential in the production of optically pure ibuprofen
synthesis
-
lipases constitute one of the most important groups of biocatalysts due to their ability to catalyze three different kinds of reactions viz. hydrolysis, esterification, and transesterification with unique chemo-, regio-, and enantiospecific selectivity. Lipase-based processes are employed for oil/fat processing, synthesis of industrially important oleochemicals, enantiopure pharmaceuticals, agrochemicals, flavor esters, structured lipids, and biodiesel production
synthesis
-
lipases maintain activity and selectivity in organic solvents, which has enabled their wide use as biocatalysts finding applications in food, dairy, detergent, and pharmaceutical industries
synthesis
-
synthesis of arylaliphatic glycolipids, ethyl esterification of docosahexaenoic acid to ethyl docosahexaenoate, synthesis of citronellol laurate from citronellol and lauric acid, optically active ester synthesis, ester synthesis, desymmetrization and production of peracids, organic synthesis of chiral intermediates, synthesis of butyl caprylate in n-heptane, synthesis of butyl lactate by transesterification, synthesis of amide
synthesis
-
synthesis of arylaliphatic glycolipids, ethyl esterification of docosahexaenoic acid to ethyl docosahexaenoate, synthesis of citronellol laurate from citronellol and lauric acid, optically active ester synthesis, ester synthesis, desymmetrization and production of peracids, organic synthesis of chiral intermediates, synthesis of butyl caprylate in n-heptane, synthesis of butyl lactate by transesterification, synthesis of amide
synthesis
-
synthesis of arylaliphatic glycolipids, ethyl esterification of docosahexaenoic acid to ethyl docosahexaenoate, synthesis of citronellol laurate from citronellol and lauric acid, optically active ester synthesis, ester synthesis, desymmetrization and production of peracids, organic synthesis of chiral intermediates, synthesis of butyl caprylate in n-heptane, synthesis of butyl lactate by transesterification, synthesis of amide
synthesis
-
synthesis of arylaliphatic glycolipids, ethyl esterification of docosahexaenoic acid to ethyl docosahexaenoate, synthesis of citronellol laurate from citronellol and lauric acid, optically active ester synthesis, ester synthesis, desymmetrization and production of peracids, organic synthesis of chiral intermediates, synthesis of butyl caprylate in n-heptane, synthesis of butyl lactate by transesterification, synthesis of amide
synthesis
-
synthesis of arylaliphatic glycolipids, ethyl esterification of docosahexaenoic acid to ethyl docosahexaenoate, synthesis of citronellol laurate from citronellol and lauric acid, optically active ester synthesis, ester synthesis, desymmetrization and production of peracids, organic synthesis of chiral intermediates, synthesis of butyl caprylate in n-heptane, synthesis of butyl lactate by transesterification, synthesis of amide
synthesis
-
synthesis of arylaliphatic glycolipids, ethyl esterification of docosahexaenoic acid to ethyl docosahexaenoate, synthesis of citronellol laurate from citronellol and lauric acid, optically active ester synthesis, ester synthesis, desymmetrization and production of peracids, organic synthesis of chiral intermediates, synthesis of butyl caprylate in n-heptane, synthesis of butyl lactate by transesterification, synthesis of amide
synthesis
-
synthesis of arylaliphatic glycolipids, ethyl esterification of docosahexaenoic acid to ethyl docosahexaenoate, synthesis of citronellol laurate from citronellol and lauric acid, optically active ester synthesis, ester synthesis, desymmetrization and production of peracids, organic synthesis of chiral intermediates, synthesis of butyl caprylate in n-heptane, synthesis of butyl lactate by transesterification, synthesis of amide
synthesis
-
synthesis of arylaliphatic glycolipids, ethyl esterification of docosahexaenoic acid to ethyl docosahexaenoate, synthesis of citronellol laurate from citronellol and lauric acid, optically active ester synthesis, ester synthesis, desymmetrization and production of peracids, organic synthesis of chiral intermediates, synthesis of butyl caprylate in n-heptane, synthesis of butyl lactate by transesterification, synthesis of amide
synthesis
-
synthesis of arylaliphatic glycolipids, ethyl esterification of docosahexaenoic acid to ethyl docosahexaenoate, synthesis of citronellol laurate from citronellol and lauric acid, optically active ester synthesis, ester synthesis, desymmetrization and production of peracids, organic synthesis of chiral intermediates, synthesis of butyl caprylate in n-heptane, synthesis of butyl lactate by transesterification, synthesis of amide
synthesis
-
the highly enantioselective lipase from Serratia marcescens ECU1010 is a robust biocatalyst for practical use in large-scale production of diltiazem intermediate
synthesis
-
the lipase from Rhizomucor miehei may be used as a means to prepare fatty acid concentrates rich in docosahexaenoic acid
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
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 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 biodiesel from canola oil. Complete conversion to fatty acid methyl esters is achieved using the enzyme immobilized on epoxy-functionalized silica, 30% (w/w) tert-butanol by substrate weight, reaction time of 96 h, 50°C and molar ratio of methanol to oil 3:1, which is added to the reaction mixture in three steps. Water suppresses the methanolysis reaction. 85% residual activity after 16 reaction cycles
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
-
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
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
synthesis
-
the enantioselective lipase shows potential to be used as a catalyst to prepare optically pure pharmaceuticals
-
synthesis
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synthesis of arylaliphatic glycolipids, ethyl esterification of docosahexaenoic acid to ethyl docosahexaenoate, synthesis of citronellol laurate from citronellol and lauric acid, optically active ester synthesis, ester synthesis, desymmetrization and production of peracids, organic synthesis of chiral intermediates, synthesis of butyl caprylate in n-heptane, synthesis of butyl lactate by transesterification, synthesis of amide
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synthesis
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synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
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synthesis
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synthesis of arylaliphatic glycolipids, ethyl esterification of docosahexaenoic acid to ethyl docosahexaenoate, synthesis of citronellol laurate from citronellol and lauric acid, optically active ester synthesis, ester synthesis, desymmetrization and production of peracids, organic synthesis of chiral intermediates, synthesis of butyl caprylate in n-heptane, synthesis of butyl lactate by transesterification, synthesis of amide
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synthesis
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the enzyme performs chemically selective hydrolysis, synthesis of optically active substances from achiral or racemic compounds
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synthesis
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synthesis of arylaliphatic glycolipids, ethyl esterification of docosahexaenoic acid to ethyl docosahexaenoate, synthesis of citronellol laurate from citronellol and lauric acid, optically active ester synthesis, ester synthesis, desymmetrization and production of peracids, organic synthesis of chiral intermediates, synthesis of butyl caprylate in n-heptane, synthesis of butyl lactate by transesterification, synthesis of amide
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synthesis
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synthesis of arylaliphatic glycolipids, ethyl esterification of docosahexaenoic acid to ethyl docosahexaenoate, synthesis of citronellol laurate from citronellol and lauric acid, optically active ester synthesis, ester synthesis, desymmetrization and production of peracids, organic synthesis of chiral intermediates, synthesis of butyl caprylate in n-heptane, synthesis of butyl lactate by transesterification, synthesis of amide
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synthesis
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synthesis of arylaliphatic glycolipids, ethyl esterification of docosahexaenoic acid to ethyl docosahexaenoate, synthesis of citronellol laurate from citronellol and lauric acid, optically active ester synthesis, ester synthesis, desymmetrization and production of peracids, organic synthesis of chiral intermediates, synthesis of butyl caprylate in n-heptane, synthesis of butyl lactate by transesterification, synthesis of amide
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synthesis
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synthesis of arylaliphatic glycolipids, ethyl esterification of docosahexaenoic acid to ethyl docosahexaenoate, synthesis of citronellol laurate from citronellol and lauric acid, optically active ester synthesis, ester synthesis, desymmetrization and production of peracids, organic synthesis of chiral intermediates, synthesis of butyl caprylate in n-heptane, synthesis of butyl lactate by transesterification, synthesis of amide
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synthesis
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synthesis of arylaliphatic glycolipids, ethyl esterification of docosahexaenoic acid to ethyl docosahexaenoate, synthesis of citronellol laurate from citronellol and lauric acid, optically active ester synthesis, ester synthesis, desymmetrization and production of peracids, organic synthesis of chiral intermediates, synthesis of butyl caprylate in n-heptane, synthesis of butyl lactate by transesterification, synthesis of amide
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synthesis
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synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
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synthesis
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synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
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synthesis
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synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
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synthesis
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synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications
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synthesis
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possible industrial application of the enzyme in continuous processes due to effective immobilization on diverse materials, overview
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synthesis
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synthesis of arylaliphatic glycolipids, ethyl esterification of docosahexaenoic acid to ethyl docosahexaenoate, synthesis of citronellol laurate from citronellol and lauric acid, optically active ester synthesis, ester synthesis, desymmetrization and production of peracids, organic synthesis of chiral intermediates, synthesis of butyl caprylate in n-heptane, synthesis of butyl lactate by transesterification, synthesis of amide
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synthesis
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useful in application to the processing of industrial fats and oils containing eicosapentanoic acid and docosahexaenoic acid, such as fish oil splitting
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synthesis
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production of (2R,3S)-3-(4-methoxyphenyl)glycidic acid methyl ester, which is an intermediate in the synthesis of diltiazem. diltiazem hydrochloride is a coronary vasodilator and a calcium channel blocker
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synthesis
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lipases maintain activity and selectivity in organic solvents, which has enabled their wide use as biocatalysts finding applications in food, dairy, detergent, and pharmaceutical industries
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synthesis
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synthesis of arylaliphatic glycolipids, ethyl esterification of docosahexaenoic acid to ethyl docosahexaenoate, synthesis of citronellol laurate from citronellol and lauric acid, optically active ester synthesis, ester synthesis, desymmetrization and production of peracids, organic synthesis of chiral intermediates, synthesis of butyl caprylate in n-heptane, synthesis of butyl lactate by transesterification, synthesis of amide
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synthesis
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the highly enantioselective lipase from Serratia marcescens ECU1010 is a robust biocatalyst for practical use in large-scale production of diltiazem intermediate
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synthesis
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the enzyme shows potential in the production of optically pure ibuprofen
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additional information
codon optimization for improved expression of LIP1 in Pichia pastoris for uuse of the enzyme in industrial processes
additional information
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codon optimization for improved expression of LIP1 in Pichia pastoris for uuse of the enzyme in industrial processes
additional information
LipB68 acts as biocatalysts in biodiesel production and produces biodiesel with a yield of 92% after 12 h, at the lowest temperature of 20°C, catalyzing the transesterification reaction of biodiesel production, thus LipB68 represents a highly competitive energy-saving biocatalyst
additional information
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LipB68 acts as biocatalysts in biodiesel production and produces biodiesel with a yield of 92% after 12 h, at the lowest temperature of 20°C, catalyzing the transesterification reaction of biodiesel production, thus LipB68 represents a highly competitive energy-saving biocatalyst
additional information
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the galactolipase/triacylglycerol lipase ratio can be used to classify phytophagy in lepidopterans
additional information
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the galactolipase/triacylglycerol lipase ratio can be used to classify phytophagy in lepidopterans
additional information
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the galactolipase/triacylglycerol lipase ratio can be used to classify phytophagy in lepidopterans
additional information
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the galactolipase/triacylglycerol lipase ratio can be used to classify phytophagy in lepidopterans
additional information
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the galactolipase/triacylglycerol lipase ratio can be used to classify phytophagy in lepidopterans
additional information
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the galactolipase/triacylglycerol lipase ratio can be used to classify phytophagy in lepidopterans
additional information
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LipB68 acts as biocatalysts in biodiesel production and produces biodiesel with a yield of 92% after 12 h, at the lowest temperature of 20°C, catalyzing the transesterification reaction of biodiesel production, thus LipB68 represents a highly competitive energy-saving biocatalyst
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