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Literature summary for 3.1.1.3 extracted from

  • Sharma, R.; Chisti, Y.; Banerjee, U.C.
    Production, purification, characterization, and applications of lipases (2001), Biotechnol. Adv., 19, 627-662.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
castor oil at 2% as carbon source, enhances the enzyme production in vivo, pH 6.9 Pseudomonas aeruginosa
additional information enzyme is not affected by benzamidine and PMSF Rhizopus arrhizus
additional information the lipase of strain F-111 is unaffected by various detergents Pseudomonas alcaligenes
Triton X-100 activation, strain F-111 Pseudomonas aeruginosa
Triton X-100 enhances the enzyme production in vivo by 50fold compared to olive oil alone in the medium Rhizomucor miehei
Tween 80 activation, strain F-111 Pseudomonas aeruginosa
yeast extract increases growth and enzyme production rate at 50°C, strain -12 Bacillus sp. (in: Bacteria)

Application

Application Comment Organism
detergent strain M1, enzyme is used for removal of fatty stains under conditions of a modern machine wash and in alkaline environment Pseudomonas alcaligenes
paper production removal of pitch, i.e. triglycerides and waxes, from the pulp produced for paper making Diutina rugosa
synthesis enantioselective hydrolysis of chiral esters Pseudomonas aeruginosa
synthesis immobilized enzyme is used for the transesterification reaction that replaces pamitic acid in palm oil with stearic acid Rhizomucor miehei
synthesis synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications Geobacillus stearothermophilus
synthesis synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications Aspergillus niger
synthesis synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications Pseudomonas sp.
synthesis synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications Acinetobacter calcoaceticus
synthesis synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications Proteus vulgaris
synthesis synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications Rhodotorula glutinis
synthesis synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications Staphylococcus epidermidis
synthesis synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications Rhizopus arrhizus
synthesis synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications Bacillus sp. (in: Bacteria)
synthesis synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications Burkholderia cepacia
synthesis synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications Aspergillus oryzae
synthesis synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications Penicillium roqueforti
synthesis synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications Diutina rugosa
synthesis synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications Moesziomyces antarcticus
synthesis synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications Hyphopichia burtonii
synthesis synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications Burkholderia sp.
synthesis synthesis of enantiopure compounds by chemo-, regio-, and stereoselective transformations, catalysation of hydrolysis of water-immiscible triglycerides at water-liquid interface, transesterifications Penicillium wortmanii

Cloned(Commentary)

Cloned (Comment) Organism
expression in Saccharomyces cerevisiae, mature enzyme encoded by gene geh SE1 is overexpressed in Escherichia coli as N-terminally HIs-tagged enzyme Staphylococcus epidermidis
gene tglA, enzyme form L3, DNA and amino acid sequence determination and analysis, functional expressionin Escherichia coli, Aspergillus oryzae is used as a host for expression of Thermomyces lanuginosus Aspergillus oryzae
isozyme gene lip1, synthetically synthesized in an optimized nucleotide sequence to avoid the interference that occurs in heterologous expression of the native gene due to unusual codon usage, functional overexpression in Pichia pastoris of the synthetic gene, expression in Candida maltosa, a related yeast with the same codon usage, secretion in active form to the culture medium Diutina rugosa
strain DSM 853, cloning and epitope mapping Rhizopus arrhizus
strain IGB83, cloning and functional expression in Xanthomonas campestris, secretion of the recombinant enzyme to the medium, expression of the enzyme also in Escherichia coli as His-tagged protein, secretion to the medium Pseudomonas aeruginosa
strain M1, DNA sequencing and analysis, for functional expression in Escherichia coli the coexpression of a lipase-specific foldase, encoded by lipH, is required to ensure the correct folding and secretion of the recombinant enzyme through the host membrane Pseudomonas alcaligenes

Protein Variants

Protein Variants Comment Organism
additional information enzyme can be immobilized on Amberlite IRC50 with good long-term stability and high adsorption capacity Rhizopus arrhizus
additional information immobilization of lipase B on Sepharose, alumina, silica, for the latter using precursors Si(OCH3)3 or Si(OCH3)4, providing a highly active, chemically and thermally stable, heterogeneous biocatalyst Moesziomyces antarcticus

Inhibitors

Inhibitors Comment Organism Structure
Ag+
-
Penicillium roqueforti
Cd2+ strain KKA-5, slight inhibition Pseudomonas aeruginosa
Cu2+ strain KKA-5, slight inhibition Pseudomonas aeruginosa
Cu2+ strong inhibition Rhizopus arrhizus
Fe2+
-
Penicillium roqueforti
Fe2+ strain KKA-5, strong inhibition Pseudomonas aeruginosa
Fe2+ strong inhibition Rhizopus arrhizus
Fe3+ strain KKA-5, strong inhibition Pseudomonas aeruginosa
Fe3+ 60% inhibition at 1 mM Pseudomonas oleovorans
Fe3+ strong inhibition Rhizopus arrhizus
Hg2+
-
Penicillium roqueforti
Hg2+ strain KKA-5, strong inhibition Pseudomonas aeruginosa
Hg2+ strong inhibition Rhizopus arrhizus
isopropyl fluorophosphate
-
Penicillium roqueforti
Mn2+ strain KKA-5, slight inhibition Pseudomonas aeruginosa
additional information enzyme from strain A30-1 is stable to alkaline protease treatment Bacillus sp. (in: Bacteria)
additional information no inhibition by Ca2+, Mg2+, Mn2+, Na+, K+, Cu2+, EDTA, p-chloromercuribenzoate, and iodoacetate Penicillium roqueforti
additional information strain KKA-5, no inhibition by Ca2+ and Mg2+ Pseudomonas aeruginosa
additional information the lipase of strain F-111 is unaffected by various detergents Pseudomonas alcaligenes
additional information no inhibition by Ca2+, Hg2+, Zn2+, Mn2+, Cu2+, Mg2+, Co2+, Cd2+, Pb2+, EDTA, and o-phenanthrolin Pseudomonas oleovorans
additional information enzyme is not affected by benzamidine and PMSF Rhizopus arrhizus
oleic acid inhibits enzyme production, product inhibition Diutina rugosa
SDS strain F-111 Pseudomonas aeruginosa
Zn2+ strain KKA-5, strong inhibition, strain MB5001: 94% inhibition at 1 mM Pseudomonas aeruginosa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.7
-
4-nitrophenyl laurate
-
Rhodotorula glutinis
2.7
-
4-nitrophenyl butyrate
-
Rhodotorula glutinis
12
-
4-nitrophenyl palmitate
-
Burkholderia cepacia

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Pseudomonas sp.
-
-
extracellular
-
Proteus vulgaris
-
-
extracellular
-
Pseudomonas oleovorans
-
-
extracellular especially in a lypolytic strain Rhizopus arrhizus
-
-
extracellular L1, L2, and L3 Aspergillus oryzae
-
-
extracellular strain F-111 Pseudomonas alcaligenes
-
-
extracellular strain KKA-5, strain MB5001, strain IGB83 Pseudomonas aeruginosa
-
-
intracellular
-
Rhizopus arrhizus 5622
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ba2+ activation, extracellular enzyme Bacillus sp. (in: Bacteria)
Ca2+ required Acinetobacter calcoaceticus
Ca2+ activation, extracellular enzyme Bacillus sp. (in: Bacteria)
Ca2+ increases enzyme expression Bacillus sp. (in: Bacteria)
Ca2+ native enzyme, required for activity Staphylococcus epidermidis
CaCl2 1.24fold stimulation at 1 mM Pseudomonas aeruginosa
Co2+ required Acinetobacter calcoaceticus
Cu2+ required Acinetobacter calcoaceticus
Iron increases enzyme expression Bacillus sp. (in: Bacteria)
Mg2+ required Acinetobacter calcoaceticus
Mg2+ enhances enzyme expression Aspergillus niger
Mg2+ increases enzyme expression Bacillus sp. (in: Bacteria)
Mg2+ required for strain F-111 and KKA-5, maximal enzyme production of strain KKA-5 at 0.8 M Mg2+ Pseudomonas oleovorans
additional information Ca2+-concentration does not affect the enzyme production Pseudomonas oleovorans
additional information strain A30-1 requires a complexed medium which must contains diverse metal ions, overview Bacillus sp. (in: Bacteria)
Na+ activation, extracellular enzyme Bacillus sp. (in: Bacteria)
taurocholic acid 1.6fold stimulation at 200 mM Pseudomonas aeruginosa
Tween 80 increases growth and enzyme production rate at 50°C, strain -12 Bacillus sp. (in: Bacteria)

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
24000
-
enzyme form L1 Aspergillus oryzae
25000
-
x * 25000, SDS-PAGE Penicillium roqueforti
29000
-
x * 29000, enzyme of strain MB5001, SDS-PAGE, x * 32000, enzyme from strain F-111, SDS-PAGE, x * 30000, enzyme of strain KKA-5, SDS-PAGE Pseudomonas aeruginosa
30000
-
x * 29000, enzyme of strain MB5001, SDS-PAGE, x * 32000, enzyme from strain F-111, SDS-PAGE, x * 30000, enzyme of strain KKA-5, SDS-PAGE Pseudomonas aeruginosa
30000
-
x * 33000, enzyme from strain KM1-56, SDS-PAGE, x * 30000, extracellular enzyme, SDS-PAGE Pseudomonas sp.
31000
-
1 * 31000, SDS-PAGE Proteus vulgaris
32000
-
extracellular enzyme, gel filtration Rhizopus arrhizus
32000
-
x * 29000, enzyme of strain MB5001, SDS-PAGE, x * 32000, enzyme from strain F-111, SDS-PAGE, x * 30000, enzyme of strain KKA-5, SDS-PAGE Pseudomonas aeruginosa
32000
-
x * 32000, strain BD 413, SDS-PAGE Acinetobacter calcoaceticus
33000
-
x * 33000, enzyme from strain KM1-56, SDS-PAGE, x * 30000, extracellular enzyme, SDS-PAGE Pseudomonas sp.
35000
-
1 * 35000 + 1 * 46000, recombinant enzyme, SDS-PAGE Staphylococcus epidermidis
45000
-
1 * 45000, strain J33 Bacillus sp. (in: Bacteria)
46000
-
1 * 35000 + 1 * 46000, recombinant enzyme, SDS-PAGE Staphylococcus epidermidis
51000
-
gel filtration Hyphopichia burtonii
80000 90000 recombinant enzyme, gel filtration and native PAGE Staphylococcus epidermidis

Organic Solvent Stability

Organic Solvent Comment Organism
1,1,1-trichloroethane enzyme catalyzes the regioselective hydrolysis of preacetylated monosaccharide derivatives in Aspergillus niger
hexane estrification of lactic acid and alcohols in hexane Moesziomyces antarcticus
n-heptane enzyme performs the hydrolysis of 4-nitrophenyl palmitate in n-heptane Burkholderia cepacia
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 Diutina rugosa
toluene catalyzes the esterification of sulcatol and fatty acids in toluene Diutina rugosa

Organism

Organism UniProt Comment Textmining
Acinetobacter calcoaceticus
-
-
-
Acinetobacter calcoaceticus BD 413
-
-
-
Aspergillus niger
-
-
-
Aspergillus oryzae
-
2 enzyme forms L1, L2, and L3
-
Bacillus sp. (in: Bacteria)
-
-
-
Bacillus sp. (in: Bacteria) J33
-
-
-
Burkholderia cepacia
-
-
-
Burkholderia sp.
-
-
-
Diutina rugosa
-
dimorphic yeast, several lipase isoforms encoded by the lip1 gene family
-
Geobacillus stearothermophilus
-
L1
-
Geobacillus stearothermophilus L1
-
L1
-
Hyphopichia burtonii
-
-
-
Moesziomyces antarcticus
-
multiple enzyme forms
-
Penicillium roqueforti
-
-
-
Penicillium roqueforti IAM7268
-
-
-
Penicillium wortmanii
-
-
-
Proteus vulgaris
-
highly alkaline enzyme
-
Pseudomonas aeruginosa
-
strain KKA-5, strain MB5001
-
Pseudomonas alcaligenes
-
strain M1, strain F-111
-
Pseudomonas oleovorans
-
strain F-111, strain KKA-5
-
Pseudomonas sp.
-
-
-
Pseudomonas sp. KM1-56
-
-
-
Rhizomucor miehei
-
-
-
Rhizopus arrhizus
-
lipolytic strain
-
Rhodotorula glutinis
-
-
-
Staphylococcus epidermidis
-
strain RP 62A, strain 9
-

Oxidation Stability

Oxidation Stability Organism
enzyme from strain A30-1 is stable to H2O2 Bacillus sp. (in: Bacteria)

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information strain 9 contains an enzyme which is organized as a preproenzyme Staphylococcus epidermidis

Purification (Commentary)

Purification (Comment) Organism
-
Proteus vulgaris
enzyme form L1, to homogeneity Aspergillus oryzae
extracellular enzyme, 1200fold Rhizopus arrhizus
from strain KW1-56: 13.9fold, extracellular enzyme: 37fold to homogeneity Pseudomonas sp.
from strain MB5001 in a 3-step procedure, from strain F-111 to homogeneity, 518fold from strain KKA-5 to homogeneity Pseudomonas aeruginosa
native enzyme to homogeneity, recombinant enzyme rROL from Saccharomyces cerevisiae, recombinant His-tagged mature enzyme Staphylococcus epidermidis
partial from strain A30-1, 175fold from strain J33 Bacillus sp. (in: Bacteria)
strain BD413, to homogeneity Acinetobacter calcoaceticus
to homogeneity Penicillium roqueforti
to homogeneity Hyphopichia burtonii

Reaction

Reaction Comment Organism Reaction ID
triacylglycerol + H2O = diacylglycerol + a carboxylate enzyme contains the conserved pentapeptide Ala-Xaa-Ser-Xaa-Gly Bacillus sp. (in: Bacteria)
triacylglycerol + H2O = diacylglycerol + a carboxylate enzyme form L3: catalytic triad is formed by conserved Ser, His and Asp residues Aspergillus oryzae

Source Tissue

Source Tissue Comment Organism Textmining
cell culture batch or fed-batch culture in a medium containing citric acid and soybean oil as substrates Pseudomonas alcaligenes
-
cell culture enzyme production in presence of 1% olive oil or corn oil in the culture medium Bacillus sp. (in: Bacteria)
-
cell culture submerged batch culture Diutina rugosa
-
additional information culture conditions, the extracellular enzyme is dependent on a special nitrogen source in the medium, e.g. peptone, while the intracellular enzyme form is not Rhizopus arrhizus
-
additional information high enzyme production Penicillium wortmanii
-
additional information medium conditions for the cell culture Pseudomonas aeruginosa
-
additional information medium conditions for the cell culture Pseudomonas oleovorans
-
additional information strain A30-1 requires a complexed medium which must contains diverse metal ions, overview Bacillus sp. (in: Bacteria)
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Bacillus sp. (in: Bacteria)

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl butyrate + H2O
-
Rhodotorula glutinis 4-nitrophenol + butyrate
-
?
4-nitrophenyl caprylate + H2O L1, best substrate Geobacillus stearothermophilus 4-nitrophenol + caprylate
-
?
4-nitrophenyl caprylate + H2O preferred substrate of lipase A Diutina rugosa 4-nitrophenol + caprylate
-
?
4-nitrophenyl caprylate + H2O L1, best substrate Geobacillus stearothermophilus L1 4-nitrophenol + caprylate
-
?
4-nitrophenyl laurate + H2O
-
Rhodotorula glutinis 4-nitrophenol + laurate
-
?
4-nitrophenyl laurate + H2O preferred substrate of lipase B Diutina rugosa 4-nitrophenol + laurate
-
?
4-nitrophenyl laurate + H2O purified enzyme of strain F-111 shows preference for Pseudomonas aeruginosa 4-nitrophenol + laurate
-
?
4-nitrophenyl myristate + H2O purified enzyme of strain F-111 shows preference for Pseudomonas aeruginosa 4-nitrophenol + myristate
-
?
4-nitrophenyl palmitate + H2O
-
Acinetobacter calcoaceticus 4-nitrophenol + palmitate
-
?
4-nitrophenyl palmitate + H2O in n-heptane Burkholderia cepacia 4-nitrophenol + palmitate
-
?
4-nitrophenyl palmitate + H2O
-
Acinetobacter calcoaceticus BD 413 4-nitrophenol + palmitate
-
?
castor oil + H2O
-
Pseudomonas aeruginosa ?
-
?
methyl beta-D-glucopyranoside + H2O regioselective deacetylation of preacylated substrate Aspergillus niger methanol + beta-D-glucose
-
?
additional information enantioselective transesterification of 2-phenoxy-1-propanol Pseudomonas sp. ?
-
?
additional information highly specific for short-chain fatty acids esters Penicillium roqueforti ?
-
?
additional information immobilized enzyme performs the transesterification reaction that replaces pamitic acid in palm oil with stearic acid Rhizomucor miehei ?
-
?
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 Moesziomyces antarcticus ?
-
?
additional information strain A30-1, active with triglycerides of C16:0 to C22:0fatty acids and on natural fats and oils Bacillus sp. (in: Bacteria) ?
-
?
additional information substrates are long acyl chain 4-nitrophenol esters Acinetobacter calcoaceticus ?
-
?
additional information highly specific for short-chain fatty acids esters Penicillium roqueforti IAM7268 ?
-
?
additional information strain A30-1, active with triglycerides of C16:0 to C22:0fatty acids and on natural fats and oils Bacillus sp. (in: Bacteria) J33 ?
-
?
additional information substrates are long acyl chain 4-nitrophenol esters Acinetobacter calcoaceticus BD 413 ?
-
?
additional information enantioselective transesterification of 2-phenoxy-1-propanol Pseudomonas sp. KM1-56 ?
-
?
R-ketoprofen + H2O lipase B is stereoselective for the R-isomer in an antichiral solvent such as isopentyl methyl ketone or S(+)-carvone Moesziomyces antarcticus ?
-
?
rac 2-(4-chlorophenoxy)propanoic acid + n-butanol esterification reaction, in n-heptane Diutina rugosa ?
-
?
sulcatol + fatty acid esterification reaction, in toluene Diutina rugosa ?
-
?
tert-butyl octanoate + H2O preferred substrate, high activity with Burkholderia sp. tert-butanol + octanoate
-
?
tributyrin + H2O
-
Geobacillus stearothermophilus dibutyrin + butyrate
-
?
tributyrin + H2O
-
Aspergillus niger dibutyrin + butyrate
-
?
tributyrin + H2O
-
Pseudomonas aeruginosa dibutyrin + butyrate
-
?
tributyrin + H2O
-
Pseudomonas sp. dibutyrin + butyrate
-
?
tributyrin + H2O
-
Acinetobacter calcoaceticus dibutyrin + butyrate
-
?
tributyrin + H2O
-
Proteus vulgaris dibutyrin + butyrate
-
?
tributyrin + H2O
-
Rhodotorula glutinis dibutyrin + butyrate
-
?
tributyrin + H2O
-
Staphylococcus epidermidis dibutyrin + butyrate
-
?
tributyrin + H2O
-
Rhizopus arrhizus dibutyrin + butyrate
-
?
tributyrin + H2O
-
Bacillus sp. (in: Bacteria) dibutyrin + butyrate
-
?
tributyrin + H2O
-
Pseudomonas alcaligenes dibutyrin + butyrate
-
?
tributyrin + H2O
-
Burkholderia cepacia dibutyrin + butyrate
-
?
tributyrin + H2O
-
Aspergillus oryzae dibutyrin + butyrate
-
?
tributyrin + H2O
-
Penicillium roqueforti dibutyrin + butyrate
-
?
tributyrin + H2O
-
Diutina rugosa dibutyrin + butyrate
-
?
tributyrin + H2O
-
Pseudomonas oleovorans dibutyrin + butyrate
-
?
tributyrin + H2O
-
Rhizomucor miehei dibutyrin + butyrate
-
?
tributyrin + H2O
-
Moesziomyces antarcticus dibutyrin + butyrate
-
?
tributyrin + H2O
-
Hyphopichia burtonii dibutyrin + butyrate
-
?
tributyrin + H2O
-
Burkholderia sp. dibutyrin + butyrate
-
?
tributyrin + H2O
-
Penicillium wortmanii dibutyrin + butyrate
-
?
tributyrin + H2O
-
Penicillium roqueforti IAM7268 dibutyrin + butyrate
-
?
tributyrin + H2O
-
Bacillus sp. (in: Bacteria) J33 dibutyrin + butyrate
-
?
tributyrin + H2O
-
Acinetobacter calcoaceticus BD 413 dibutyrin + butyrate
-
?
tributyrin + H2O
-
Geobacillus stearothermophilus L1 dibutyrin + butyrate
-
?
tributyrin + H2O
-
Pseudomonas sp. KM1-56 dibutyrin + butyrate
-
?
triolein + H2O hydrolysis at all positions, strain J33 Bacillus sp. (in: Bacteria) diolein + oleate
-
?
triolein + H2O preferred substrate of enzyme form L1 Aspergillus oryzae diolein + oleate
-
?
triolein + H2O hydrolysis at all positions, strain J33 Bacillus sp. (in: Bacteria) J33 diolein + oleate
-
?

Subunits

Subunits Comment Organism
? x * 25000, SDS-PAGE Penicillium roqueforti
? 1 * 31000, SDS-PAGE Proteus vulgaris
? x * 29000, enzyme of strain MB5001, SDS-PAGE, x * 32000, enzyme from strain F-111, SDS-PAGE, x * 30000, enzyme of strain KKA-5, SDS-PAGE Pseudomonas aeruginosa
? x * 32000, strain BD 413, SDS-PAGE Acinetobacter calcoaceticus
? x * 33000, enzyme from strain KM1-56, SDS-PAGE, x * 30000, extracellular enzyme, SDS-PAGE Pseudomonas sp.
dimer 1 * 35000 + 1 * 46000, recombinant enzyme, SDS-PAGE Staphylococcus epidermidis
monomer 1 * 51000, SDS-PAGE Hyphopichia burtonii
monomer 1 * 24000, enzyme form L1 Aspergillus oryzae
monomer 1 * 32000, extracellular enzyme, SDS-PAGE Rhizopus arrhizus
monomer 1 * 45000, strain J33 Bacillus sp. (in: Bacteria)

Synonyms

Synonyms Comment Organism
amano AP
-
Moesziomyces antarcticus
amano B
-
Moesziomyces antarcticus
amano CE
-
Moesziomyces antarcticus
amano CES
-
Moesziomyces antarcticus
amano P
-
Moesziomyces antarcticus
amno N-AP
-
Moesziomyces antarcticus
BAL
-
Moesziomyces antarcticus
Bile-salt-stimulated lipase
-
Moesziomyces antarcticus
BSSL
-
Moesziomyces antarcticus
butyrinase
-
Moesziomyces antarcticus
cacordase
-
Moesziomyces antarcticus
CALB
-
Moesziomyces antarcticus
capalase L
-
Moesziomyces antarcticus
Carboxyl ester lipase
-
Moesziomyces antarcticus
cholesterol esterase
-
Moesziomyces antarcticus
CRL
-
Diutina rugosa
Cytotoxic T lymphocyte lipase
-
Moesziomyces antarcticus
EDL
-
Moesziomyces antarcticus
endothelial cell-derived lipase
-
Moesziomyces antarcticus
endothelial-derived lipase
-
Moesziomyces antarcticus
GA 56 (enzyme)
-
Moesziomyces antarcticus
Gastric lipase
-
Moesziomyces antarcticus
GEH
-
Moesziomyces antarcticus
glycerol ester hydrolase
-
Moesziomyces antarcticus
glycerol-ester hydrolase
-
Moesziomyces antarcticus
heparin releasable hepatic lipase
-
Moesziomyces antarcticus
hepatic lipase
-
Moesziomyces antarcticus
hepatic monoacylglycerol acyltransferase
-
Moesziomyces antarcticus
Lingual lipase
-
Moesziomyces antarcticus
lipase
-
Geobacillus stearothermophilus
lipase
-
Aspergillus niger
lipase
-
Pseudomonas aeruginosa
lipase
-
Pseudomonas sp.
lipase
-
Acinetobacter calcoaceticus
lipase
-
Proteus vulgaris
lipase
-
Rhodotorula glutinis
lipase
-
Staphylococcus epidermidis
lipase
-
Rhizopus arrhizus
lipase
-
Bacillus sp. (in: Bacteria)
lipase
-
Pseudomonas alcaligenes
lipase
-
Burkholderia cepacia
lipase
-
Aspergillus oryzae
lipase
-
Penicillium roqueforti
lipase
-
Pseudomonas oleovorans
lipase
-
Rhizomucor miehei
lipase
-
Moesziomyces antarcticus
lipase
-
Hyphopichia burtonii
lipase
-
Burkholderia sp.
lipase
-
Penicillium wortmanii
lipase, triacylglycerol
-
Moesziomyces antarcticus
lipazin
-
Moesziomyces antarcticus
liver lipase
-
Moesziomyces antarcticus
meito MY 30
-
Moesziomyces antarcticus
meito Sangyo OF lipase
-
Moesziomyces antarcticus
Pancreatic lipase
-
Moesziomyces antarcticus
Pancreatic lysophospholipase
-
Moesziomyces antarcticus
PGE
-
Moesziomyces antarcticus
PL-RP2
-
Moesziomyces antarcticus
post-heparin plasma protamine-resistant lipase
-
Moesziomyces antarcticus
PPL
-
Moesziomyces antarcticus
Pregastric esterase
-
Moesziomyces antarcticus
Pregastric lipase
-
Moesziomyces antarcticus
salt-resistant post-heparin lipase
-
Moesziomyces antarcticus
steapsin
-
Moesziomyces antarcticus
Sterol esterase
-
Moesziomyces antarcticus
takedo 1969-4-9
-
Moesziomyces antarcticus
teenesterase
-
Moesziomyces antarcticus
tiacetinase
-
Moesziomyces antarcticus
tibutyrin esterase
-
Moesziomyces antarcticus
triacylglycerol ester hydrolase
-
Moesziomyces antarcticus
Triacylglycerol lipase
-
Moesziomyces antarcticus
tributyrase
-
Moesziomyces antarcticus
tributyrinase
-
Moesziomyces antarcticus
triglyceridase
-
Moesziomyces antarcticus
triglyceride hydrolase
-
Moesziomyces antarcticus
triglyceride lipase
-
Moesziomyces antarcticus
triolein hydrolase
-
Moesziomyces antarcticus
tween hydrolase
-
Moesziomyces antarcticus
tween-hydrolyzing esterase
-
Moesziomyces antarcticus
Tweenase
-
Moesziomyces antarcticus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
extracellular enzyme Rhizopus arrhizus
40
-
strain F-111 Pseudomonas oleovorans
45
-
-
Hyphopichia burtonii
45
-
crude enzyme Penicillium wortmanii
45 60 extracellular enzyme Pseudomonas sp.
50
-
optimal growth temperature, strain RS-12, and extracellular enzyme Bacillus sp. (in: Bacteria)
55
-
strain MB5001 Pseudomonas aeruginosa
60
-
enzyme from strain A30-1, also optimal growth temperature for the strain in vivo at pH 9.0 Bacillus sp. (in: Bacteria)
60
-
strain KW1-56 Pseudomonas sp.
60 65 L1 Geobacillus stearothermophilus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
40 50 strain RS-12, no growth at 40°C, maximal growth at 50°C Bacillus sp. (in: Bacteria)

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
highly thermostable enzyme, strain A30-1 Bacillus sp. (in: Bacteria)
additional information
-
lipase B can be stabilized by covalent immobilization Moesziomyces antarcticus
additional information
-
thermostable Pseudomonas aeruginosa
additional information
-
thermostable enzyme Geobacillus stearothermophilus
45
-
extracellular enzyme, 30 min, 65% remaining activity Rhizopus arrhizus
45
-
half-life 45 min Rhodotorula glutinis
55
-
half-life 11.8 min Rhodotorula glutinis
60
-
15 h, 90% remaining activity Bacillus sp. (in: Bacteria)
60
-
extracellular enzyme, stable up to Pseudomonas sp.
60
-
purified enzyme from strain KW1-56, 24 h, 96% remaining activity, thermostable enzyme Pseudomonas sp.
75
-
after 30 min 100% remaining activity, after 8 h 50% remaining activity, extracellular enzyme shows 50% remaining activity after 15 min Bacillus sp. (in: Bacteria)

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
native enzyme Staphylococcus epidermidis
6.5
-
-
Hyphopichia burtonii
7
-
crude enzyme Penicillium wortmanii
7 9 extracellular enzyme Pseudomonas sp.
7.5
-
-
Rhodotorula glutinis
7.5
-
extracellular enzyme Rhizopus arrhizus
7.8 8.8
-
Acinetobacter calcoaceticus
8
-
strain MB5001 Pseudomonas aeruginosa
8.5
-
strain KKA-5 Pseudomonas aeruginosa
9 10 L1 Geobacillus stearothermophilus
9.5
-
enzyme from strain A30-1 Bacillus sp. (in: Bacteria)
10
-
-
Proteus vulgaris

pH Range

pH Minimum pH Maximum Comment Organism
6 10 strain F-111 Pseudomonas oleovorans

pI Value

Organism Comment pI Value Maximum pI Value
Pseudomonas sp. extracellular enzyme
-
4.5
Hyphopichia burtonii isoelectric focusing
-
5.8
Pseudomonas aeruginosa strain F-111 7.4 7.3
Rhizopus arrhizus extracellular enzyme
-
7.6