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Literature summary for 3.1.1.3 extracted from

  • Liu, Z.; Chi, Z.; Wang, L.; Li, J.
    Production, purification and characterization of an extracellular lipase from Aureobasidium pullulans HN2.3 with potential application for the hydrolysis of edible oils (2008), Biochem. Eng. J., 40, 445-451.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
Ag+ 80% residual activity at 5 mM Aureobasidium pullulans
Ba2+ 74.3% residual activity at 5 mM Aureobasidium pullulans
Ca2+ 73% residual activity at 5 mM Aureobasidium pullulans
Co2+ 68% residual activity at 5 mM Aureobasidium pullulans
Cu2+ 62% residual activity at 5 mM Aureobasidium pullulans
Fe2+ 30% residual activity at 5 mM Aureobasidium pullulans
Fe3+ 77% residual activity at 5 mM Aureobasidium pullulans
Hg2+ 32.3% residual activity at 5 mM Aureobasidium pullulans
iodoacetic acid 88% residual activity at 5 mM Aureobasidium pullulans
Li+ 82% residual activity at 5 mM Aureobasidium pullulans
Mg2+ 78% residual activity at 5 mM Aureobasidium pullulans
Mn2+ 71% residual activity at 5 mM Aureobasidium pullulans
additional information not inhibited by EDTA Aureobasidium pullulans
phenylmethanesulfonyl fluoride 67.2% residual activity at 5 mM Aureobasidium pullulans
SDS 21.3% residual activity at 5 mM Aureobasidium pullulans
Zn2+ 59.1% residual activity at 5 mM Aureobasidium pullulans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.608
-
4-nitrophenyl laurate
-
Aureobasidium pullulans

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Aureobasidium pullulans
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
63500
-
SDS-PAGE Aureobasidium pullulans

Organism

Organism UniProt Comment Textmining
Aureobasidium pullulans
-
-
-
Aureobasidium pullulans HN2.3
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, Sephadex-75 gel filtration, and DEAE-Sepharose column chromatography Aureobasidium pullulans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
26
-
enzyme from crude supernatant Aureobasidium pullulans
88.6
-
enzyme after 3.4fold purification Aureobasidium pullulans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl laurate + H2O
-
Aureobasidium pullulans 4-nitrophenol + laurate
-
?
4-nitrophenyl laurate + H2O
-
Aureobasidium pullulans HN2.3 4-nitrophenol + laurate
-
?
lard + H2O
-
Aureobasidium pullulans ?
-
?
lard + H2O
-
Aureobasidium pullulans HN2.3 ?
-
?
olive oil + H2O
-
Aureobasidium pullulans ?
-
?
olive oil + H2O
-
Aureobasidium pullulans HN2.3 ?
-
?
peanut oil + H2O highest hydrolytic activity towards peanut oil Aureobasidium pullulans ?
-
?
peanut oil + H2O highest hydrolytic activity towards peanut oil Aureobasidium pullulans HN2.3 ?
-
?
soybean oil + H2O
-
Aureobasidium pullulans ?
-
?
soybean oil + H2O
-
Aureobasidium pullulans HN2.3 ?
-
?

Synonyms

Synonyms Comment Organism
extracellular lipase
-
Aureobasidium pullulans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
-
Aureobasidium pullulans

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 50
-
Aureobasidium pullulans

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
20 50 the residual lipase activity is maintained at 100% and 71% activity compared to the control after treatment for 1 h at 20°C and 30°C, respectively, the enzyme is inactivated rapidly at temperature higher than 20°C and is inactivated totally at 50°C within 1 h Aureobasidium pullulans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Aureobasidium pullulans

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 8.5
-
Aureobasidium pullulans