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Literature summary extracted from

  • van Heerden, E.; Litthauer, D.; Verger, R.
    Biochemical characterization and kinetic properties of a purified lipase from Aspergillus niger in bulk phase and monomolecular films (2002), Enzyme Microb. Technol., 30, 902-909.
No PubMed abstract available

General Stability

EC Number General Stability Organism
3.1.1.3 Ca2+ stabilizes the enzyme Aspergillus niger

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.3 additional information
-
 additional information reaction kinetics in a monomolecular layer of different diacylglycerides Aspergillus niger

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.3 extracellular secreted to the culture medium Aspergillus niger
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.3 40000
-
 x * 40000, SDS-PAGE Aspergillus niger

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Aspergillus niger
-
-
-
3.1.1.3 Aspergillus niger Tiegh
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.3 from culture supernatant, to homogeneity Aspergillus niger

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.3 729
-
 purified enzyme, substrate tricaprylin Aspergillus niger

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 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 Aspergillus niger ?
-
 ?
3.1.1.3 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 Aspergillus niger Tiegh ?
-
 ?
3.1.1.3 triacetin + H2O
-
 Aspergillus niger diacetin + acetate
-
 ?
3.1.1.3 tributyrin + H2O
-
 Aspergillus niger dibutyrin + butyrate
-
 ?
3.1.1.3 tributyrin + H2O
-
 Aspergillus niger Tiegh dibutyrin + butyrate
-
 ?
3.1.1.3 tricaproin + H2O
-
 Aspergillus niger dicaproin + caproate
-
 ?
3.1.1.3 tricaprylin + H2O best substrate Aspergillus niger dicaprylin + caprylate
-
 ?
3.1.1.3 tricaprylin + H2O best substrate Aspergillus niger Tiegh dicaprylin + caprylate
-
 ?
3.1.1.3 trilinolein + H2O trans C18:1(9) Aspergillus niger dilinolein + linoleate
-
 ?
3.1.1.3 trilinolein + H2O trans C18:1(9) Aspergillus niger Tiegh dilinolein + linoleate
-
 ?
3.1.1.3 triolein + H2O cis-C18:1(9) Aspergillus niger diolein + oleate
-
 ?
3.1.1.3 triolein + H2O cis-C18:1(9) Aspergillus niger Tiegh diolein + oleate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.3 ? x * 40000, SDS-PAGE Aspergillus niger

Synonyms

EC Number Synonyms Comment Organism
3.1.1.3 lipase
-
 Aspergillus niger

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.3 25 35
-
 Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.3 3 5
-
 Aspergillus niger