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Literature summary for 3.1.1.3 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
Search for more literature for 3.1.1.3

General Stability

General Stability Organism
Ca2+ stabilizes the enzyme Aspergillus niger

KM Value [mM]

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

Localization

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
-
-
Aspergillus niger Tiegh
-
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
lipase
-
 Aspergillus niger

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3 5
-
 Aspergillus niger