Literature summary extracted from
Namboodiri, V.M.H.; Chattopadhyaya, R.
Purification and biochemical characterization of a novel thermostable lipase from Aspergillus niger (2000), Lipids, 35, 495-502.
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
3.1.1.3 |
1,10-phenanthroline |
inhibition at 10-30 mM |
Aspergillus niger |
|
3.1.1.3 |
chymotrypsin |
proteolytic cleavage only of the heat-denatured enzyme, not of the native enzyme |
Aspergillus niger |
|
3.1.1.3 |
Cu2+ |
strong inhibition, 40% residual activity at 50 mM |
Aspergillus niger |
|
3.1.1.3 |
endoprotease Glu-C |
proteolytic cleavage only of the heat-denatured enzyme, not of the native enzyme |
Aspergillus niger |
|
3.1.1.3 |
Fe2+ |
strong inhibition, 30% residual activity at 50 mM |
Aspergillus niger |
|
3.1.1.3 |
Fe3+ |
strong inhibition, 25% residual activity at 50 mM |
Aspergillus niger |
|
3.1.1.3 |
additional information |
no inhibition by EDTA 50 mM |
Aspergillus niger |
|
3.1.1.3 |
papain |
proteolytic cleavage only of the heat-denatured enzyme, not of the native enzyme |
Aspergillus niger |
|
3.1.1.3 |
thrombin |
proteolytic cleavage only of the heat-denatured enzyme, not of the native enzyme |
Aspergillus niger |
|
3.1.1.3 |
Trypsin |
proteolytic cleavage only of the heat-denatured enzyme, not of the native enzyme |
Aspergillus niger |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
3.1.1.3 |
additional information |
enzyme activity is not affected by Mg2+, K+, Na+, Ca2+, Mn2+, NH4+, and Zn2+ up to 1.0 M |
Aspergillus niger |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
3.1.1.3 |
35500 |
- |
gel filtration |
Aspergillus niger |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.1.1.3 |
Aspergillus niger |
- |
- |
- |
Posttranslational Modification
EC Number |
Posttranslational Modification |
Comment |
Organism |
---|
3.1.1.3 |
glycoprotein |
contains 2.8% sugar, which is not essentail for activity |
Aspergillus niger |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.1.1.3 |
50fold, 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 |
208.2 |
- |
purified enzyme |
Aspergillus niger |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.1.1.3 |
additional information |
substrate is olive oil, the enzyme is 1,3-specific |
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 |
35 |
55 |
- |
Aspergillus niger |
Temperature Range [°C]
EC Number |
Temperature Minimum [°C] |
Temperature Maximum [°C] |
Comment |
Organism |
---|
3.1.1.3 |
20 |
75 |
- |
Aspergillus niger |
Temperature Stability [°C]
EC Number |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
---|
3.1.1.3 |
50 |
- |
60 min stable |
Aspergillus niger |
3.1.1.3 |
60 |
- |
50% remaining activity after 60 min |
Aspergillus niger |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
3.1.1.3 |
5 |
6 |
- |
Aspergillus niger |
pH Range
EC Number |
pH Minimum |
pH Maximum |
Comment |
Organism |
---|
3.1.1.3 |
5 |
7.5 |
- |
Aspergillus niger |
pI Value
EC Number |
Organism |
Comment |
pI Value Maximum |
pI Value |
---|
3.1.1.3 |
Aspergillus niger |
isoelectric focusing |
- |
4.4 |