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Literature summary extracted from

  • Saxena, R.K.; Davidson, W.S.; Sheoran, A.; Giri, B.
    Purification and characterization of an alkaline thermostable lipase from Aspergillus carneus (2003), Process Biochem., 39, 239-247.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.3 hexadecyl trimethyl ammonium bromide strong activation Aspergillus carneus
3.1.1.3 additional information no effect by metal chelators Aspergillus carneus
3.1.1.3 n-octyl-alpha-D-glucopyranoside strong activation Aspergillus carneus
3.1.1.3 n-octyl-beta-D-glucopyranoside strong activation Aspergillus carneus
3.1.1.3 taurocholic acid strong activation, 2.7fold at 10 mM Aspergillus carneus

General Stability

EC Number General Stability Organism
3.1.1.3 half-life of the enzyme is enhanced by glycine, sorbitol, glycerol, glucose, and ammonium chloride Aspergillus carneus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.3 Bromosuccinimide
-
Aspergillus carneus
3.1.1.3 cholic acid
-
Aspergillus carneus
3.1.1.3 diethyl 4-nitrophenyl phosphate strong inhibition Aspergillus carneus
3.1.1.3 additional information no effect by metal chelators, no inhibition by trinitrobenzene sulfonic acid, N-ethylmaleimide, p-chloromercuribenzoate, o-phenanthroline, and 4,4'-dipyridyl-disulfide Aspergillus carneus
3.1.1.3 N-lauroyl sarcosine strong inhibition Aspergillus carneus
3.1.1.3 PMSF strong inhibition Aspergillus carneus
3.1.1.3 SDS strong inhibition Aspergillus carneus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.3 additional information
-
additional information enzyme follows first order reaction kinetics during inactivation Aspergillus carneus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.3 Mg2+ acivation Aspergillus carneus
3.1.1.3 Na+ acivation Aspergillus carneus
3.1.1.3 NH4+ acivation Aspergillus carneus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.3 27000
-
about, native PAGE Aspergillus carneus

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
3.1.1.3 Butanol 80% loss of activity after 30 min, complete loss of activity after 24 h Aspergillus carneus
3.1.1.3 Ethanol complete loss of activity after 30 min in 90% ethanol, loss of 41% activity after 30 min in 40% ethanol Aspergillus carneus
3.1.1.3 additional information the enzyme is highly active in presence of many different organic solvents, overview Aspergillus carneus
3.1.1.3 propan-2-ol 97% loss of activity after 30 min in 60% propan-2-ol, loss of only 3% activity after 30 min in 30% propan-2-ol Aspergillus carneus

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Aspergillus carneus
-
alkaline thermostable lipase
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.1.3 glycoprotein 12.3% glycosylated Aspergillus carneus

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.3 24.1fold Aspergillus carneus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.1.3 triacylglycerol + H2O = diacylglycerol + a carboxylate a tryptophan residue plays an important role in maintaining the ative conformation of the enzyme Aspergillus carneus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.3 502
-
purified enzyme Aspergillus carneus

Storage Stability

EC Number Storage Stability Organism
3.1.1.3 22°C, room temperature, lyophilized enzyme, completely stable for more than 1 year Aspergillus carneus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 4-nitrophenyl acetate + H2O low activity Aspergillus carneus 4-nitrophenol + acetate
-
?
3.1.1.3 4-nitrophenyl caproate + H2O
-
Aspergillus carneus 4-nitrophenol + caproate
-
?
3.1.1.3 4-nitrophenyl laurate + H2O enzyme shows a preference for lauric acid and a 1,3-position specificity Aspergillus carneus 4-nitrophenol + laurate
-
?
3.1.1.3 4-nitrophenyl myristate + H2O
-
Aspergillus carneus 4-nitrophenol + myristate
-
?
3.1.1.3 4-nitrophenyl palmitate + H2O
-
Aspergillus carneus 4-nitrophenol + palmitate
-
?
3.1.1.3 4-nitrophenyl stearate + H2O low activity Aspergillus carneus 4-nitrophenol + stearate
-
?
3.1.1.3 additional information the enzyme utilizes olive oil as a substrate, no activity with 2-nitrophenyl palmitate Aspergillus carneus ?
-
?

Subunits

EC Number Subunits Comment Organism
3.1.1.3 monomer 1 * 27000, SDS-PAGE Aspergillus carneus

Synonyms

EC Number Synonyms Comment Organism
3.1.1.3 lipase
-
Aspergillus carneus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.3 37
-
-
Aspergillus carneus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.3 5 90
-
Aspergillus carneus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.3 additional information
-
thermostability is enhanced by glycine, sorbitol, glycerol, glucose, and ammonium chloride Aspergillus carneus
3.1.1.3 70
-
5 min, stable, after 10 min enzyme shows loss of 45% activity Aspergillus carneus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.3 9
-
-
Aspergillus carneus

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.1.1.3 Aspergillus carneus isoelectric focusing 4.4 4.3