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Literature summary for 3.2.1.15 extracted from

  • Martins, E.S.; Silva, D.; da Silva, R.; Leite, R.S.; Gomes, E.
    Purification and characterization of polygalacturonase produced by thermophilic Thermoascus aurantiacus CBMAI-756 in submerged fermentation (2007), Antonie van Leeuwenhoek, 91, 291-299.
    View publication on PubMed
Search for more literature for 3.2.1.15

Inhibitors

Inhibitors Comment Organism Structure
EDTA 2 mM inhibits 25% of enzyme activity Thermoascus aurantiacus
Hg2+ 2 mM inhibits 100% of enzyme activity Thermoascus aurantiacus
Mg2+ 2 mM inhibits 7% of enzyme activity Thermoascus aurantiacus
Mn2+ 2 mM inhibits 75% of enzyme activity Thermoascus aurantiacus
Zn2+ 2 mM inhibits 50% of enzyme activity Thermoascus aurantiacus

Metals/Ions

Metals/Ions Comment Organism Structure
Ag+ slightly stimulates Thermoascus aurantiacus
K+ slightly stimulates Thermoascus aurantiacus
additional information Ca2+ has no effect Thermoascus aurantiacus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30000
-
 x * 30000, SDS-PAGE Thermoascus aurantiacus

Organism

Organism UniProt Comment Textmining
Thermoascus aurantiacus
-
-
-
Thermoascus aurantiacus CBMAI-756
-
-
-

Purification (Commentary)

Purification (Comment) Organism
to apparent homogeneity, 21fold, by gel filtration and cation-exchange chromatography Thermoascus aurantiacus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5000
-
 13.7fold purified enzyme Thermoascus aurantiacus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the purified enzyme is an endo/exo-enzyme, releasing mono, di- and tri-galacturonic acids within 10 min of hydrolysis Thermoascus aurantiacus ?
-
 ?
additional information the purified enzyme is an endo/exo-enzyme, releasing mono, di- and tri-galacturonic acids within 10 min of hydrolysis Thermoascus aurantiacus CBMAI-756 ?
-
 ?
pectin + H2O citrus or apple pectin, highest enzyme activity with citrus pectin Thermoascus aurantiacus ?
-
 ?
pectin + H2O citrus or apple pectin, highest enzyme activity with citrus pectin Thermoascus aurantiacus CBMAI-756 ?
-
 ?
polygalacturonic acid + H2O
-
 Thermoascus aurantiacus ?
-
 ?
polygalacturonic acid + H2O
-
 Thermoascus aurantiacus CBMAI-756 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 30000, SDS-PAGE Thermoascus aurantiacus

Synonyms

Synonyms Comment Organism
endo-PG
-
 Thermoascus aurantiacus
endo-polygalacturonase
-
 Thermoascus aurantiacus
Exo-PG
-
 Thermoascus aurantiacus
exo-polygalacturonase
-
 Thermoascus aurantiacus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
-
 Thermoascus aurantiacus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 the purified enzyme is 100% stable at 50°C for 1 h, half-life of 10 min at 60°C. At 60°C, enzymatic activity decreases to only 20% of original activity after 1 h Thermoascus aurantiacus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
-
 Thermoascus aurantiacus

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 6.5 in the absence of substrate, the purified enzyme is stable in a narrow pH range, with 100% stability at 5.0, although 55% of this activity is retained at pH 6.5. It maintains 33% of initial activity at pH 9.0 Thermoascus aurantiacus

pI Value

Organism Comment pI Value Maximum pI Value
Thermoascus aurantiacus isoelectric focusing
-
 7.8