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Literature summary 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

Inhibitors

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

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.15 30000
-
 x * 30000, SDS-PAGE Thermoascus aurantiacus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.15 Thermoascus aurantiacus
-
-
-
3.2.1.15 Thermoascus aurantiacus CBMAI-756
-
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.15 5000
-
 13.7fold purified enzyme Thermoascus aurantiacus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.15 additional information the purified enzyme is an endo/exo-enzyme, releasing mono, di- and tri-galacturonic acids within 10 min of hydrolysis Thermoascus aurantiacus ?
-
 ?
3.2.1.15 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 ?
-
 ?
3.2.1.15 pectin + H2O citrus or apple pectin, highest enzyme activity with citrus pectin Thermoascus aurantiacus ?
-
 ?
3.2.1.15 pectin + H2O citrus or apple pectin, highest enzyme activity with citrus pectin Thermoascus aurantiacus CBMAI-756 ?
-
 ?
3.2.1.15 polygalacturonic acid + H2O
-
 Thermoascus aurantiacus ?
-
 ?
3.2.1.15 polygalacturonic acid + H2O
-
 Thermoascus aurantiacus CBMAI-756 ?
-
 ?

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
3.2.1.15 endo-PG
-
 Thermoascus aurantiacus
3.2.1.15 endo-polygalacturonase
-
 Thermoascus aurantiacus
3.2.1.15 Exo-PG
-
 Thermoascus aurantiacus
3.2.1.15 exo-polygalacturonase
-
 Thermoascus aurantiacus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.15 65
-
-
 Thermoascus aurantiacus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.15 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.15 5.5
-
-
 Thermoascus aurantiacus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.15 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

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.15 Thermoascus aurantiacus isoelectric focusing
-
 7.8