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Literature summary extracted from

  • Buga, M.; Ibrahim, S.; Nok, A.
    Physico-chemical characteristics of immobilized polygalacturonase from Aspergillus niger (SA6) (2010), Afr. J. Biotechnol., 9, 8934-8943.
No PubMed abstract available

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.15 additional information immobilization of the partially purified native enzyme, the sodium alginate immobilized polygalacturonase exhibits more stability to changes in pH than the temperature. Activity of the immobilized polygalacturonase is reduced to 34.56% and 14.81% of the initial activity after the second and third catalytic cycles, respectively, half-life is 10 min at pH 4.5, 40°C Aspergillus niger

General Stability

EC Number General Stability Organism
3.2.1.67 calcium alginate-immobilized polygalacturonase exhibits more stability to changes in pH than the temperature. The activity of the immobilized polygalacturonase reduces to 34.56% and 14.81% of the initial activity in the second and third catalytic cycles, respectively Aspergillus niger

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.15 35000
-
 x * 35000, SDS-PAGE Aspergillus niger
3.2.1.67 35000
-
 1 * 40000 + 1 * 35000, endo- and exo-polygalacturonase, SDS-PAGE Aspergillus niger
3.2.1.67 40000
-
 1 * 40000 + 1 * 35000, endo- and exo-polygalacturonase, SDS-PAGE Aspergillus niger

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.15 Aspergillus niger
-
-
-
3.2.1.15 Aspergillus niger SA6
-
-
-
3.2.1.67 Aspergillus niger
-
-
-
3.2.1.67 Aspergillus niger SA6
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.15 native enzyme 9fold by ultrafiltration, ammonium sulfate fractionation, ion exchange chromatography, and gel filtration Aspergillus niger
3.2.1.67 ammonium sulfate precipitation, DEAE-Sepharose column chromatography, and Sephadex G-75 gel filtration Aspergillus niger

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.15 246
-
 partially purified enzyme, pH 4.5, 40°C Aspergillus niger
3.2.1.67 26.99
-
 crude enzyme, at pH 4.5 and 40°C Aspergillus niger
3.2.1.67 246
-
 after 9.1fold purification, at pH 4.5 and 40°C Aspergillus niger

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.67 citric pectin + H2O
-
 Aspergillus niger D-galacturonic acid + ?
-
 ?
3.2.1.67 citric pectin + H2O
-
 Aspergillus niger SA6 D-galacturonic acid + ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.15 ? x * 35000, SDS-PAGE Aspergillus niger
3.2.1.67 heterodimer 1 * 40000 + 1 * 35000, endo- and exo-polygalacturonase, SDS-PAGE Aspergillus niger

Synonyms

EC Number Synonyms Comment Organism
3.2.1.15 endo PG
-
 Aspergillus niger
3.2.1.67 exo polygalacturonase
-
 Aspergillus niger
3.2.1.67 exoPG
-
 Aspergillus niger
3.2.1.67 pectinase
-
 Aspergillus niger

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.15 40
-
-
 Aspergillus niger
3.2.1.67 40
-
-
 Aspergillus niger

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.67 50 70 the immobilized polygalacturonase is most stable at 50°C and least stable at 70°C Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.15 4.5
-
-
 Aspergillus niger
3.2.1.67 4.5
-
-
 Aspergillus niger

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.67 4 5 the immobilized polygalacturonase is stable between pH 4.0 and 5.0. The enzyme is however more stable at pH 5.0 Aspergillus niger