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Literature summary extracted from

  • Li, H.; Sun, W.; Gao, Y.; Wu, Y.; Huang, L.; Huang, E.; Wang, A.; Yin, X.; Wang, Q.; Xie, T.; Zeng, Z.
    Cloning, recombinant expression and characterization of a new glucoamylase gene from Aureobasidium pullulans NRRL 12974 and its potential application in raw potato starch degradation (2011), Afr. J. Biotechnol., 10, 9122-9131.
No PubMed abstract available

Application

EC Number Application Comment Organism
3.2.1.3 industry this glucoamylase may find important applications in the starch saccharification industry and in bioethanol production Aureobasidium pullulans

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.3 gene APGA1, DNA and amino acid sequence determination and analysis, expression in Pichia pastoris Aureobasidium pullulans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.3 extracellular
-
Aureobasidium pullulans
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.3 66000
-
x * 66000, SDS-PAGE Aureobasidium pullulans

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.3 Aureobasidium pullulans E2GDF4 gene APGA1
-
3.2.1.3 Aureobasidium pullulans NRRL 12974 E2GDF4 gene APGA1
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.3 glycoprotein
-
Aureobasidium pullulans

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.3 recombinant enzyme from Pichia pastoris by ultrafiltration, gel filtration, and anion exchange chromatography to homogeneity Aureobasidium pullulans

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.3 298
-
purified recombinant enzyme, pH 4.5, 60°C, substarte raw potato starch Aureobasidium pullulans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.3 amylopectin + H2O
-
Aureobasidium pullulans ?
-
?
3.2.1.3 amylopectin + H2O
-
Aureobasidium pullulans NRRL 12974 ?
-
?
3.2.1.3 amylose + H2O
-
Aureobasidium pullulans ?
-
?
3.2.1.3 amylose + H2O
-
Aureobasidium pullulans NRRL 12974 ?
-
?
3.2.1.3 glycogen + H2O
-
Aureobasidium pullulans ?
-
?
3.2.1.3 glycogen + H2O
-
Aureobasidium pullulans NRRL 12974 ?
-
?
3.2.1.3 additional information poor activity with pullulan and laminarin Aureobasidium pullulans ?
-
?
3.2.1.3 additional information poor activity with pullulan and laminarin Aureobasidium pullulans NRRL 12974 ?
-
?
3.2.1.3 raw potato starch + H2O
-
Aureobasidium pullulans ?
-
?
3.2.1.3 soluble starch + H2O
-
Aureobasidium pullulans ?
-
?
3.2.1.3 soluble starch + H2O
-
Aureobasidium pullulans NRRL 12974 ?
-
?

Subunits

EC Number Subunits Comment Organism
3.2.1.3 ? x * 66000, SDS-PAGE Aureobasidium pullulans

Synonyms

EC Number Synonyms Comment Organism
3.2.1.3 APGA1
-
Aureobasidium pullulans
3.2.1.3 glucoamylase
-
Aureobasidium pullulans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.3 60
-
-
Aureobasidium pullulans

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.3 30 80 activity range Aureobasidium pullulans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.3 4.5
-
-
Aureobasidium pullulans

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.3 3 6 purified recombinant enzyme, stable between pH 3 and pH 6. The catalytic activity of the enzyme is reduced quickly at higher than pH 5 and is totally lost at higher than pH 7 Aureobasidium pullulans