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Literature summary for 3.2.1.3 extracted from

  • Pasin, T.M.; Benassi, V.M.; Heinen, P.R.; Damasio, A.R.L.; Cereia, M.; Jorge, J.A.; Polizeli, M.L.T.M.
    Purification and functional properties of a novel glucoamylase activated by manganese and lead produced by Aspergillus japonicus (2017), Int. J. Biol. Macromol., 102, 779-788 .
    View publication on PubMed
Search for more literature for 3.2.1.3

Activating Compound

Activating Compound Comment Organism Structure
EDTA causes a slight activation of 12% at 5 mM Aspergillus japonicus

Application

Application Comment Organism
industry biotechnological applications of this glucoamylase from Aspergillus japonicus in the recycling and deinking process by the paper industries. Glucoamylases are used in food, pharmaceutical and textile industries Aspergillus japonicus
paper production biotechnological applications of this glucoamylase from Aspergillus japonicus in the recycling and deinking process by the paper industries Aspergillus japonicus

Inhibitors

Inhibitors Comment Organism Structure
Mn2+ activates 51% and 65% at 5 mM and 10 mM, respectively, inhibitory at above 15 mM Aspergillus japonicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten and Lineweaver-Burk kinetics Aspergillus japonicus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Aspergillus japonicus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ activates 51% and 65% at 5 mM and 10 mM, respectively, inhibitory at above 15 mM Aspergillus japonicus
Pb2+ activates Aspergillus japonicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
72000
-
 native enzyme, native PAGE Aspergillus japonicus

Organism

Organism UniProt Comment Textmining
Aspergillus japonicus
-
 originally isolated from soil
-
Aspergillus japonicus Saito
-
 originally isolated from soil
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the glycoprotein composition is estimated as 15% for the crude enzyme and 5.5% for the purified glucoamylase Aspergillus japonicus

Purification (Commentary)

Purification (Comment) Organism
extracellular enzyme 1.32fold from crude cell extract by anion exchange chromatography and dialysis Aspergillus japonicus

Source Tissue

Source Tissue Comment Organism Textmining
mycelium the fungus is cultivated in Khanna medium, pH 5.5, for 4 days, at 25°C, in static condition, supplemented with potato starch and maltose in different concentrations, effects on Aspergillus japonicus cultivation, overview Aspergillus japonicus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
301.77
-
 purified native extracellular enzyme, pH 5.0, 65°C Aspergillus japonicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl D-glucopyranoside + H2O
-
 Aspergillus japonicus 4-nitrophenol + D-glucopyranose
-
 ?
4-nitrophenyl D-glucopyranoside + H2O
-
 Aspergillus japonicus Saito 4-nitrophenol + D-glucopyranose
-
 ?
amylopectin + H2O best substrate Aspergillus japonicus D-glucose + ?
-
 ?
amylopectin + H2O best substrate Aspergillus japonicus Saito D-glucose + ?
-
 ?
amylose + H2O
-
 Aspergillus japonicus ?
-
 ?
amylose + H2O
-
 Aspergillus japonicus Saito ?
-
 ?
maltose + H2O
-
 Aspergillus japonicus ?
-
 ?
maltose + H2O
-
 Aspergillus japonicus Saito ?
-
 ?
starch + H2O corn starch, potato starch, hydrolyzed potato starch, and rice starch Aspergillus japonicus ?
-
 ?
starch + H2O corn starch, potato starch, hydrolyzed potato starch, and rice starch Aspergillus japonicus Saito ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 72000, SDS-PAGE Aspergillus japonicus

Synonyms

Synonyms Comment Organism
glucoamylase
-
 Aspergillus japonicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
-
 Aspergillus japonicus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 80 at temperatures between 55°C and 65°C the glucoamylase retains 95-100% of its activity, at 70°C over 75% of the activity remains, 23% at 80°C Aspergillus japonicus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
 purified native enzyme, after 90 min about 95% of activity is remaining, after 300 min 20% activity remains Aspergillus japonicus
50
-
 purified native enzyme, 1 h, stable, 50% activity remaining after 2 h Aspergillus japonicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
 Aspergillus japonicus

pH Range

pH Minimum pH Maximum Comment Organism
4 6.5 over 50% of maximal activity within this range, profile overview Aspergillus japonicus

pH Stability

pH Stability pH Stability Maximum Comment Organism
3 7 purified native enzyme, stable at Aspergillus japonicus

General Information

General Information Comment Organism
evolution the enzyme belongs to the superfamily of CBM 20, phylogenetic tree Aspergillus japonicus