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Literature summary extracted from

  • Chen, J.; Li, D.C.; Zhang, Y.Q.; Zhou, Q.X.
    Purification and characterization of a thermostable glucoamylase from Chaetomium thermophilum (2005), J. Gen. Appl. Microbiol., 51, 175-181.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.2.1.3 biotechnology the enzyme might be useful in biotechnological processes Thermochaetoides thermophila
3.2.1.3 industry the enzyme is used in industrial starch degradation Thermochaetoides thermophila

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.3 Ag+ complete inhibition at 1 mM Thermochaetoides thermophila
3.2.1.3 Cu2+ 12% inhibition at 1 mM Thermochaetoides thermophila
3.2.1.3 Fe2+ 80% inhibition at 1 mM Thermochaetoides thermophila
3.2.1.3 Hg2+ complete inhibition at 1 mM Thermochaetoides thermophila
3.2.1.3 Mn2+ 11% inhibition at 1 mM Thermochaetoides thermophila
3.2.1.3 additional information poor inhibition by Ba2+ at 1 mM Thermochaetoides thermophila
3.2.1.3 Zn2+ 25% inhibition at 1 mM Thermochaetoides thermophila

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.3 extracellular the enzyme is secreted to the culture medium Thermochaetoides thermophila
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.3 Ca2+ 20% activation at 1 mM Thermochaetoides thermophila
3.2.1.3 K+ 10% activation at 1 mM Thermochaetoides thermophila
3.2.1.3 additional information no effect by Mg2+ at 1 mM Thermochaetoides thermophila
3.2.1.3 Na+ 12% activation at 1 mM Thermochaetoides thermophila

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.3 64000
-
 1 * 64000, SDS-PAGE Thermochaetoides thermophila
3.2.1.3 65400
-
 gel filtration and native PAGE Thermochaetoides thermophila

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.3 Thermochaetoides thermophila
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.3 native soluble enzyme from culture medium 16.3 fold to homogeneity by ammonium sulfate fractionation, ion exchange and hydrophobic interaction chromatography, and gel filtration Thermochaetoides thermophila

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 71.2
-
 purified enzyme Thermochaetoides thermophila

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.3 starch + H2O
-
 Thermochaetoides thermophila starch + beta-D-glucose
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.3 monomer 1 * 64000, SDS-PAGE Thermochaetoides thermophila

Synonyms

EC Number Synonyms Comment Organism
3.2.1.3 exo-1,4-alpha-D-glucanohydrolase
-
 Thermochaetoides thermophila
3.2.1.3 glucoamylase
-
 Thermochaetoides thermophila

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.3 65
-
-
 Thermochaetoides thermophila

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.3 50 60 stable at, purified enzyme Thermochaetoides thermophila
3.2.1.3 65
-
 60 min, 50% activity remaining of purified enzyme Thermochaetoides thermophila
3.2.1.3 70
-
 30 min, 40% activity remaining of purified enzyme Thermochaetoides thermophila

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.3 4
-
-
 Thermochaetoides thermophila

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.3 2.5 9 30% of maximal activity at pH 3.0 and pH 8.5, 50% of maximal activity at pH 3.5 and pH 7.0 Thermochaetoides thermophila

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.3 3.5 8 stable at pH 3.0-8.0, about 50% remaining activity at pH 3.0 and pH 10.0, 30% at pH 2.5 and pH 11.0 Thermochaetoides thermophila