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Literature summary extracted from

  • Koc, O.; Metin, K.
    Purification and characterization of a thermostable glucoamylase produced by Aspergillus flavus HBF34 (2010), Afr. J. Biotechnol., 9, 3414-3424.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.3 Al3+
-
 Aspergillus flavus
3.2.1.3 Cu2+
-
 Aspergillus flavus
3.2.1.3 EDTA
-
 Aspergillus flavus
3.2.1.3 Fe3+
-
 Aspergillus flavus
3.2.1.3 Hg2+
-
 Aspergillus flavus
3.2.1.3 Mg2+
-
 Aspergillus flavus
3.2.1.3 N-bromosuccinimide
-
 Aspergillus flavus
3.2.1.3 Na2O3Se
-
 Aspergillus flavus
3.2.1.3 NH4Cl
-
 Aspergillus flavus
3.2.1.3 Ni2+
-
 Aspergillus flavus
3.2.1.3 Phenylmethanesulfonylfluoride
-
 Aspergillus flavus
3.2.1.3 Zn2+
-
 Aspergillus flavus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.3 Ba2+ activates Aspergillus flavus
3.2.1.3 Ca2+ activates Aspergillus flavus
3.2.1.3 Co2+ activates at 1 mM, no effect at 10 mM Aspergillus flavus
3.2.1.3 Mn2+ activates Aspergillus flavus
3.2.1.3 additional information no effects on enzyme activity by Li+ and K+, and by NaCl Aspergillus flavus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.3 Aspergillus flavus
-
 two isozymes
-
3.2.1.3 Aspergillus flavus HBF34
-
 two isozymes
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.3 native isozymes 120fold by starch affinity chromatography, isozyme separation by PAGE zymography Aspergillus flavus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.3 mycelium
-
 Aspergillus flavus
-

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 6619
-
 purified enzyme, pH 6.0, 60°C Aspergillus flavus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.3 additional information the enzyme is active on the following substrates in descending order: glycogen, amylopectin, corn starch, rice starch, wheat starch, maltose, amylose, dextrin, maltotriose, raffinose, and sucrose Aspergillus flavus ?
-
 ?
3.2.1.3 additional information the enzyme is active on the following substrates in descending order: glycogen, amylopectin, corn starch, rice starch, wheat starch, maltose, amylose, dextrin, maltotriose, raffinose, and sucrose Aspergillus flavus HBF34 ?
-
 ?
3.2.1.3 soluble potato starch + H2O
-
 Aspergillus flavus ?
-
 ?
3.2.1.3 soluble potato starch + H2O
-
 Aspergillus flavus HBF34 ?
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.3 60
-
-
 Aspergillus flavus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.3 10 60 activity increases linearly from 10°C to 60°C and reaches a maximum at 60°C Aspergillus flavus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.3 27
-
 purified isozymes, 72 h, no loss in activity Aspergillus flavus
3.2.1.3 40
-
 purified isozymes, 72 h, no loss in activity Aspergillus flavus
3.2.1.3 50
-
 purified isozymes, 72 h, 46% activity remaining Aspergillus flavus
3.2.1.3 65
-
 purified isozymes, 95% activity remaining Aspergillus flavus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.3 6
-
-
 Aspergillus flavus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.3 3 8 purified isozymes, 72 h, 78% activity remaining Aspergillus flavus

General Information

EC Number General Information Comment Organism
3.2.1.3 physiological function glucoamylase is an exo-acting enzyme that catalyses the production of beta-glucose from the non-reducing ends of amylose, amylopectin and glycogen Aspergillus flavus