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Literature summary extracted from

  • Karim, K.M.; Husaini, A.; Hossain, M.A.; Sing, N.N.; Mohd Sinang, F.; Hussain, M.H.; Roslan, H.A.
    Heterologous, expression, and characterization of thermostable glucoamylase derived from Aspergillus flavus NSH9 in Pichia pastoris (2016), BioMed Res. Int., 2016, 5962028 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.3 Ca2+ activates at above 5 mM Aspergillus flavus
3.2.1.3 Cu2+ activates at 1 mM, inhibits at above 5 mM Aspergillus flavus
3.2.1.3 Fe2+ activates at 1 mM Aspergillus flavus
3.2.1.3 Mg2+ activates at 1 mM Aspergillus flavus
3.2.1.3 Pb2+ activates at 1 mM, inhibits at above 5 mM Aspergillus flavus
3.2.1.3 Zn2+ activates at 1 mM, inhibits at above 5 mM Aspergillus flavus

Application

EC Number Application Comment Organism
3.2.1.3 food industry glucoamylase is an important group of enzymes in starch processing in the food industries, as it is used for the production of glucose and fructose syrup from liquefied starch Aspergillus flavus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.3 gene GAA, DNA and amino acid sequence determination and analysis, phylogenic tree, the N-terminal 17 amino acids are presumed to be a signal peptide, recombinant methanol-induced expression of FLAG-tagged enzyme in Pichia pastoris strain GS115 Aspergillus flavus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.3 Cu2+ activates at above 1 mM, inhibits at above 5 mM Aspergillus flavus
3.2.1.3 Na+ at above 5 mM Aspergillus flavus
3.2.1.3 Pb2+ activates at above 1 mM, inhibits at above 5 mM Aspergillus flavus
3.2.1.3 Zn2+ activates at above 1 mM, inhibits at above 5 mM Aspergillus flavus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.3 additional information the N-terminal 17 amino acids are presumed to be a signal peptide Aspergillus flavus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.3 additional information metal ions, such as Na+, K+, Ca2+ and Cd2+, have no significant effect on the recombinant glucoamylase activity at concentration of 1 mM Aspergillus flavus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.3 additional information Aspergillus flavus glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme ?
-
?
3.2.1.3 additional information Aspergillus flavus NSH9 glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme ?
-
?
3.2.1.3 starch + H2O Aspergillus flavus
-
?
-
?
3.2.1.3 starch + H2O Aspergillus flavus NSH9
-
?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.3 Aspergillus flavus A0A166HLT6
-
-
3.2.1.3 Aspergillus flavus NSH9 A0A166HLT6
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.3 amylopectin
-
Aspergillus flavus ?
-
?
3.2.1.3 amylopectin
-
Aspergillus flavus NSH9 ?
-
?
3.2.1.3 glycogen + H2O lower activity Aspergillus flavus ?
-
?
3.2.1.3 glycogen + H2O lower activity Aspergillus flavus NSH9 ?
-
?
3.2.1.3 additional information glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme Aspergillus flavus ?
-
?
3.2.1.3 additional information glucoamylase is an exo-acting enzyme that yields beta-D-glucose from the nonreducing ends of starch and related oligo- and polysaccharide chains by hydrolyzing alpha-1,4 and alpha-1,6 linkages. The enzyme is able to completely hydrolyze starch if incubated for extended periods of time and hence called the saccharifying enzyme Aspergillus flavus NSH9 ?
-
?
3.2.1.3 starch + H2O
-
Aspergillus flavus ?
-
?
3.2.1.3 starch + H2O best substrate, soluble starch and gelatinized raw sago starch Aspergillus flavus ?
-
?
3.2.1.3 starch + H2O
-
Aspergillus flavus NSH9 ?
-
?
3.2.1.3 starch + H2O best substrate, soluble starch and gelatinized raw sago starch Aspergillus flavus NSH9 ?
-
?

Subunits

EC Number Subunits Comment Organism
3.2.1.3 ? x * 78000, recombinant enzyme, SDS-PAGE, x * 55100, about, recombinant enzyme, sequence calculation Aspergillus flavus
3.2.1.3 More the enzyme from Aspergillus flavus strain NSH9 contains no starch binding domain (SBD) Aspergillus flavus

Synonyms

EC Number Synonyms Comment Organism
3.2.1.3 1,4-alpha-D-glucan glucohydrolase
-
Aspergillus flavus
3.2.1.3 glucoamylase
-
Aspergillus flavus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.3 70
-
recombinant enzyme Aspergillus flavus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.3 3.5 8 activity range, profile overview Aspergillus flavus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.3 60
-
purified recombinant enzyme, pH 5.0, stable for 15 min, loss of 20% activity after 30 min, and of 50% after 45 min, 12% activity remains after 90 min, inactivation after 120 min Aspergillus flavus
3.2.1.3 80
-
purified recombinant enzyme, pH 5.0, loss of 8% activity after 15 min, loss of 20% activity after 30 min, and of 75% after 45 min, 3% activity remains after 75 min, inactivation after 90 min Aspergillus flavus
3.2.1.3 90
-
purified recombinant enzyme, pH 5.0, loss of 12% activity after 15 min, loss of 75% activity after 30 min, and of 85% after 45 min, inactivation after 75 min Aspergillus flavus
3.2.1.3 100
-
purified recombinant enzyme, pH 5.0, loss of 43% activity after 15 min, loss of 80% activity after 30 min, and of 88% after 45 min, inactivation after 60 min Aspergillus flavus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.3 5
-
recombinant enzyme Aspergillus flavus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.3 3.5 8 activity range, profile overview Aspergillus flavus

General Information

EC Number General Information Comment Organism
3.2.1.3 additional information the thermostable glucoamylase from Aspergillus flavus strain NSH9 contains no starch binding domain (SBD) Aspergillus flavus