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Literature summary for 3.2.1.3 extracted from

  • Kovalenko, G.A.; Perminova, L.V.; Terenteva, T.G.; Plaksin, G.V.
    Catalytic properties of glucoamylase immobilized on synthetic carbon material Sibunit (2007), Appl. Biochem. Microbiol., 43, 374-378.
No PubMed abstract available
Search for more literature for 3.2.1.3

Application

Application Comment Organism
biotechnology the enzyme from commercial preparation is immobilized by sorption on a carbon support Sibunit, starch and dextrin hydrolysis kinetic parameters of glucoamylase, including the rate constant of thermal inactivation, show that immobilization of the enzyme results in a 1000fold increase in enzyme stability in comparison to the dissolved enzyme, presence of the dextrin substrate has a stabilizing effect, increase in dextrin concentration to 53% increases the thermostability of the immobilized enzyme, the immobilized-enzyme biocatalyst for starch saccharification has a high operational stability, half-inactivation time at 60°C exceeds 30 days Aspergillus awamori

Protein Variants

Protein Variants Comment Organism
additional information the enzyme from commercial preparation is immobilized by sorption on a carbon support Sibunit, starch and dextrin hydrolysis kinetic parameters of glucoamylase, including the rate constant of thermal inactivation, show that immobilization of the enzyme results in a 1000fold increase in enzyme stability in comparison to the dissolved enzyme, presence of the dextrin substrate has a stabilizing effect, increase in dextrin concentration to 53% increases the thermostability of the immobilized enzyme, the immobilized-enzyme biocatalyst for starch saccharification has a high operational stability, half-inactivation time at 60°C exceeds 30 days, method optimization, overview Aspergillus awamori

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dextrin + 6 H2O Aspergillus awamori the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules 7 D-glucose
-
 ?
starch + H2O Aspergillus awamori the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules D-glucose + ?
-
 ?

Organism

Organism UniProt Comment Textmining
Aspergillus awamori
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Aspergillus awamori

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Aspergillus awamori
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
200
-
 purified commercial preparation Aspergillus awamori

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dextrin + 6 H2O the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules Aspergillus awamori 7 D-glucose
-
 ?
dextrin + 6 H2O potato dextrin, the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules Aspergillus awamori 7 D-glucose
-
 ?
starch + H2O the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules Aspergillus awamori D-glucose + ?
-
 ?

Synonyms

Synonyms Comment Organism
exo-1,4-alpha-glucosidase
-
 Aspergillus awamori
glucoamylase
-
 Aspergillus awamori

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
 Aspergillus awamori

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 80
-
 Aspergillus awamori

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.6
-
-
 Aspergillus awamori