EC Number | Application | Comment | Organism |
---|---|---|---|
3.2.1.3 | 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 |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.2.1.3 | 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 |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.3 | dextrin + 6 H2O | Aspergillus awamori | the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules | 7 D-glucose | - |
? | |
3.2.1.3 | starch + H2O | Aspergillus awamori | the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules | D-glucose + ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.3 | Aspergillus awamori | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.1.3 | - |
Aspergillus awamori |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.2.1.3 | commercial preparation | - |
Aspergillus awamori | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.2.1.3 | 200 | - |
purified commercial preparation | Aspergillus awamori |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.3 | dextrin + 6 H2O | the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules | Aspergillus awamori | 7 D-glucose | - |
? | |
3.2.1.3 | 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 | - |
? | |
3.2.1.3 | starch + H2O | the enzyme performs hydrolytic cleavage of terminal alpha-glycosyl residues from starch and dextrin molecules | Aspergillus awamori | D-glucose + ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.3 | exo-1,4-alpha-glucosidase | - |
Aspergillus awamori |
3.2.1.3 | glucoamylase | - |
Aspergillus awamori |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.3 | 50 | - |
- |
Aspergillus awamori |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.3 | 25 | 80 | - |
Aspergillus awamori |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.3 | 4.6 | - |
- |
Aspergillus awamori |