EC Number | General Stability | Organism |
---|---|---|
3.2.1.3 | denaturation and renaturation does not seem to offer an economical approach to improve the usage time of immobilized enzyme | Aspergillus niger |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.2.1.3 | 0.13 | - |
maltopentaose | free enzyme | Aspergillus niger | |
3.2.1.3 | 0.15 | - |
maltoheptaose | immobilized enzyme | Aspergillus niger |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.3 | Aspergillus niger | - |
glucoamylase II | - |
EC Number | Renatured (Comment) | Organism |
---|---|---|
3.2.1.3 | optimal renaturation | Aspergillus niger |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.2.1.3 | additional information | - |
- |
Aspergillus niger |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.3 | maltoheptaose + H2O | - |
Aspergillus niger | ? | - |
? | |
3.2.1.3 | maltopentaose + H2O | - |
Aspergillus niger | ? | - |
? | |
3.2.1.3 | starch + H2O | - |
Aspergillus niger | glucose + ? | - |
? |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.3 | 60 | - |
pH 4.5, 5 min, stable up to | Aspergillus niger |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.3 | 4.5 | - |
free and immobilized enzyme | Aspergillus niger |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
3.2.1.3 | 2 | 7 | pH 2.0: about 55% of maximal activity, pH 7.0: about 25% of maximal activity, free and immobilized enzyme | Aspergillus niger |