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Literature summary extracted from
- Amyloglucosidase enzymatic reactivity inside lipid vesicles (2007), J. Biol. Eng., 1:4, no pp. given.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | synthesis | entrapment of amyloglucosidase into dipalmitoylphosphatidylcholine multilamellar vesicles and large unilamellar vesicles for biocatalysis inside liposomes and bioanalytical applications, overview | Aspergillus niger |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | additional information | entrapment of amyloglucosidase into dipalmitoylphosphatidylcholine multilamellar vesicles and large unilamellar vesicles, vesicle formation, method optimization, enzyme activity is very stable during the first three batch runs, overview | Aspergillus niger |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.3 | additional information | product inhibition, kinetics | Aspergillus niger |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.3 | additional information | - |
additional information | kinetics of starch hydrolysis by AMG modeled for two different systems, free enzyme in aqueous solution and entrapped enzyme within vesicles in aqueous suspension, overview, Michaelis-Menten kinetic model with product inhibition for intrinsic kinetics | Aspergillus niger | |
| 3.2.1.3 | 1.15 | - |
starch | pH 4.5, 55°C, multilamellar liposome-entrapped enzyme | Aspergillus niger |  |
| 3.2.1.3 | 1.55 | - |
starch | pH 4.5, 55°C, free soluble enzyme | Aspergillus niger | |
| 3.2.1.3 | 1.64 | - |
starch | pH 4.5, 55°C, large unilamellar liposome-entrapped enzyme | Aspergillus niger | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.2.1.3 | additional information | liposome | Aspergillus niger | - |
- |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.3 | starch + H2O | Aspergillus niger | - |
? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.3 | Aspergillus niger | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.2.1.3 | commercial preparation | - |
Aspergillus niger | - |
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 | 5.76 | 8.86 | liposome-entrapped enzyme | Aspergillus niger |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.3 | starch + H2O | - |
Aspergillus niger | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | amyloglucosidase | - |
Aspergillus niger |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 55 | - |
assay at | Aspergillus niger |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 50 | - |
pH 5.0, soluble enzyme half-life: 160 h, liposome-entrapped enzyme shows full activity after 180 h | Aspergillus niger |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 4.5 | - |
assay at | Aspergillus niger |
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