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Literature summary for 3.2.1.3 extracted from
- Purification, characterization, and substrate specificity of a glucoamylase with steroidal saponin-rhamnosidase activity from Curvularia lunata (2007), Appl. Microbiol. Biotechnol., 76, 1329-1338.
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | the enzyme is industrially an important biocatalyst that decomposes starch into glucose by tearing-off alpha-1,4-linked glucose residue from the non-reduced end of the polysaccharide chain | Curvularia lunata |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 66000 | - |
x * 66000, SDS-PAGE | Curvularia lunata |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Curvularia lunata | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme 5.0fold by ammonium sulfate fractionation, gel filtration, and cation and anion exchange chromatography to homogeneity | Curvularia lunata |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 2.54 | - |
culture supernatant, substrate starch | Curvularia lunata |
| 19.73 | - |
purified enzyme, substrate starch | Curvularia lunata |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the glucoamylase also shows steroidal saponin-rhamnosidase activity, EC 3.2.1.40, being able to hydrolyze the terminal rhamnosyl of steroidal saponins and the sugar chain at the C-3 position of spirostanosides, the enzyme also hydrolyzed the terminal rhamnosyl residues of the sugar chain at the C-3 position while retaining the glucosyl residues at the C-26 position of furostanosides, substrate specificity, overview | Curvularia lunata | ? | - |
? |  |
| starch + H2O | soluble starch | Curvularia lunata | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 66000, SDS-PAGE | Curvularia lunata |
| More | enzyme amino acid sequence analysis by MALDI-TOF mass spectrometry | Curvularia lunata |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 1,4-alpha-D-glucan glucohydrolase | - |
Curvularia lunata |
| glucoamylase | - |
Curvularia lunata |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
- |
Curvularia lunata |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 70 | - |
Curvularia lunata |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | - |
purified enzyme, 30-40% remaining activity | Curvularia lunata |
| 30 | - |
purified enzyme, stable | Curvularia lunata |
| 30 | 40 | purified enzyme, 80% of maximal activity within this range | Curvularia lunata |
| 50 | - |
purified enzyme, 70% remaining activity | Curvularia lunata |
| 70 | - |
purified enzyme, 30-40% remaining activity | Curvularia lunata |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 4 | - |
- |
Curvularia lunata |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 3 | 8 | - |
Curvularia lunata |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 3 | - |
purified enzyme, 60% remaining activity | Curvularia lunata |
| 4 | 7 | purified enzyme, 90% of maximal activity within this range | Curvularia lunata |
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