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Literature summary for 3.2.1.41 extracted from
- A GH57 family amylopullulanase from deep-sea Thermococcus siculi: expression of the gene and characterization of the recombinant enzyme (2011), Curr. Microbiol., 62, 222-228.
Application
| Application | Comment | Organism |
|---|---|---|
| industry | the acidic thermoactive amylopullulanase-MalE fusion protein and the hydrolytic domain of the amylopullulanase can be employed for industrial saccharification of starch | Thermococcus siculi |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21(DE3) cells | Thermococcus siculi |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Thermococcus siculi | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 148600 | - |
x * 148600, calculated from amino acid sequence | Thermococcus siculi |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermococcus siculi | B6SED6 | - |
- |
| Thermococcus siculi HJ21 | B6SED6 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| ammonium sulfate precipitation, DEAE-52 column chromatography, TSK G2000 SWXL column chromatography, and Sephadex G-100 gel filtration | Thermococcus siculi |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | amylopullulanases (type II pullulanases) are able to degrade both the alpha-1,6 and alpha-1,4 glucosidic bonds of starch | Thermococcus siculi | ? | - |
? |  |
| additional information | amylopullulanases (type II pullulanases) are able to degrade both the alpha-1,6 and alpha-1,4 glucosidic bonds of starch | Thermococcus siculi HJ21 | ? | - |
? | |
| pullulan + H2O | - |
Thermococcus siculi | ? | - |
? | |
| pullulan + H2O | - |
Thermococcus siculi HJ21 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 148600, calculated from amino acid sequence | Thermococcus siculi |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| amylopullulanase | - |
Thermococcus siculi |
| Apu | - |
Thermococcus siculi |
| pullulan-6-glucanohydrolase | - |
Thermococcus siculi |
| type II pullulanase | - |
Thermococcus siculi |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 95 | - |
temperature optimum for both amylase and pullulanase activities | Thermococcus siculi |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | 110 | the pullulanase shows 96%, 91%, 70%, and 50% of the maximum activity at 80, 90, 100 and 110°C, respectively. The residual total activities of the amylopullulanase-MalE fusion protein and the hydrolytic domain of the amylopullulanase are both 89% after incubation at 100°C for 1 h | Thermococcus siculi |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
optimum pH for amylase activity | Thermococcus siculi |
| 6 | - |
optimum pH for pullulanase activity | Thermococcus siculi |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 6.5 | after incubation at 95°C for 4 h in a pH range from 5.0 to 6.5, the residual pullulanase and amylase activities of the enzyme are above 90% of the maximum activity | Thermococcus siculi |
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