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Literature summary for 2.4.1.1 extracted from
- Physiological aggregation of maltodextrin phosphorylase from Pyrococcus furiosus and its application in a process of batch starch degradation to alpha-D-glucose-1-phosphate (2008), J. Ind. Microbiol. Biotechnol., 35, 219-223.
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | maltodextrin phosphorylase from Pyrococcus furiosus is fused with the cellulose-binding domain of Clostridium cellulovorans serving as an aggregation module. After molecular cloning of the corresponding gene fusion construct and controlled expression in Escherichia coli BL21, 83% of total maltodextrin phosphorylase activity is displayed in active inclusion bodies. These active inclusion bodies are easily isolated by nonionic detergent treatment and directly used for maltodextrin conversion to alpha-D-glucose-1-phosphate in a repetitive batch mode. Only 10% of enzyme activity is lost after ten conversion cycles at optimum conditions | Pyrococcus furiosus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| maltodextrin phosphorylase from Pyrococcus furiosus is fused with the cellulose-binding domain of Clostridium cellulovorans serving as an aggregation module. After molecular cloning of the corresponding gene fusion construct and controlled expression in Escherichia coli BL21, 83% of total maltodextrin phosphorylase activity is displayed in active inclusion bodies | Pyrococcus furiosus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus furiosus | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| maltodextrin phosphorylase | - |
Pyrococcus furiosus |
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