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Literature summary for 1.1.1.47 extracted from
- Semi-continuous flow biocatalysis with affinity co-immobilized ketoreductase and glucose dehydrogenase (2020), Molecules, 25, 4278 .
Application
| Application | Comment | Organism |
|---|---|---|
| biotechnology | co-immobilization of ketoreductase (KRED) and glucose dehydrogenase (GDH) on highly cross-linked agarose (sepharose) via affnity interaction between His-tagged enzymes (six histidine residues on the N-terminus of the protein) and agarose matrix charged with nickel (Ni2+ ions). Immobilized enzymes are applied in a set of biotransformation reactions in repeated batch flow-reactor mode. Immobilization reduces the requirement for cofactor (NADP+) and allows the use of higher substrate concentration in comparison with free enzymes | Priestia megaterium |
| synthesis | co-immobilization of ketoreductase (KRED) and glucose dehydrogenase (GDH) on highly cross-linked agarose (sepharose) via affnity interaction between His-tagged enzymes (six histidine residues on the N-terminus of the protein) and agarose matrix charged with nickel (Ni2+ ions). Immobilized enzymes are applied in a set of biotransformation reactions in repeated batch flow-reactor mode. Immobilization reduces the requirement for cofactor (NADP+) and allows the use of higher substrate concentration in comparison with free enzymes | Priestia megaterium |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli BL21(DE3) with a combined lac and T7 promoter | Priestia megaterium |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Priestia megaterium | - |
- |
- |
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