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Literature summary for 1.1.3.21 extracted from
- Co-immobilization of lipase, glycerol kinase, glycerol-3-phosphate oxidase and peroxidase onto alkylamine glass beads through glutaraldehyde coupling (2002), Indian J. Biochem. Biophys., 39, 342-346.
General Stability
| General Stability | Organism |
|---|---|
| enzyme coimmobilized with lipase, glycerol kinase and peroxidase onto glutaraldehyde onto glutaraldehyde activated alkylamine glass beads is active even after regulate use for 6 months when stored at 4°C in distilled water. Immobilized enzyme possess higher pH and thermal and storage stability than soluble enzyme | Aerococcus viridans |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aerococcus viridans | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| sn-glycerol-3-phosphate + O2 | - |
Aerococcus viridans | glycerone phosphate + H2O2 | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GPO | - |
Aerococcus viridans |
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Release 2023.1 (January 2023)
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