General Stability | Organism |
---|---|
the enzyme in phosphate buffer pressurized with CO2 up to 9 MPa for 1 h at 35°C loses most of its activity. Although the residual activity is higher in MES buffer than in phosphate buffer, deactivation cannot be prevented. With 0.7 M glycerol, the residual activity is double that without additives, and with 1-1.2 M trehalose, the residual activity is 1.5times that without additives. The stability of the enzyme is improved dramatically by immobilization onto the ion-exchange polymer Mukouyama 2000, the biocatalytic activity is fully retained even after treatment at 11 MPa. The stability of the enzyme immobilized on Toyonite-200 is lower than that of free enzyme | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate | - |
Saccharomyces cerevisiae | acetaldehyde + CO2 | - |
r |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
thiamine diphosphate | - |
Saccharomyces cerevisiae |